PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 11478406-5 2001 RESULTS: PMA promoted a marked transient translocation of ventricular PKCalpha from the cytosol to the membranes within 10 minutes in lean rats, whereas it had a much weaker effect in obese rats. Tetradecanoylphorbol Acetate 9-12 protein kinase C, alpha Rattus norvegicus 70-78 11494368-5 2001 A PKC activator, phorbol-12-myristate-13-acetate, enhanced the secretion of BDNF. Tetradecanoylphorbol Acetate 17-48 protein kinase C, alpha Rattus norvegicus 2-5 11435343-4 2001 Methods and Results-PKC was downregulated by prolonged (24-hour) treatment with phorbol 12-myristate 13-acetate (4 microgram/kg body weight) before subsequent experiments in rats. Tetradecanoylphorbol Acetate 80-111 protein kinase C, alpha Rattus norvegicus 20-23 11699875-8 2001 The PKC inhibitor, Go6976, which only inhibits conventional PKCalpha and _, suppressed TPA-induced glucose uptake, but suppressed insulin-induced glucose uptake to only a small extent. Tetradecanoylphorbol Acetate 87-90 protein kinase C, alpha Rattus norvegicus 4-7 11301042-3 2001 The current study further investigates the signaling pathways activated by BisA by comparing its effects with those of the PKC agonist phorbol 12-myristate 13-acetate (PMA) in the IEC-18 intestinal crypt cell line. Tetradecanoylphorbol Acetate 135-166 protein kinase C, alpha Rattus norvegicus 123-126 11301042-3 2001 The current study further investigates the signaling pathways activated by BisA by comparing its effects with those of the PKC agonist phorbol 12-myristate 13-acetate (PMA) in the IEC-18 intestinal crypt cell line. Tetradecanoylphorbol Acetate 168-171 protein kinase C, alpha Rattus norvegicus 123-126 11301042-10 2001 On the other hand, BisA and PMA both promoted PKC-dependent activation of Erk 1 and 2 in this system. Tetradecanoylphorbol Acetate 28-31 protein kinase C, alpha Rattus norvegicus 46-49 11699875-9 2001 On the other hand, the PKC inhibitor, RO32-0432, which inhibits conventional, novel, and atypical PKCs, markedly suppressed both insulin- and TPA-induced glucose uptake. Tetradecanoylphorbol Acetate 142-145 protein kinase C, alpha Rattus norvegicus 23-26 10790161-6 2000 The protein kinase C (PKC) activator 4beta-phorbol 12-myristate 13-acetate (PMA, 100 pM to 200 nM), also stimulated Ca2+ spiking and this effect was additive with a submaximal concentration of AVP (50 pM). Tetradecanoylphorbol Acetate 37-74 protein kinase C, alpha Rattus norvegicus 22-25 11181442-5 2001 Thus, total PKC activity does not indicate absolute sensitivity of a cell system to TPA-induced suppression of communication, but within a certain cell system increasing PKC activity may enhance the sensitivity to TPA in this respect. Tetradecanoylphorbol Acetate 214-217 protein kinase C, alpha Rattus norvegicus 170-173 11181442-9 2001 Long-term treatment with TPA caused strong down-regulation of PKC alpha, delta and epsilon, but little down-regulation of PKC mu. Tetradecanoylphorbol Acetate 25-28 protein kinase C, alpha Rattus norvegicus 62-90 11208899-2 2001 Ro31-8220, a PKC inhibitor, reduced TPA-stimulated release of choline- and ethanolamine-metabolites to basal levels. Tetradecanoylphorbol Acetate 36-39 protein kinase C, alpha Rattus norvegicus 13-16 11208899-7 2001 Exposure of bipolar undifferentiated CG-4 line cells to TPA resulted in down-regulatation of PKC-alpha and PKC-beta which could not be detected by Western blotting after a few hours; PKC-epsilon was down-regulated much more slowly but PKCs delta, zeta and iota were not influenced by 48 h exposure of cells to TPA. Tetradecanoylphorbol Acetate 56-59 protein kinase C, alpha Rattus norvegicus 93-102 11113454-5 2000 Activation of PKC by both TeTx and TPA results in a loss of transport capacity and serotonin transporter (SERT) phosphorylation, which are abolished by coapplication of the specific PKC inhibitor bisindolylmaleimide-1. Tetradecanoylphorbol Acetate 35-38 protein kinase C, alpha Rattus norvegicus 14-17 10996858-4 2000 Furthermore, the ability to translocate was present in young animals after a short treatment with the phorbol ester 12-O-tetradecanoyl phorbol 13-acetate (TPA; 100 nM) or dioctanoyl-glycerol (50 microM), whereas the ability was absent in aged rats, suggesting that PKC function was impaired with aging independent of agonist stimulation. Tetradecanoylphorbol Acetate 155-158 protein kinase C, alpha Rattus norvegicus 265-268 10889170-10 2000 Phorbol myristate acetate and phenylephrine triggered translocation of PKC-alpha and PKC-delta isoforms from the cytosol to the membrane in control aortas; in cirrhotic aortas, only PKC-alpha was translocated. Tetradecanoylphorbol Acetate 0-25 protein kinase C, alpha Rattus norvegicus 71-80 10889170-10 2000 Phorbol myristate acetate and phenylephrine triggered translocation of PKC-alpha and PKC-delta isoforms from the cytosol to the membrane in control aortas; in cirrhotic aortas, only PKC-alpha was translocated. Tetradecanoylphorbol Acetate 0-25 protein kinase C, alpha Rattus norvegicus 182-191 11095914-8 2000 Activation of classical and novel PKC isozymes by phorbol 12-myristate 13-acetate and phorbol 12,13-dibutyrate stimulated goblet cell glycoprotein secretion. Tetradecanoylphorbol Acetate 50-81 protein kinase C, alpha Rattus norvegicus 34-37 10968651-4 2000 RESULTS: In control rat myocytes, pretreatment with phorbol 12-myristate 13-acetate (PMA), an activator of protein kinase C (PKC), reduced the rate of Mn2+ quench to 68% of the untreated cell response. Tetradecanoylphorbol Acetate 52-83 protein kinase C, alpha Rattus norvegicus 125-128 10968651-4 2000 RESULTS: In control rat myocytes, pretreatment with phorbol 12-myristate 13-acetate (PMA), an activator of protein kinase C (PKC), reduced the rate of Mn2+ quench to 68% of the untreated cell response. Tetradecanoylphorbol Acetate 85-88 protein kinase C, alpha Rattus norvegicus 125-128 10790161-6 2000 The protein kinase C (PKC) activator 4beta-phorbol 12-myristate 13-acetate (PMA, 100 pM to 200 nM), also stimulated Ca2+ spiking and this effect was additive with a submaximal concentration of AVP (50 pM). Tetradecanoylphorbol Acetate 76-79 protein kinase C, alpha Rattus norvegicus 22-25 10790161-10 2000 Pretreatment for 24 h with 1 microM PMA downregulated expression of PKC-alpha and -delta, but not PKC-epsilon, and prevented the Ca2+-spiking responses to either 1 nM PMA or 100 pM AVP. Tetradecanoylphorbol Acetate 36-39 protein kinase C, alpha Rattus norvegicus 68-88 10571249-4 1999 An 8-hr pretreatment with PMA, which led to down-regulation of PKC-alpha and -delta isoenzymes, still inhibited sPLA2-IIA induction. Tetradecanoylphorbol Acetate 26-29 protein kinase C, alpha Rattus norvegicus 63-83 10659998-5 1999 Prior treatment of VSMCs with staurosporine (1 microM), a PKC inhibitor, inhibited the ability of PMA to attenuate BK-induced responses, suggesting that the inhibitory effect of PMA is mediated through the activation of PKC. Tetradecanoylphorbol Acetate 98-101 protein kinase C, alpha Rattus norvegicus 58-61 10659998-5 1999 Prior treatment of VSMCs with staurosporine (1 microM), a PKC inhibitor, inhibited the ability of PMA to attenuate BK-induced responses, suggesting that the inhibitory effect of PMA is mediated through the activation of PKC. Tetradecanoylphorbol Acetate 98-101 protein kinase C, alpha Rattus norvegicus 220-223 10578141-9 1999 4 The extent of cellular damage in response to addition of SNAP to the incubation medium was enhanced by coincubation with the PKC activator, phorbol 12-myristate 13-acetate (PMA; 1 and 10 microM). Tetradecanoylphorbol Acetate 142-173 protein kinase C, alpha Rattus norvegicus 127-130 10578141-9 1999 4 The extent of cellular damage in response to addition of SNAP to the incubation medium was enhanced by coincubation with the PKC activator, phorbol 12-myristate 13-acetate (PMA; 1 and 10 microM). Tetradecanoylphorbol Acetate 175-178 protein kinase C, alpha Rattus norvegicus 127-130 10512355-5 1999 We identified and determined the glucose transporters and PKC isoforms affected by insulin and 12-O-tetradecanoylphorbol-13-acetate (TPA). Tetradecanoylphorbol Acetate 95-131 protein kinase C, alpha Rattus norvegicus 58-61 10512355-5 1999 We identified and determined the glucose transporters and PKC isoforms affected by insulin and 12-O-tetradecanoylphorbol-13-acetate (TPA). Tetradecanoylphorbol Acetate 133-136 protein kinase C, alpha Rattus norvegicus 58-61 10512355-10 1999 TPA translocated and activated PKC-alpha, -beta2, and -delta; these effects were not noticeably affected by PI3K inhibitors. Tetradecanoylphorbol Acetate 0-3 protein kinase C, alpha Rattus norvegicus 31-40 10208993-3 1999 Incubation with the phorbol ester 12-O-tetradecanoylphorbol-13-acetate (TPA; 10(-7) M) was associated with a transient induction in both cell fractions of calcium/phosphatidylserine-dependent PKC activity, which was elevated from 15 min to 1 h. Consistent with this, mRNAs for the calcium/phospholipid-dependent isomeric forms of PKC (alpha, beta, and gamma) were detected. Tetradecanoylphorbol Acetate 34-70 protein kinase C, alpha Rattus norvegicus 192-195 10629861-5 1999 Short-time (10-20 min) treatment with phorbol 12-myristate 13-acetate (PMA) induced translocation of PKC alpha from cytosolic to particulate fraction. Tetradecanoylphorbol Acetate 38-69 protein kinase C, alpha Rattus norvegicus 101-110 10629861-5 1999 Short-time (10-20 min) treatment with phorbol 12-myristate 13-acetate (PMA) induced translocation of PKC alpha from cytosolic to particulate fraction. Tetradecanoylphorbol Acetate 71-74 protein kinase C, alpha Rattus norvegicus 101-110 10629861-6 1999 PKC alpha was completely downregulated by treatment with 100 nM PMA for 24 hours. Tetradecanoylphorbol Acetate 64-67 protein kinase C, alpha Rattus norvegicus 0-9 10444518-5 1999 We examined the PKC isomers that are translocated by ATP, UTP, TPA, and dioctanoylglycerol in cultured type II cells isolated from adult rats. Tetradecanoylphorbol Acetate 63-66 protein kinase C, alpha Rattus norvegicus 16-19 10444518-8 1999 TPA and dioctanoylglycerol also activated PKC-alpha, -betaI, -betaII, -delta, and -eta, but those isoforms were not activated by ATP or UTP. Tetradecanoylphorbol Acetate 0-3 protein kinase C, alpha Rattus norvegicus 42-86 10444518-2 1999 Such agents include 12-O-tetradecanoylphorbol 13-acetate (TPA) and cell-permeable diacylglycerols that directly activate PKC. Tetradecanoylphorbol Acetate 20-56 protein kinase C, alpha Rattus norvegicus 121-124 10208993-3 1999 Incubation with the phorbol ester 12-O-tetradecanoylphorbol-13-acetate (TPA; 10(-7) M) was associated with a transient induction in both cell fractions of calcium/phosphatidylserine-dependent PKC activity, which was elevated from 15 min to 1 h. Consistent with this, mRNAs for the calcium/phospholipid-dependent isomeric forms of PKC (alpha, beta, and gamma) were detected. Tetradecanoylphorbol Acetate 34-70 protein kinase C, alpha Rattus norvegicus 330-357 10208993-3 1999 Incubation with the phorbol ester 12-O-tetradecanoylphorbol-13-acetate (TPA; 10(-7) M) was associated with a transient induction in both cell fractions of calcium/phosphatidylserine-dependent PKC activity, which was elevated from 15 min to 1 h. Consistent with this, mRNAs for the calcium/phospholipid-dependent isomeric forms of PKC (alpha, beta, and gamma) were detected. Tetradecanoylphorbol Acetate 72-75 protein kinase C, alpha Rattus norvegicus 192-195 10208993-3 1999 Incubation with the phorbol ester 12-O-tetradecanoylphorbol-13-acetate (TPA; 10(-7) M) was associated with a transient induction in both cell fractions of calcium/phosphatidylserine-dependent PKC activity, which was elevated from 15 min to 1 h. Consistent with this, mRNAs for the calcium/phospholipid-dependent isomeric forms of PKC (alpha, beta, and gamma) were detected. Tetradecanoylphorbol Acetate 72-75 protein kinase C, alpha Rattus norvegicus 330-357 10208993-4 1999 The expression levels of mRNAs for PKCalpha and PKCbeta were also up-regulated (2.5- to 3-fold) by TPA (10(-7) M), but these effects were much slower (peaking after 12 h) than those on phosphotransferase activity. Tetradecanoylphorbol Acetate 99-102 protein kinase C, alpha Rattus norvegicus 35-43 10208993-5 1999 In the presence of TPA (10(-7) M), expression of androgen receptor (AR) mRNA showed a transient time-dependent down-regulation ( approximately 70%), in which the nadir was reached after 6 h and baseline expression was again obtained after 12 h. The regulatory effect of PKC activation on AR mRNA was confirmed by the absence of response to a biologically inactive phorbol ester. Tetradecanoylphorbol Acetate 19-22 protein kinase C, alpha Rattus norvegicus 270-273 10098498-6 1999 The Ca2+ ionophore, A23187 or ionomycin, mimicked the effect of AVP, whereas the protein kinase C (PKC) activator, TPA, only induced a slight increase in AA release. Tetradecanoylphorbol Acetate 115-118 protein kinase C, alpha Rattus norvegicus 99-102 10411311-7 1999 Overnight treatment with 4beta-phorbol 12-myristate 13-acetate, an activator of PKC, down-regulated PKC alpha, delta, and epsilon, but not PKC zeta. Tetradecanoylphorbol Acetate 25-62 protein kinase C, alpha Rattus norvegicus 100-129 10411311-7 1999 Overnight treatment with 4beta-phorbol 12-myristate 13-acetate, an activator of PKC, down-regulated PKC alpha, delta, and epsilon, but not PKC zeta. Tetradecanoylphorbol Acetate 25-62 protein kinase C, alpha Rattus norvegicus 80-83 10188728-1 1999 Treatment with low (nanomolar) concentrations of phorbol-12-myristate-13-acetate (PMA) for 5 to 30 min suppresses locomotion of Walker 256 carcinosarcoma cells, suggesting that activation of protein kinase C (PKC) is a stop signal for tumor cell locomotion. Tetradecanoylphorbol Acetate 49-80 protein kinase C, alpha Rattus norvegicus 209-212 10188728-1 1999 Treatment with low (nanomolar) concentrations of phorbol-12-myristate-13-acetate (PMA) for 5 to 30 min suppresses locomotion of Walker 256 carcinosarcoma cells, suggesting that activation of protein kinase C (PKC) is a stop signal for tumor cell locomotion. Tetradecanoylphorbol Acetate 82-85 protein kinase C, alpha Rattus norvegicus 209-212 10188728-5 1999 Long-term incubation with PMA (0.1 microM, 6 hr) resulted in significant reduction of expression of conventional PKCs alpha, betaI, betaII and gamma and of the novel PKC eta to 10% to 26% of controls. Tetradecanoylphorbol Acetate 26-29 protein kinase C, alpha Rattus norvegicus 113-148 10188728-5 1999 Long-term incubation with PMA (0.1 microM, 6 hr) resulted in significant reduction of expression of conventional PKCs alpha, betaI, betaII and gamma and of the novel PKC eta to 10% to 26% of controls. Tetradecanoylphorbol Acetate 26-29 protein kinase C, alpha Rattus norvegicus 113-116 10188728-9 1999 Motility and polarized shape of the down-regulated cells were no longer susceptible to short-term treatment with PMA, showing that active PKC is indeed responsible for the inhibitory effects of PMA. Tetradecanoylphorbol Acetate 113-116 protein kinase C, alpha Rattus norvegicus 138-141 10188728-9 1999 Motility and polarized shape of the down-regulated cells were no longer susceptible to short-term treatment with PMA, showing that active PKC is indeed responsible for the inhibitory effects of PMA. Tetradecanoylphorbol Acetate 194-197 protein kinase C, alpha Rattus norvegicus 138-141 10098498-9 1999 Western blots demonstrated expression of PKCalpha, betaI, epsilon, delta, and zeta in H9c2 cells; PKC inhibitors (staurosporine or Ro 31-8220) or down-regulation of PKCalpha, betaI, epsilon, and delta by long-term (24 h) TPA treatment caused a partial blockade of the AVP-induced response, whereas the A23187-induced AA release was unaffected by down-regulation of these isoforms. Tetradecanoylphorbol Acetate 221-224 protein kinase C, alpha Rattus norvegicus 41-82 10098498-9 1999 Western blots demonstrated expression of PKCalpha, betaI, epsilon, delta, and zeta in H9c2 cells; PKC inhibitors (staurosporine or Ro 31-8220) or down-regulation of PKCalpha, betaI, epsilon, and delta by long-term (24 h) TPA treatment caused a partial blockade of the AVP-induced response, whereas the A23187-induced AA release was unaffected by down-regulation of these isoforms. Tetradecanoylphorbol Acetate 221-224 protein kinase C, alpha Rattus norvegicus 41-44 10098498-9 1999 Western blots demonstrated expression of PKCalpha, betaI, epsilon, delta, and zeta in H9c2 cells; PKC inhibitors (staurosporine or Ro 31-8220) or down-regulation of PKCalpha, betaI, epsilon, and delta by long-term (24 h) TPA treatment caused a partial blockade of the AVP-induced response, whereas the A23187-induced AA release was unaffected by down-regulation of these isoforms. Tetradecanoylphorbol Acetate 221-224 protein kinase C, alpha Rattus norvegicus 165-200 10098498-12 1999 AVP- or TPA-induced activation and tyrosine phosphorylation of p42 MAPK were completely blocked by down-regulation of PKCalpha, betaI, epsilon, and delta, but still occurred, together with the cytosolic PLA2 mobility shift, in the absence of external Ca2+. Tetradecanoylphorbol Acetate 8-11 protein kinase C, alpha Rattus norvegicus 118-153 10090765-2 1999 Previously we have demonstrated that protein kinase Calpha (PKCalpha) directly interacts with phospholipase D1 (PLD1), activating the enzymatic activity of PLD1 in the presence of phorbol 12-myristate 13-acetate (PMA) [Lee, T. G., et al. Tetradecanoylphorbol Acetate 180-211 protein kinase C, alpha Rattus norvegicus 37-58 10085163-14 1999 TPA treatment of 3T3-F442A adipocytes decreased PKC alpha, beta, delta, and epsilon isoforms, whereas PKC lambda, theta, zeta, micro, iota, and gamma remained unchanged or decreased minimally. Tetradecanoylphorbol Acetate 0-3 protein kinase C, alpha Rattus norvegicus 48-138 10090765-2 1999 Previously we have demonstrated that protein kinase Calpha (PKCalpha) directly interacts with phospholipase D1 (PLD1), activating the enzymatic activity of PLD1 in the presence of phorbol 12-myristate 13-acetate (PMA) [Lee, T. G., et al. Tetradecanoylphorbol Acetate 180-211 protein kinase C, alpha Rattus norvegicus 60-68 10090765-2 1999 Previously we have demonstrated that protein kinase Calpha (PKCalpha) directly interacts with phospholipase D1 (PLD1), activating the enzymatic activity of PLD1 in the presence of phorbol 12-myristate 13-acetate (PMA) [Lee, T. G., et al. Tetradecanoylphorbol Acetate 213-216 protein kinase C, alpha Rattus norvegicus 37-58 10090765-2 1999 Previously we have demonstrated that protein kinase Calpha (PKCalpha) directly interacts with phospholipase D1 (PLD1), activating the enzymatic activity of PLD1 in the presence of phorbol 12-myristate 13-acetate (PMA) [Lee, T. G., et al. Tetradecanoylphorbol Acetate 213-216 protein kinase C, alpha Rattus norvegicus 60-68 10090765-10 1999 PMA elicits translocation of PKCalpha to the CEMs, inducing PLD activation through the interaction of PKCalpha with PLD1 in the CEMs. Tetradecanoylphorbol Acetate 0-3 protein kinase C, alpha Rattus norvegicus 29-37 10090765-10 1999 PMA elicits translocation of PKCalpha to the CEMs, inducing PLD activation through the interaction of PKCalpha with PLD1 in the CEMs. Tetradecanoylphorbol Acetate 0-3 protein kinase C, alpha Rattus norvegicus 102-110 10092879-2 1999 Injection into rats of 4 beta-phorbol 12-myristate 13-acetate, a known activator of PKC, caused a rapid and marked increase in PKC activity (+325% at 10 min) in the GE fraction, along with an increase in the abundance of the PKC alpha-isoform as seen on Western immunoblots. Tetradecanoylphorbol Acetate 23-61 protein kinase C, alpha Rattus norvegicus 84-87 10094489-10 1999 The PKC isoform most translocated by TPA was PKC-delta. Tetradecanoylphorbol Acetate 37-40 protein kinase C, alpha Rattus norvegicus 4-7 10092879-2 1999 Injection into rats of 4 beta-phorbol 12-myristate 13-acetate, a known activator of PKC, caused a rapid and marked increase in PKC activity (+325% at 10 min) in the GE fraction, along with an increase in the abundance of the PKC alpha-isoform as seen on Western immunoblots. Tetradecanoylphorbol Acetate 23-61 protein kinase C, alpha Rattus norvegicus 127-130 10092879-2 1999 Injection into rats of 4 beta-phorbol 12-myristate 13-acetate, a known activator of PKC, caused a rapid and marked increase in PKC activity (+325% at 10 min) in the GE fraction, along with an increase in the abundance of the PKC alpha-isoform as seen on Western immunoblots. Tetradecanoylphorbol Acetate 23-61 protein kinase C, alpha Rattus norvegicus 225-234 10092879-5 1999 In contrast, addition of purified PKC increased (twofold) PDE activity in GE fractions from control rats but affected only slightly the activity in GE fractions from 4 beta-phorbol 12-myristate 13-acetate-treated rats. Tetradecanoylphorbol Acetate 168-204 protein kinase C, alpha Rattus norvegicus 34-37 9447980-5 1998 Consistent with the involvement of the ubiquitin-proteasome pathway in the degradation of PKC isoforms, ubiquitinated PKC alpha, delta, and epsilon were detected within 30 min of TPA treatment. Tetradecanoylphorbol Acetate 179-182 protein kinase C, alpha Rattus norvegicus 90-93 9989263-3 1999 Upon treatment with phorbol myristate acetate (PMA), PKC alpha translocated from the cytosolic fraction to the membrane fraction to which PLD1 also localized. Tetradecanoylphorbol Acetate 20-45 protein kinase C, alpha Rattus norvegicus 53-62 9989263-3 1999 Upon treatment with phorbol myristate acetate (PMA), PKC alpha translocated from the cytosolic fraction to the membrane fraction to which PLD1 also localized. Tetradecanoylphorbol Acetate 47-50 protein kinase C, alpha Rattus norvegicus 53-62 9989263-5 1999 However, most of GFP-PKC alpha was translocated from the cytosol to the plasma membrane after treatment with PMA. Tetradecanoylphorbol Acetate 109-112 protein kinase C, alpha Rattus norvegicus 21-30 9862447-4 1998 Cytokine-induced activation of neutral SMase was inhibited by stimulation of protein kinase C (PKC) by the phorbol ester TPA which caused a reduction of ceramide back to control levels. Tetradecanoylphorbol Acetate 121-124 protein kinase C, alpha Rattus norvegicus 95-98 9862447-5 1998 This inhibitory effect of TPA was reversed by the specific PKC-inhibitor Ro-318220. Tetradecanoylphorbol Acetate 26-29 protein kinase C, alpha Rattus norvegicus 59-62 9862447-6 1998 Long-term incubation (24 h) of mesangial cells with TPA, which downregulates PKC-alpha, -delta, and -epsilon isoenzymes, resulted in a recovery of IL-1beta-stimulated neutral SMase activity as well as ceramide formation. Tetradecanoylphorbol Acetate 52-55 protein kinase C, alpha Rattus norvegicus 77-108 9604867-12 1998 Prolonged treatment of the cells with TPA downregulated PKC-alpha and -beta, but not PKC-zeta. Tetradecanoylphorbol Acetate 38-41 protein kinase C, alpha Rattus norvegicus 56-75 9612227-0 1998 Chronic exposure to TPA depletes PKC alpha and augments Ca-dependent insulin secretion from cultured rat islets. Tetradecanoylphorbol Acetate 20-23 protein kinase C, alpha Rattus norvegicus 33-42 9612227-4 1998 In agreement with previous studies, culturing in TPA reduced the islet content of immunoreactive PKC alpha by > 95% and abolished the capacity of the phorbol ester to stimulate secretion during a subsequent dynamic perifusion. Tetradecanoylphorbol Acetate 49-52 protein kinase C, alpha Rattus norvegicus 97-106 9792719-8 1998 Down-regulation of PKC by prolonged treatment with 4beta-phorbol 12-myristate 13-acetate also abolished H2O2-stimulated PLD activity. Tetradecanoylphorbol Acetate 51-88 protein kinase C, alpha Rattus norvegicus 19-22 9681449-4 1998 Studies with protein kinase inhibitors and phorbol 12-myristate 13-acetate showed that protein kinase C (PKC) is activated intracellularly. Tetradecanoylphorbol Acetate 43-74 protein kinase C, alpha Rattus norvegicus 105-108 9447980-5 1998 Consistent with the involvement of the ubiquitin-proteasome pathway in the degradation of PKC isoforms, ubiquitinated PKC alpha, delta, and epsilon were detected within 30 min of TPA treatment. Tetradecanoylphorbol Acetate 179-182 protein kinase C, alpha Rattus norvegicus 118-127 9447980-7 1998 Compounds that inhibit activation of PKC prevented both TPA- and diacylglycerol-induced PKC depletion and ubiquitination. Tetradecanoylphorbol Acetate 56-59 protein kinase C, alpha Rattus norvegicus 37-40 9447980-7 1998 Compounds that inhibit activation of PKC prevented both TPA- and diacylglycerol-induced PKC depletion and ubiquitination. Tetradecanoylphorbol Acetate 56-59 protein kinase C, alpha Rattus norvegicus 88-91 9447980-8 1998 Moreover, a kinase-dead ATP-binding mutant of PKC alpha could not be depleted by TPA treatment. Tetradecanoylphorbol Acetate 81-84 protein kinase C, alpha Rattus norvegicus 46-55 9374197-6 1997 Down-regulation of PKC by prolonged (18 h) treatment with 1 microM PMA prevented the A beta-induced S6 phosphorylation. Tetradecanoylphorbol Acetate 67-70 protein kinase C, alpha Rattus norvegicus 19-22 9039136-3 1997 Angiotensin II (ANG II), endothelin-1 (ET-1), and 12-O-tetradecanoylphorbol 13-acetate (TPA) stimulated fourfold to fivefold PKC activity in PKC-alpha cDNA-transfected RTASM cells. Tetradecanoylphorbol Acetate 50-86 protein kinase C, alpha Rattus norvegicus 125-128 9295164-2 1997 We found that protein kinase C alp (PKCalpha) stimulated PLD1 activity in the presence of phorbol myristate acetate (PMA). Tetradecanoylphorbol Acetate 90-115 protein kinase C, alpha Rattus norvegicus 36-44 9295164-2 1997 We found that protein kinase C alp (PKCalpha) stimulated PLD1 activity in the presence of phorbol myristate acetate (PMA). Tetradecanoylphorbol Acetate 117-120 protein kinase C, alpha Rattus norvegicus 36-44 9075734-7 1997 Down-regulation of PKC activity by long term 12-O-tetradecanoylphorbol 13-acetate (TPA) treatment (24 h) diminished, but did not abolish, the effect of SP on VIP-stimulated cAMP production. Tetradecanoylphorbol Acetate 45-81 protein kinase C, alpha Rattus norvegicus 19-22 9075734-7 1997 Down-regulation of PKC activity by long term 12-O-tetradecanoylphorbol 13-acetate (TPA) treatment (24 h) diminished, but did not abolish, the effect of SP on VIP-stimulated cAMP production. Tetradecanoylphorbol Acetate 83-86 protein kinase C, alpha Rattus norvegicus 19-22 9075734-9 1997 TPA, which translocates PKC alpha, beta, and delta in lactotrophs, had a synergistic effect on cAMP formation induced by VIP, but did also, unlike SP, display cAMP rising abilities when cells were not exposed to VIP and forskolin. Tetradecanoylphorbol Acetate 0-3 protein kinase C, alpha Rattus norvegicus 24-33 9124366-5 1997 12-O-tetradecanoylphorbol-13-acetate stimulated surfactant secretion and activated PKC-alpha, -beta, -delta, and -eta isozymes in a dose-dependent manner. Tetradecanoylphorbol Acetate 0-36 protein kinase C, alpha Rattus norvegicus 83-117 9068340-4 1997 Halothane and PMA in combination reduced membrane PKC activity to undetectable levels and reduced cytosol PKC activity (P < 0.01). Tetradecanoylphorbol Acetate 14-17 protein kinase C, alpha Rattus norvegicus 50-53 9068340-4 1997 Halothane and PMA in combination reduced membrane PKC activity to undetectable levels and reduced cytosol PKC activity (P < 0.01). Tetradecanoylphorbol Acetate 14-17 protein kinase C, alpha Rattus norvegicus 106-109 9068340-7 1997 Experiments using isoform-selective antibodies to PKC alpha, PKC beta or PKC gamma demonstrated synergistic interactions between halothane and PMA in promoting translocation of the three conventional PKC isoforms from the cytosol to the membrane fraction of synaptosomes and down-regulation of their immunoreactivity. Tetradecanoylphorbol Acetate 143-146 protein kinase C, alpha Rattus norvegicus 50-59 9068340-7 1997 Experiments using isoform-selective antibodies to PKC alpha, PKC beta or PKC gamma demonstrated synergistic interactions between halothane and PMA in promoting translocation of the three conventional PKC isoforms from the cytosol to the membrane fraction of synaptosomes and down-regulation of their immunoreactivity. Tetradecanoylphorbol Acetate 143-146 protein kinase C, alpha Rattus norvegicus 50-53 9068340-8 1997 Halothane and PMA together reduced cytosol PKC alpha/beta/gamma immunoreactivity significantly more (P < 0.05) than PMA alone. Tetradecanoylphorbol Acetate 14-17 protein kinase C, alpha Rattus norvegicus 43-52 9039136-3 1997 Angiotensin II (ANG II), endothelin-1 (ET-1), and 12-O-tetradecanoylphorbol 13-acetate (TPA) stimulated fourfold to fivefold PKC activity in PKC-alpha cDNA-transfected RTASM cells. Tetradecanoylphorbol Acetate 50-86 protein kinase C, alpha Rattus norvegicus 141-150 9039136-3 1997 Angiotensin II (ANG II), endothelin-1 (ET-1), and 12-O-tetradecanoylphorbol 13-acetate (TPA) stimulated fourfold to fivefold PKC activity in PKC-alpha cDNA-transfected RTASM cells. Tetradecanoylphorbol Acetate 88-91 protein kinase C, alpha Rattus norvegicus 125-128 9039136-3 1997 Angiotensin II (ANG II), endothelin-1 (ET-1), and 12-O-tetradecanoylphorbol 13-acetate (TPA) stimulated fourfold to fivefold PKC activity in PKC-alpha cDNA-transfected RTASM cells. Tetradecanoylphorbol Acetate 88-91 protein kinase C, alpha Rattus norvegicus 141-150 9035611-10 1996 Inhibition of PKC activity by PKC inhibitors (H-7 or staurosporine) or downregulation induced by prolonged treatment with phorbol 12-myristate 13-acetate (PMA) or thyleametoxin (TX) significantly blocked the NE-induced AA release, which indicates PKC is involved in mediating NE-induced AA release. Tetradecanoylphorbol Acetate 155-158 protein kinase C, alpha Rattus norvegicus 14-17 9633822-8 1997 By contrast, TPA promoted rapid activation of all three PKC isozymes. Tetradecanoylphorbol Acetate 13-16 protein kinase C, alpha Rattus norvegicus 56-59 9633822-9 1997 Both the TPA- and FGF-2-mediated PKC activation were prolonged and possibly involved cyclic redistribution of isozymes between soluble and particulate cell fractions. Tetradecanoylphorbol Acetate 9-12 protein kinase C, alpha Rattus norvegicus 33-36 9633822-11 1997 The results of these studies indicate that FGF-2 and TPA independently and conjointly modulate rat prostate-cancer-cell antisense-transfectant doubling time and suggest that effector modulation of rat prostate-cancer-cell proliferation is achieved by processes involving PKC and/or ras mediated signaling. Tetradecanoylphorbol Acetate 53-56 protein kinase C, alpha Rattus norvegicus 271-274 9046017-2 1997 PKC activity was measured in cytosolic and particulate fractions prepared from control myocytes and those treated with either phorbol ester (phorbol 12-myristate 13-acetate, PMA) or a permeant synthetic diacylglycerol analog (1-oleoyl-2-acetylglycerol, OAG) in the absence or presence of an inhibitor of diacylglycerol kinase activity, compound R59022. Tetradecanoylphorbol Acetate 141-172 protein kinase C, alpha Rattus norvegicus 0-3 9046017-2 1997 PKC activity was measured in cytosolic and particulate fractions prepared from control myocytes and those treated with either phorbol ester (phorbol 12-myristate 13-acetate, PMA) or a permeant synthetic diacylglycerol analog (1-oleoyl-2-acetylglycerol, OAG) in the absence or presence of an inhibitor of diacylglycerol kinase activity, compound R59022. Tetradecanoylphorbol Acetate 174-177 protein kinase C, alpha Rattus norvegicus 0-3 9046017-14 1997 Incubation of the myocytes with PMA, but not OAG, resulted in translocation of PKC from the cytosolic to the particulate fraction. Tetradecanoylphorbol Acetate 32-35 protein kinase C, alpha Rattus norvegicus 79-82 9633822-0 1997 Fibroblast growth factor-2 and TPA enhance prostate-cancer-cell proliferation and activate members of the Ras and PKC signal transduction pathways. Tetradecanoylphorbol Acetate 31-34 protein kinase C, alpha Rattus norvegicus 114-117 8863847-8 1996 A complete down-regulation of PKC-alpha and PKC-delta was seen after 24-hr treatment with 12-O-tetradecanoylphorbol-13-acetate. Tetradecanoylphorbol Acetate 90-126 protein kinase C, alpha Rattus norvegicus 30-39 8780012-2 1996 To explore the role of protein kinase C (PKC) in this action of NGF, PKC was down-regulated by long-term treatment of the cells with phorbol 12-myristate 13-acetate (PMA). Tetradecanoylphorbol Acetate 133-164 protein kinase C, alpha Rattus norvegicus 41-44 8922537-1 1996 Insulin and 12-O-tetradecanoyl phorbol-13-acetate (TPA) induce both glucose uptake and translocation of protein kinase C (PKC) from cytosol to membrane in insulin-sensitive tissues as previously reported by several investigators. Tetradecanoylphorbol Acetate 12-49 protein kinase C, alpha Rattus norvegicus 122-125 8922537-1 1996 Insulin and 12-O-tetradecanoyl phorbol-13-acetate (TPA) induce both glucose uptake and translocation of protein kinase C (PKC) from cytosol to membrane in insulin-sensitive tissues as previously reported by several investigators. Tetradecanoylphorbol Acetate 51-54 protein kinase C, alpha Rattus norvegicus 122-125 8922537-5 1996 TPA also induced time-dependent increases in PKC alpha and gamma (34% and 500% increase, respectively) but not in PKC zeta. Tetradecanoylphorbol Acetate 0-3 protein kinase C, alpha Rattus norvegicus 45-54 8877408-4 1996 Incubation of cells with 20 nM phorbol 12-myristate 13-acetate (PMA) for 6 h caused down-regulation of protein kinase C (PKC) alpha and beta isozymes, whereas it had no effect on PKC delta, epsilon and zeta isozymes. Tetradecanoylphorbol Acetate 31-62 protein kinase C, alpha Rattus norvegicus 103-131 8877408-4 1996 Incubation of cells with 20 nM phorbol 12-myristate 13-acetate (PMA) for 6 h caused down-regulation of protein kinase C (PKC) alpha and beta isozymes, whereas it had no effect on PKC delta, epsilon and zeta isozymes. Tetradecanoylphorbol Acetate 64-67 protein kinase C, alpha Rattus norvegicus 103-131 8780012-2 1996 To explore the role of protein kinase C (PKC) in this action of NGF, PKC was down-regulated by long-term treatment of the cells with phorbol 12-myristate 13-acetate (PMA). Tetradecanoylphorbol Acetate 133-164 protein kinase C, alpha Rattus norvegicus 69-72 8780012-2 1996 To explore the role of protein kinase C (PKC) in this action of NGF, PKC was down-regulated by long-term treatment of the cells with phorbol 12-myristate 13-acetate (PMA). Tetradecanoylphorbol Acetate 166-169 protein kinase C, alpha Rattus norvegicus 69-72 8780012-5 1996 These data, as well as that PMA alone can induce AA release in PC12 cells, suggest that PKC is necessary for NGF-induced AA release. Tetradecanoylphorbol Acetate 28-31 protein kinase C, alpha Rattus norvegicus 88-91 7548173-5 1995 RBL-2H3 cells express PKC alpha, beta, delta, epsilon and zeta isozymes and down-regulation of PKC by exposure to PMA (20 nM) for 1-2 h caused rapid decrease in PKC alpha and beta isozymes, leaving PKC delta, epsilon and zeta isozymes intact. Tetradecanoylphorbol Acetate 114-117 protein kinase C, alpha Rattus norvegicus 22-31 8730514-5 1996 Downregulation of PKC alpha and PKC epsilon isoforms following chronic phorbol myristate 12, 13-acetate (PMA) pre-treatment resulted in the abolition of AII-stimulated MAP kinase activation. Tetradecanoylphorbol Acetate 105-108 protein kinase C, alpha Rattus norvegicus 18-27 8871296-3 1995 On the other hand, when the cells were stimulated by phorbol 12-myristate 13-acetate (PMA) or ionophore (A23187), PKCalpha and beta were predominantly translocated. Tetradecanoylphorbol Acetate 53-84 protein kinase C, alpha Rattus norvegicus 114-131 8871296-3 1995 On the other hand, when the cells were stimulated by phorbol 12-myristate 13-acetate (PMA) or ionophore (A23187), PKCalpha and beta were predominantly translocated. Tetradecanoylphorbol Acetate 86-89 protein kinase C, alpha Rattus norvegicus 114-131 7548173-5 1995 RBL-2H3 cells express PKC alpha, beta, delta, epsilon and zeta isozymes and down-regulation of PKC by exposure to PMA (20 nM) for 1-2 h caused rapid decrease in PKC alpha and beta isozymes, leaving PKC delta, epsilon and zeta isozymes intact. Tetradecanoylphorbol Acetate 114-117 protein kinase C, alpha Rattus norvegicus 22-25 7548173-5 1995 RBL-2H3 cells express PKC alpha, beta, delta, epsilon and zeta isozymes and down-regulation of PKC by exposure to PMA (20 nM) for 1-2 h caused rapid decrease in PKC alpha and beta isozymes, leaving PKC delta, epsilon and zeta isozymes intact. Tetradecanoylphorbol Acetate 114-117 protein kinase C, alpha Rattus norvegicus 161-170 7548173-6 1995 Apparent decreases in the levels of PKC alpha and beta to about 50% were observed after adding 20 nM PMA for 1 h, when PMA-stimulated PLD activity was inhibited by up to 70%. Tetradecanoylphorbol Acetate 101-104 protein kinase C, alpha Rattus norvegicus 36-45 7548173-6 1995 Apparent decreases in the levels of PKC alpha and beta to about 50% were observed after adding 20 nM PMA for 1 h, when PMA-stimulated PLD activity was inhibited by up to 70%. Tetradecanoylphorbol Acetate 119-122 protein kinase C, alpha Rattus norvegicus 36-45 7647574-3 1995 Phorbol 12-myristate 13-acetate (PMA) was used as a PKC activator in this study. Tetradecanoylphorbol Acetate 0-31 protein kinase C, alpha Rattus norvegicus 52-55 7738187-12 1995 Both 12-O-tetradecanoyl phorbol 13-acetate and 1,25(OH)2D3 activated endogenous PKC, as assessed by inhibition of myristoylated alanine-rich C kinase substrate back-phosphorylation by exogenous PKC. Tetradecanoylphorbol Acetate 5-42 protein kinase C, alpha Rattus norvegicus 80-83 7738187-12 1995 Both 12-O-tetradecanoyl phorbol 13-acetate and 1,25(OH)2D3 activated endogenous PKC, as assessed by inhibition of myristoylated alanine-rich C kinase substrate back-phosphorylation by exogenous PKC. Tetradecanoylphorbol Acetate 5-42 protein kinase C, alpha Rattus norvegicus 194-197 7779868-4 1995 Phorbol ester (TPA) caused rapid depletion of myotube PKC alpha and PKC alpha and PKC delta isoforms from the cytosolic compartment and rapid appearance of these isoforms in the membrane fraction. Tetradecanoylphorbol Acetate 15-18 protein kinase C, alpha Rattus norvegicus 54-63 7779868-4 1995 Phorbol ester (TPA) caused rapid depletion of myotube PKC alpha and PKC alpha and PKC delta isoforms from the cytosolic compartment and rapid appearance of these isoforms in the membrane fraction. Tetradecanoylphorbol Acetate 15-18 protein kinase C, alpha Rattus norvegicus 68-77 7647574-3 1995 Phorbol 12-myristate 13-acetate (PMA) was used as a PKC activator in this study. Tetradecanoylphorbol Acetate 33-36 protein kinase C, alpha Rattus norvegicus 52-55 7647574-4 1995 PKC activity assay revealed that PMA (300 nM) induced a rapid translocation from cytosol to membrane within 1 min and led to an almost complete translocation within 15 min. Tetradecanoylphorbol Acetate 33-36 protein kinase C, alpha Rattus norvegicus 0-3 7647574-8 1995 Treatment with PMA (300 nM) for 24 h resulted in the down-regulation of PKC alpha, delta, and epsilon, but not PKC zeta. Tetradecanoylphorbol Acetate 15-18 protein kinase C, alpha Rattus norvegicus 72-81 7475951-4 1995 PKC-alpha was mobilized to the membrane fraction by the phorbol ester, TPA, but not by the phosphoinositide-coupled agonists carbachol, methoxamine and substance P (SP). Tetradecanoylphorbol Acetate 71-74 protein kinase C, alpha Rattus norvegicus 0-9 7814423-8 1995 Here we investigate possible molecular mechanisms underlying the reciprocal effects of PKC alpha and PKC beta I. Overexpression of both isoforms enhanced 12-O-tetradecanoyl phorbol-13 acetate-induced expression of the growth regulatory genes c-jun, c-myc, and collagenase and enhanced feedback inhibition of epidermal growth factor receptor binding and cellular levels of diacylglycerol. Tetradecanoylphorbol Acetate 154-191 protein kinase C, alpha Rattus norvegicus 87-96 7475951-6 1995 Biochemical assay of total PKC confirmed that cytosolic enzyme activity was significantly reduced by TPA and carbachol to 29% and 75% respectively of control levels. Tetradecanoylphorbol Acetate 101-104 protein kinase C, alpha Rattus norvegicus 27-30 8021256-3 1994 Upon stimulation by serum or EGF, endogenous PKC species showed no indication of activation such as translocation or down-regulation, whereas TPA or synthetic diacylglycerol caused activation of all these PKC species when judged by these criteria. Tetradecanoylphorbol Acetate 142-145 protein kinase C, alpha Rattus norvegicus 205-208 8052650-2 1994 These cells could be largely depleted of the endogenous PKC isozymes by chronic treatment with phorbol 12-myristate 13-acetate followed by permeabilization of the cells with streptolysin O. Tetradecanoylphorbol Acetate 95-126 protein kinase C, alpha Rattus norvegicus 56-59 7524684-2 1994 TPA, but not CCK-8, caused translocation of PKC enzyme activity from the cytosol fraction to the membrane fraction. Tetradecanoylphorbol Acetate 0-3 protein kinase C, alpha Rattus norvegicus 44-47 8021256-6 1994 On the other hand, TPA caused increased phosphorylation of all three PKC species. Tetradecanoylphorbol Acetate 19-22 protein kinase C, alpha Rattus norvegicus 69-72 8021256-7 1994 Overexpression of these PKC members by introduction of the corresponding cDNA expression plasmids resulted in the enhancement of the cell response to TPA when monitored in terms of transcriptional activation through TPA- or serum-responsive elements. Tetradecanoylphorbol Acetate 150-153 protein kinase C, alpha Rattus norvegicus 24-27 8021256-7 1994 Overexpression of these PKC members by introduction of the corresponding cDNA expression plasmids resulted in the enhancement of the cell response to TPA when monitored in terms of transcriptional activation through TPA- or serum-responsive elements. Tetradecanoylphorbol Acetate 216-219 protein kinase C, alpha Rattus norvegicus 24-27 8021256-9 1994 In contrast to these nonphysiological stimuli, serum (or EGF) stimulation of 3Y1 cells that overexpress the respective PKC members revealed a clear difference between cPKC and nPKC, in that overexpression of nPKC delta or nPKC epsilon resulted in a large increase in TPA- or serum-responsive element activation, whereas the overexpression of cPKC alpha increased activation only very slightly. Tetradecanoylphorbol Acetate 267-270 protein kinase C, alpha Rattus norvegicus 119-122 8242260-14 1993 The protein kinase C (PKC) activator, phorbol 12-myristate 13-acetate (PMA), but not the biologically inactive 4 alpha-phorbol 12,13-didecanoate, increased phospholipase D activity in mesangial cells, suggesting that PKC may mediate nucleotide-induced phosphatidylcholine hydrolysis. Tetradecanoylphorbol Acetate 38-69 protein kinase C, alpha Rattus norvegicus 22-25 7507104-8 1994 Exposure to 1 microM TPA for 24 h down-regulated PKC-alpha, -delta, and -epsilon, but not PKC-zeta. Tetradecanoylphorbol Acetate 21-24 protein kinase C, alpha Rattus norvegicus 49-80 8146021-5 1994 Conversely, PMA-induced inhibition of EPO mRNA accumulation was paralleled by translocation of PKC alpha from cytosol to membranes and the time- and dose-dependent attenuation of the inhibitory effect of PMA on EPO mRNA levels was paralleled by down-regulation of PKC alpha. Tetradecanoylphorbol Acetate 12-15 protein kinase C, alpha Rattus norvegicus 95-104 8146021-5 1994 Conversely, PMA-induced inhibition of EPO mRNA accumulation was paralleled by translocation of PKC alpha from cytosol to membranes and the time- and dose-dependent attenuation of the inhibitory effect of PMA on EPO mRNA levels was paralleled by down-regulation of PKC alpha. Tetradecanoylphorbol Acetate 12-15 protein kinase C, alpha Rattus norvegicus 264-273 8146021-5 1994 Conversely, PMA-induced inhibition of EPO mRNA accumulation was paralleled by translocation of PKC alpha from cytosol to membranes and the time- and dose-dependent attenuation of the inhibitory effect of PMA on EPO mRNA levels was paralleled by down-regulation of PKC alpha. Tetradecanoylphorbol Acetate 204-207 protein kinase C, alpha Rattus norvegicus 95-104 8146021-5 1994 Conversely, PMA-induced inhibition of EPO mRNA accumulation was paralleled by translocation of PKC alpha from cytosol to membranes and the time- and dose-dependent attenuation of the inhibitory effect of PMA on EPO mRNA levels was paralleled by down-regulation of PKC alpha. Tetradecanoylphorbol Acetate 204-207 protein kinase C, alpha Rattus norvegicus 264-273 8293569-16 1994 12-O-Tetradecanoylphorbol 13-acetate (TPA, 300 nmol/L) induced translocation of soluble PKC-alpha, PKC-delta, and PKC-epsilon to the particulate fraction at 30 minutes and complete (PKC-alpha and PKC-delta) or 80% (PKC-epsilon) downregulation at 24 hours. Tetradecanoylphorbol Acetate 0-36 protein kinase C, alpha Rattus norvegicus 88-97 8293569-16 1994 12-O-Tetradecanoylphorbol 13-acetate (TPA, 300 nmol/L) induced translocation of soluble PKC-alpha, PKC-delta, and PKC-epsilon to the particulate fraction at 30 minutes and complete (PKC-alpha and PKC-delta) or 80% (PKC-epsilon) downregulation at 24 hours. Tetradecanoylphorbol Acetate 0-36 protein kinase C, alpha Rattus norvegicus 182-191 8293569-16 1994 12-O-Tetradecanoylphorbol 13-acetate (TPA, 300 nmol/L) induced translocation of soluble PKC-alpha, PKC-delta, and PKC-epsilon to the particulate fraction at 30 minutes and complete (PKC-alpha and PKC-delta) or 80% (PKC-epsilon) downregulation at 24 hours. Tetradecanoylphorbol Acetate 38-41 protein kinase C, alpha Rattus norvegicus 88-97 8293569-16 1994 12-O-Tetradecanoylphorbol 13-acetate (TPA, 300 nmol/L) induced translocation of soluble PKC-alpha, PKC-delta, and PKC-epsilon to the particulate fraction at 30 minutes and complete (PKC-alpha and PKC-delta) or 80% (PKC-epsilon) downregulation at 24 hours. Tetradecanoylphorbol Acetate 38-41 protein kinase C, alpha Rattus norvegicus 182-191 8242260-14 1993 The protein kinase C (PKC) activator, phorbol 12-myristate 13-acetate (PMA), but not the biologically inactive 4 alpha-phorbol 12,13-didecanoate, increased phospholipase D activity in mesangial cells, suggesting that PKC may mediate nucleotide-induced phosphatidylcholine hydrolysis. Tetradecanoylphorbol Acetate 38-69 protein kinase C, alpha Rattus norvegicus 217-220 8242260-14 1993 The protein kinase C (PKC) activator, phorbol 12-myristate 13-acetate (PMA), but not the biologically inactive 4 alpha-phorbol 12,13-didecanoate, increased phospholipase D activity in mesangial cells, suggesting that PKC may mediate nucleotide-induced phosphatidylcholine hydrolysis. Tetradecanoylphorbol Acetate 71-74 protein kinase C, alpha Rattus norvegicus 22-25 8242260-14 1993 The protein kinase C (PKC) activator, phorbol 12-myristate 13-acetate (PMA), but not the biologically inactive 4 alpha-phorbol 12,13-didecanoate, increased phospholipase D activity in mesangial cells, suggesting that PKC may mediate nucleotide-induced phosphatidylcholine hydrolysis. Tetradecanoylphorbol Acetate 71-74 protein kinase C, alpha Rattus norvegicus 217-220 8242260-16 1993 Down-regulation of PKC-alpha and -delta isoenzymes by 8 h PMA treatment still resulted in full phospholipase D activation. Tetradecanoylphorbol Acetate 58-61 protein kinase C, alpha Rattus norvegicus 19-28 1616941-8 1992 Short treatment with PMA decreased the activity of PKC 1 (peaks 1b (PKC-alpha) and 1c) and to a lesser extent of PKC 2; cells from lean animals were more sensitive to PMA than those obtained from obese rats. Tetradecanoylphorbol Acetate 21-24 protein kinase C, alpha Rattus norvegicus 68-77 8425487-1 1993 In rat adipocytes, chronic incubation with 12-O-tetradecanoylphorbol-13-acetate (TPA) reduced immunoreactive protein kinase-C (PKC) beta, gamma, delta, and zeta isoforms by 40-60% and PKC alpha by 75%, but had little effect on PKC epsilon levels. Tetradecanoylphorbol Acetate 43-79 protein kinase C, alpha Rattus norvegicus 184-193 8425487-1 1993 In rat adipocytes, chronic incubation with 12-O-tetradecanoylphorbol-13-acetate (TPA) reduced immunoreactive protein kinase-C (PKC) beta, gamma, delta, and zeta isoforms by 40-60% and PKC alpha by 75%, but had little effect on PKC epsilon levels. Tetradecanoylphorbol Acetate 43-79 protein kinase C, alpha Rattus norvegicus 127-130 8425487-1 1993 In rat adipocytes, chronic incubation with 12-O-tetradecanoylphorbol-13-acetate (TPA) reduced immunoreactive protein kinase-C (PKC) beta, gamma, delta, and zeta isoforms by 40-60% and PKC alpha by 75%, but had little effect on PKC epsilon levels. Tetradecanoylphorbol Acetate 81-84 protein kinase C, alpha Rattus norvegicus 184-193 8425487-1 1993 In rat adipocytes, chronic incubation with 12-O-tetradecanoylphorbol-13-acetate (TPA) reduced immunoreactive protein kinase-C (PKC) beta, gamma, delta, and zeta isoforms by 40-60% and PKC alpha by 75%, but had little effect on PKC epsilon levels. Tetradecanoylphorbol Acetate 81-84 protein kinase C, alpha Rattus norvegicus 127-130 1426252-5 1992 Various PKC pseudosubstrate peptides are phosphorylated by PKC-eta in a phospholipid and TPA-dependent but calcium-independent manner. Tetradecanoylphorbol Acetate 89-92 protein kinase C, alpha Rattus norvegicus 8-11 8452537-3 1993 Stimulation of cardiomyocytes with 4 beta-phorbol 12-myristate 13-acetate (PMA) led to a rapid increase in particulate-bound PKC activity, a response attributed to the activation of alpha-, delta- and zeta- type PKCs but not beta-type PKC. Tetradecanoylphorbol Acetate 35-73 protein kinase C, alpha Rattus norvegicus 125-128 8452537-3 1993 Stimulation of cardiomyocytes with 4 beta-phorbol 12-myristate 13-acetate (PMA) led to a rapid increase in particulate-bound PKC activity, a response attributed to the activation of alpha-, delta- and zeta- type PKCs but not beta-type PKC. Tetradecanoylphorbol Acetate 35-73 protein kinase C, alpha Rattus norvegicus 212-215 8452537-3 1993 Stimulation of cardiomyocytes with 4 beta-phorbol 12-myristate 13-acetate (PMA) led to a rapid increase in particulate-bound PKC activity, a response attributed to the activation of alpha-, delta- and zeta- type PKCs but not beta-type PKC. Tetradecanoylphorbol Acetate 75-78 protein kinase C, alpha Rattus norvegicus 125-128 8452537-3 1993 Stimulation of cardiomyocytes with 4 beta-phorbol 12-myristate 13-acetate (PMA) led to a rapid increase in particulate-bound PKC activity, a response attributed to the activation of alpha-, delta- and zeta- type PKCs but not beta-type PKC. Tetradecanoylphorbol Acetate 75-78 protein kinase C, alpha Rattus norvegicus 212-215 8452537-5 1993 Confirming this, 4 beta-phorbol 12-monoacetate and 4 alpha-phorbol had no effect on cellular eicosanoid formation, while the PMA-induced response was fully abolished both in the presence of the PKC inhibitors staurosporine and CGP 41251 and in PKC-down-regulated cells. Tetradecanoylphorbol Acetate 125-128 protein kinase C, alpha Rattus norvegicus 194-197 8452537-5 1993 Confirming this, 4 beta-phorbol 12-monoacetate and 4 alpha-phorbol had no effect on cellular eicosanoid formation, while the PMA-induced response was fully abolished both in the presence of the PKC inhibitors staurosporine and CGP 41251 and in PKC-down-regulated cells. Tetradecanoylphorbol Acetate 125-128 protein kinase C, alpha Rattus norvegicus 244-247 8081948-14 1993 Phorbol 12-myristate 13-acetate stimulation of PKC caused down-regulation of PKC-alpha, -delta and -epsilon isoenzymes in epithelial and mesangial cells. Tetradecanoylphorbol Acetate 0-31 protein kinase C, alpha Rattus norvegicus 47-50 8081948-14 1993 Phorbol 12-myristate 13-acetate stimulation of PKC caused down-regulation of PKC-alpha, -delta and -epsilon isoenzymes in epithelial and mesangial cells. Tetradecanoylphorbol Acetate 0-31 protein kinase C, alpha Rattus norvegicus 77-107 1741758-4 1991 PC12 cells were "down-regulated" by prior treatment (24 h) with phorbol 12-myristate 13-acetate (PMA; 1 microM), which nearly abolished endogenous PKC activity. Tetradecanoylphorbol Acetate 64-95 protein kinase C, alpha Rattus norvegicus 147-150 1741758-4 1991 PC12 cells were "down-regulated" by prior treatment (24 h) with phorbol 12-myristate 13-acetate (PMA; 1 microM), which nearly abolished endogenous PKC activity. Tetradecanoylphorbol Acetate 97-100 protein kinase C, alpha Rattus norvegicus 147-150 1659379-6 1991 On exposure to PMA a complete depletion of PKC-alpha is observed within 8 h. In contrast, down-regulation of PKC-epsilon to 10-20% of that found in control cells requires a 24 h treatment with PMA. Tetradecanoylphorbol Acetate 15-18 protein kinase C, alpha Rattus norvegicus 43-52 1659379-6 1991 On exposure to PMA a complete depletion of PKC-alpha is observed within 8 h. In contrast, down-regulation of PKC-epsilon to 10-20% of that found in control cells requires a 24 h treatment with PMA. Tetradecanoylphorbol Acetate 193-196 protein kinase C, alpha Rattus norvegicus 43-52 2318854-4 1990 Like endogenous and exogenously expressed wild type PKC alpha, the mutant PKC alpha K----R is translocated from the cytosol to the particulate fraction when cells are treated with a phorbol ester, 12-O-tetradecanoylphorbol-13-acetate (TPA). Tetradecanoylphorbol Acetate 197-233 protein kinase C, alpha Rattus norvegicus 74-83 1861152-4 1991 Further, an increase in calcium/phospholipid-dependent kinase (PKC) activity resulting from the treatment of PC12 cells with NGF and TPA was observed concomitant with the increased phosphorylation of NF-M. Tetradecanoylphorbol Acetate 133-136 protein kinase C, alpha Rattus norvegicus 63-66 1861152-7 1991 These data suggest that NGF with or without TPA stimulates NF-M phosphorylation as a result of a complex series of events which include PKC-independent and PKC-dependent pathways. Tetradecanoylphorbol Acetate 44-47 protein kinase C, alpha Rattus norvegicus 136-139 1861152-7 1991 These data suggest that NGF with or without TPA stimulates NF-M phosphorylation as a result of a complex series of events which include PKC-independent and PKC-dependent pathways. Tetradecanoylphorbol Acetate 44-47 protein kinase C, alpha Rattus norvegicus 156-159 1653025-5 1991 Treatment with TPA provoked a loss of activity of peaks 1b (PKC-alpha) and 1c, whereas peak 1a (PKC-beta) activity was not affected. Tetradecanoylphorbol Acetate 15-18 protein kinase C, alpha Rattus norvegicus 60-77 2318854-4 1990 Like endogenous and exogenously expressed wild type PKC alpha, the mutant PKC alpha K----R is translocated from the cytosol to the particulate fraction when cells are treated with a phorbol ester, 12-O-tetradecanoylphorbol-13-acetate (TPA). Tetradecanoylphorbol Acetate 235-238 protein kinase C, alpha Rattus norvegicus 74-83 2318854-5 1990 On the other hand, the mutant PKC alpha K----R is not degraded when cells are treated with TPA, making a clear contrast to wild type PKC alpha; i.e. the mutant is resistant to TPA-mediated down-regulation. Tetradecanoylphorbol Acetate 91-94 protein kinase C, alpha Rattus norvegicus 30-39 2318854-5 1990 On the other hand, the mutant PKC alpha K----R is not degraded when cells are treated with TPA, making a clear contrast to wild type PKC alpha; i.e. the mutant is resistant to TPA-mediated down-regulation. Tetradecanoylphorbol Acetate 176-179 protein kinase C, alpha Rattus norvegicus 30-39 2318854-5 1990 On the other hand, the mutant PKC alpha K----R is not degraded when cells are treated with TPA, making a clear contrast to wild type PKC alpha; i.e. the mutant is resistant to TPA-mediated down-regulation. Tetradecanoylphorbol Acetate 176-179 protein kinase C, alpha Rattus norvegicus 133-142 2318854-7 1990 These results suggest a link between the kinase activity of PKC alpha and the sensitivity to TPA-mediated proteolytic degradation. Tetradecanoylphorbol Acetate 93-96 protein kinase C, alpha Rattus norvegicus 60-69 24297175-8 2014 Arginine vasopressin (100 and 500 pm) and the PKC activator phorbol 12-myristate 13-acetate (1 nm) each inhibited human (h) Kv7.5 and hKv7.4/7.5, but not hKv7.4 channels expressed in A7r5 cells. Tetradecanoylphorbol Acetate 60-91 protein kinase C, alpha Rattus norvegicus 46-49 33035505-8 2020 The PKC activator PMA, but not the diacylglycerol analogue OAG, stimulated ICa1.2 in a concentration-dependent manner; conversely, the PKCalpha inhibitor Go6976 markedly reduced basal ICa1.2 and, similarly to the PKCdelta (rottlerin) and PKCepsilon translocation inhibitors antagonised PMA-induced current stimulation. Tetradecanoylphorbol Acetate 18-21 protein kinase C, alpha Rattus norvegicus 4-7 33035505-8 2020 The PKC activator PMA, but not the diacylglycerol analogue OAG, stimulated ICa1.2 in a concentration-dependent manner; conversely, the PKCalpha inhibitor Go6976 markedly reduced basal ICa1.2 and, similarly to the PKCdelta (rottlerin) and PKCepsilon translocation inhibitors antagonised PMA-induced current stimulation. Tetradecanoylphorbol Acetate 18-21 protein kinase C, alpha Rattus norvegicus 135-143 33035505-8 2020 The PKC activator PMA, but not the diacylglycerol analogue OAG, stimulated ICa1.2 in a concentration-dependent manner; conversely, the PKCalpha inhibitor Go6976 markedly reduced basal ICa1.2 and, similarly to the PKCdelta (rottlerin) and PKCepsilon translocation inhibitors antagonised PMA-induced current stimulation. Tetradecanoylphorbol Acetate 286-289 protein kinase C, alpha Rattus norvegicus 4-7 33035505-8 2020 The PKC activator PMA, but not the diacylglycerol analogue OAG, stimulated ICa1.2 in a concentration-dependent manner; conversely, the PKCalpha inhibitor Go6976 markedly reduced basal ICa1.2 and, similarly to the PKCdelta (rottlerin) and PKCepsilon translocation inhibitors antagonised PMA-induced current stimulation. Tetradecanoylphorbol Acetate 286-289 protein kinase C, alpha Rattus norvegicus 135-143 31002911-11 2019 In addition, phorbol-12-myristate-13-acetate (PMA, a activator of PKC) markedly attenuated the suppressive effects of propofol on ERK1/2 phosphorylation and NSC proliferation. Tetradecanoylphorbol Acetate 13-44 protein kinase C, alpha Rattus norvegicus 66-69 31002911-11 2019 In addition, phorbol-12-myristate-13-acetate (PMA, a activator of PKC) markedly attenuated the suppressive effects of propofol on ERK1/2 phosphorylation and NSC proliferation. Tetradecanoylphorbol Acetate 46-49 protein kinase C, alpha Rattus norvegicus 66-69 25915883-12 2015 Treatment with PKC-activating agent phorbol-12-myristate-13-acetate attenuated exendin-4-induced relaxations and reduced GLP-1R expression in WKY arteries, which were reversed by GFX, Go6976, or hispidin. Tetradecanoylphorbol Acetate 36-67 protein kinase C, alpha Rattus norvegicus 15-18 22552935-7 2012 alpha-Tocopherol (PKC inhibitor) significantly increased arginine transport in both pregnant and CRF pregnant rats, effects that were attenuated by ex vivo incubation of glomeruli with PMA (a PKC stimulant). Tetradecanoylphorbol Acetate 185-188 protein kinase C, alpha Rattus norvegicus 18-21 22552935-7 2012 alpha-Tocopherol (PKC inhibitor) significantly increased arginine transport in both pregnant and CRF pregnant rats, effects that were attenuated by ex vivo incubation of glomeruli with PMA (a PKC stimulant). Tetradecanoylphorbol Acetate 185-188 protein kinase C, alpha Rattus norvegicus 192-195 22092277-6 2012 Phorbol myristate acetate (100 nmol/L, 10 min) induced the translocation of the PKCalpha, betaI, betaII, delta and epsilon isoforms, whereas 48 h pretreatment of cells with 1 mumol/L Scu significantly inhibited PMA-induced PKCbetaI, betaII and delta translocation. Tetradecanoylphorbol Acetate 0-25 protein kinase C, alpha Rattus norvegicus 80-88 22092277-6 2012 Phorbol myristate acetate (100 nmol/L, 10 min) induced the translocation of the PKCalpha, betaI, betaII, delta and epsilon isoforms, whereas 48 h pretreatment of cells with 1 mumol/L Scu significantly inhibited PMA-induced PKCbetaI, betaII and delta translocation. Tetradecanoylphorbol Acetate 211-214 protein kinase C, alpha Rattus norvegicus 80-88 20610768-5 2010 Using a cell surface biotinylation assay, we showed that PKC activation with phorbol 12-myristate 13-acetate (PMA) increased (approximately 3-fold) cell surface levels of TRPM4-GFP protein in <10 min. Tetradecanoylphorbol Acetate 77-108 protein kinase C, alpha Rattus norvegicus 57-60 21803046-10 2011 Whereas TMX-induced PKC activation was not attenuated inhibition of PKCbeta, inhibition of PKCalpha with HBDDE prevented inhibitory effects of both PMA and TMX. Tetradecanoylphorbol Acetate 148-151 protein kinase C, alpha Rattus norvegicus 91-99 20610768-5 2010 Using a cell surface biotinylation assay, we showed that PKC activation with phorbol 12-myristate 13-acetate (PMA) increased (approximately 3-fold) cell surface levels of TRPM4-GFP protein in <10 min. Tetradecanoylphorbol Acetate 110-113 protein kinase C, alpha Rattus norvegicus 57-60 20610768-8 2010 PMA-induced translocation of TRPM4 to the plasma membrane was independent of PKCalpha and PKCbeta activity but was inhibited by blockade of PKCdelta with rottlerin. Tetradecanoylphorbol Acetate 0-3 protein kinase C, alpha Rattus norvegicus 77-85 20006981-5 2010 The PKCalpha activator, phorbol-12-myristate-13-acetate (PMA) induced the expression of VDR in the rat liver, and the induction of VDR by 1,25(OH)(2)D(3) and CDCA was inhibited by the PKCalpha inhibitor, bisindolyl maleimide I (Bis I). Tetradecanoylphorbol Acetate 24-55 protein kinase C, alpha Rattus norvegicus 4-12 20006981-5 2010 The PKCalpha activator, phorbol-12-myristate-13-acetate (PMA) induced the expression of VDR in the rat liver, and the induction of VDR by 1,25(OH)(2)D(3) and CDCA was inhibited by the PKCalpha inhibitor, bisindolyl maleimide I (Bis I). Tetradecanoylphorbol Acetate 24-55 protein kinase C, alpha Rattus norvegicus 184-192 20006981-5 2010 The PKCalpha activator, phorbol-12-myristate-13-acetate (PMA) induced the expression of VDR in the rat liver, and the induction of VDR by 1,25(OH)(2)D(3) and CDCA was inhibited by the PKCalpha inhibitor, bisindolyl maleimide I (Bis I). Tetradecanoylphorbol Acetate 57-60 protein kinase C, alpha Rattus norvegicus 4-12 20006981-5 2010 The PKCalpha activator, phorbol-12-myristate-13-acetate (PMA) induced the expression of VDR in the rat liver, and the induction of VDR by 1,25(OH)(2)D(3) and CDCA was inhibited by the PKCalpha inhibitor, bisindolyl maleimide I (Bis I). Tetradecanoylphorbol Acetate 57-60 protein kinase C, alpha Rattus norvegicus 184-192 19250646-0 2009 Involvement of PKC alpha in PMA-induced facilitation of exocytosis and vesicle fusion in PC12 cells. Tetradecanoylphorbol Acetate 28-31 protein kinase C, alpha Rattus norvegicus 15-24 20798497-1 2010 BACKGROUND: In this report, we explored the role of PKCalpha and PKCe as mediators of phorbol 12-myristate13-acetate (PMA)-induced proliferation in pituitary tumor GH3B6 cells, and determined if the ERK1/2 and Akt pathways were activated. Tetradecanoylphorbol Acetate 118-121 protein kinase C, alpha Rattus norvegicus 52-60 20798497-5 2010 RESULTS: Incubation with PMA for 15 min stimulated PKCalpha and PKCe activation, which was correlated with the phosphorylation of ERK1/2 but not Akt. Tetradecanoylphorbol Acetate 25-28 protein kinase C, alpha Rattus norvegicus 51-59 19672103-7 2010 Moreover, calphostin C (a PKC inhibitor) inhibited TGF-beta(1)-induced alpha-SMA expression, whereas phorbol-12-myristate-13-acetate (a PKC activator) induced it. Tetradecanoylphorbol Acetate 101-132 protein kinase C, alpha Rattus norvegicus 136-139 19250646-4 2009 Amperometric measurements based on carbon fiber microelectrodes demonstrated that PKC alpha has a key role in the PMA-mediated facilitation of exocytosis and vesicle fusion in neuroendocrine PC12 cells. Tetradecanoylphorbol Acetate 114-117 protein kinase C, alpha Rattus norvegicus 82-91 18456322-6 2008 Ba(2+) influx was reduced by 30-40% when cells were treated with either a PKC inhibitor (Go 6983, bisindolylmaleimide) or the PKC activator phorbol-12-myristate-13-acetate. Tetradecanoylphorbol Acetate 140-171 protein kinase C, alpha Rattus norvegicus 126-129 17845534-4 2007 PKC-alpha and PKC-zeta were located predominantly in the cytosol and were redistributed to the membrane by the PKC agonist, phorbol 12-myristate 13-acetate (PMA), while PKC-delta and PKC-epsilon were highly membrane-bound and did not undergo translocation by PMA. Tetradecanoylphorbol Acetate 124-155 protein kinase C, alpha Rattus norvegicus 0-9 18295358-3 2008 Reciprocal immunoprecipitations followed by Western blot analysis demonstrated that all PKC isozymes expressed in rat hepatocytes are modified by tyrosine nitration and tyrosine phosphorylation in different ways upon exposure of cells to a direct PKC activator (TPA), or to an extracellular ligand known to activate PKC-dependent pathways (epinephrine). Tetradecanoylphorbol Acetate 262-265 protein kinase C, alpha Rattus norvegicus 88-91 17845534-4 2007 PKC-alpha and PKC-zeta were located predominantly in the cytosol and were redistributed to the membrane by the PKC agonist, phorbol 12-myristate 13-acetate (PMA), while PKC-delta and PKC-epsilon were highly membrane-bound and did not undergo translocation by PMA. Tetradecanoylphorbol Acetate 124-155 protein kinase C, alpha Rattus norvegicus 0-3 17845534-4 2007 PKC-alpha and PKC-zeta were located predominantly in the cytosol and were redistributed to the membrane by the PKC agonist, phorbol 12-myristate 13-acetate (PMA), while PKC-delta and PKC-epsilon were highly membrane-bound and did not undergo translocation by PMA. Tetradecanoylphorbol Acetate 157-160 protein kinase C, alpha Rattus norvegicus 0-9 17845534-4 2007 PKC-alpha and PKC-zeta were located predominantly in the cytosol and were redistributed to the membrane by the PKC agonist, phorbol 12-myristate 13-acetate (PMA), while PKC-delta and PKC-epsilon were highly membrane-bound and did not undergo translocation by PMA. Tetradecanoylphorbol Acetate 157-160 protein kinase C, alpha Rattus norvegicus 0-3 17845534-4 2007 PKC-alpha and PKC-zeta were located predominantly in the cytosol and were redistributed to the membrane by the PKC agonist, phorbol 12-myristate 13-acetate (PMA), while PKC-delta and PKC-epsilon were highly membrane-bound and did not undergo translocation by PMA. Tetradecanoylphorbol Acetate 259-262 protein kinase C, alpha Rattus norvegicus 0-9 17845534-4 2007 PKC-alpha and PKC-zeta were located predominantly in the cytosol and were redistributed to the membrane by the PKC agonist, phorbol 12-myristate 13-acetate (PMA), while PKC-delta and PKC-epsilon were highly membrane-bound and did not undergo translocation by PMA. Tetradecanoylphorbol Acetate 259-262 protein kinase C, alpha Rattus norvegicus 0-3 17908462-12 2007 PKC down-regulation by PMA pretreatment or PKC inhibition by Ro31-8220 pre-incubation abolished the effect of 5% CSE on PASMCs proliferation. Tetradecanoylphorbol Acetate 23-26 protein kinase C, alpha Rattus norvegicus 0-3 17106253-9 2006 Dot blot indicated that Bicyclol inhibited mRNA expressions of H-ras, c-myc and PKCalpha genes by TPA-stimulation. Tetradecanoylphorbol Acetate 98-101 protein kinase C, alpha Rattus norvegicus 80-88 16005455-5 2005 PMA treatment produced a concentration-dependent increase in cell injury and PKC activity. Tetradecanoylphorbol Acetate 0-3 protein kinase C, alpha Rattus norvegicus 77-80 16155104-6 2006 Phorbol 12-myristate 13-acetate (PMA) induced nuclear translocation of endogenous PKC alpha and Ad-wtPKC alpha concomitantly with an increase in nuclear TR alpha1 protein. Tetradecanoylphorbol Acetate 0-31 protein kinase C, alpha Rattus norvegicus 82-91 16155104-6 2006 Phorbol 12-myristate 13-acetate (PMA) induced nuclear translocation of endogenous PKC alpha and Ad-wtPKC alpha concomitantly with an increase in nuclear TR alpha1 protein. Tetradecanoylphorbol Acetate 33-36 protein kinase C, alpha Rattus norvegicus 82-91 16283633-6 2006 Injection of phorbolmyristate acetate (PMA), an activator of protein kinase C (PKC) that in turn upregulates OPG expression, also delayed eruption by 1 day. Tetradecanoylphorbol Acetate 13-37 protein kinase C, alpha Rattus norvegicus 79-82 16283633-6 2006 Injection of phorbolmyristate acetate (PMA), an activator of protein kinase C (PKC) that in turn upregulates OPG expression, also delayed eruption by 1 day. Tetradecanoylphorbol Acetate 39-42 protein kinase C, alpha Rattus norvegicus 79-82 16283633-7 2006 PMA was only injected from Days 1-4 such that PKC-alpha would be increased and activated. Tetradecanoylphorbol Acetate 0-3 protein kinase C, alpha Rattus norvegicus 46-55 16042408-3 2005 In vivo phosphorylation studies in COS-1 cells transfected with murine PPARalpha showed that the level of phosphorylated PPARalpha is increased by treatment with the PP Wy-14,643 as well as the PKC activator phorbol myristol acetate (PMA). Tetradecanoylphorbol Acetate 234-237 protein kinase C, alpha Rattus norvegicus 194-197 16046711-7 2005 The insulin secretion induced by phorbol 12-myristate 13-acetate (a stimulator of PKC) was higher in islets of LPN and LPP rats than in the respective controls, especially at 8.3 mmol glucose/L. Tetradecanoylphorbol Acetate 33-64 protein kinase C, alpha Rattus norvegicus 82-85 15878350-7 2005 In HEK-293 cells transfected with rat EBP50 cDNA, a treatment with 12 myristate 13-acetate (PMA) induced a translocation of PKCalpha and beta isoforms to the membrane and increased 32P incorporation into EBP50. Tetradecanoylphorbol Acetate 92-95 protein kinase C, alpha Rattus norvegicus 124-132 16342423-8 2005 In H9c2 cells, coincubation with PMA lead to an increase in the rate of the IGF1 receptor activation, and this may further implicate a role for PKC in regulating the IGF1R. Tetradecanoylphorbol Acetate 33-36 protein kinase C, alpha Rattus norvegicus 144-147 15821757-7 2005 At 1 microM, both agents inhibited PMA-induced PKC activity in ARVM. Tetradecanoylphorbol Acetate 35-38 protein kinase C, alpha Rattus norvegicus 47-50 15855058-8 2005 Inhibition of PKCalpha in isolated TII cells by long-time incubation with PMA inhibited PKCalpha and Prx-1 but not Prx-6. Tetradecanoylphorbol Acetate 74-77 protein kinase C, alpha Rattus norvegicus 14-22 15855058-8 2005 Inhibition of PKCalpha in isolated TII cells by long-time incubation with PMA inhibited PKCalpha and Prx-1 but not Prx-6. Tetradecanoylphorbol Acetate 74-77 protein kinase C, alpha Rattus norvegicus 88-96 15647254-5 2005 A highly specific PKC beta inhibitor, LY379196, blocked dopamine efflux that was stimulated by either amphetamine or the PKC activator, 12-O-tetradecanoylphorbol-13-acetate. Tetradecanoylphorbol Acetate 136-172 protein kinase C, alpha Rattus norvegicus 18-21 15862172-11 2005 Following exposure of RPE cells to PMA for 24 hr, PKC-delta was significantly down regulated, whereas PKC-alpha, -beta, -epsilon and -zeta remained unchanged. Tetradecanoylphorbol Acetate 35-38 protein kinase C, alpha Rattus norvegicus 102-138 15804434-1 2005 We have previously demonstrated that pressure application of the protein kinase C (PKC) activator phorbol 12-myristate 13-acetate (PMA) onto some neurons in the anterior hypothalamic area of rats increases neural activity in vivo and that this PKC activation-induced increase of neural activity is enhanced in spontaneously hypertensive rats (SHR), an animal model for genetic hypertension. Tetradecanoylphorbol Acetate 98-129 protein kinase C, alpha Rattus norvegicus 83-86 15804434-1 2005 We have previously demonstrated that pressure application of the protein kinase C (PKC) activator phorbol 12-myristate 13-acetate (PMA) onto some neurons in the anterior hypothalamic area of rats increases neural activity in vivo and that this PKC activation-induced increase of neural activity is enhanced in spontaneously hypertensive rats (SHR), an animal model for genetic hypertension. Tetradecanoylphorbol Acetate 98-129 protein kinase C, alpha Rattus norvegicus 244-247 15804434-1 2005 We have previously demonstrated that pressure application of the protein kinase C (PKC) activator phorbol 12-myristate 13-acetate (PMA) onto some neurons in the anterior hypothalamic area of rats increases neural activity in vivo and that this PKC activation-induced increase of neural activity is enhanced in spontaneously hypertensive rats (SHR), an animal model for genetic hypertension. Tetradecanoylphorbol Acetate 131-134 protein kinase C, alpha Rattus norvegicus 83-86 15804434-1 2005 We have previously demonstrated that pressure application of the protein kinase C (PKC) activator phorbol 12-myristate 13-acetate (PMA) onto some neurons in the anterior hypothalamic area of rats increases neural activity in vivo and that this PKC activation-induced increase of neural activity is enhanced in spontaneously hypertensive rats (SHR), an animal model for genetic hypertension. Tetradecanoylphorbol Acetate 131-134 protein kinase C, alpha Rattus norvegicus 244-247 15695610-5 2005 We identified an interaction between actin and the PKC alpha isoenzyme in non-activated metaphase II (MII) eggs and in eggs activated by phorbol ester 12-O-tetradecanoyl phorbol-13-acetate (TPA). Tetradecanoylphorbol Acetate 151-188 protein kinase C, alpha Rattus norvegicus 51-60 15695610-5 2005 We identified an interaction between actin and the PKC alpha isoenzyme in non-activated metaphase II (MII) eggs and in eggs activated by phorbol ester 12-O-tetradecanoyl phorbol-13-acetate (TPA). Tetradecanoylphorbol Acetate 190-193 protein kinase C, alpha Rattus norvegicus 51-60 14638691-4 2004 In the current study, comparative analysis of PKCalpha processing induced by the PKC agonists phorbol 12-myristate 13-acetate and bryostatin 1 in IEC-18 rat intestinal epithelial cells demonstrates that: (a) at least two pathways of PKCalpha down-regulation can co-exist within cells, and (b) a single PKC agonist can activate both pathways at the same time. Tetradecanoylphorbol Acetate 94-125 protein kinase C, alpha Rattus norvegicus 46-54 15271671-4 2004 PMA induced nuclear translocation of endogenous and AdV-WT PKC-alpha in NRVMs. Tetradecanoylphorbol Acetate 0-3 protein kinase C, alpha Rattus norvegicus 59-68 15271671-15 2004 However, AdV-DN PKC-alpha partially blocked PMA-induced ERK activation. Tetradecanoylphorbol Acetate 44-47 protein kinase C, alpha Rattus norvegicus 16-25 14961054-7 2004 Furthermore, the phenylephrine concentration-response curve was potentiated in the presence of phorbol 12-myristate13-acetate (PMA) (0.1 microM), a PKC activator (EC50: phenylephrine 1.0 +/- 0.8 microM vs phenylephrine + PMA 0.3 +/- 0.1 microM) and inhibited in the presence of chelerythrine chloride (30 microM), a PKC inhibitor (EC50: phenylephrine 1.0 +/- 0.8 microM vs phenylephrine + chelerythrine chloride 5.7 +/- 2.4 microM). Tetradecanoylphorbol Acetate 95-125 protein kinase C, alpha Rattus norvegicus 148-151 14961054-7 2004 Furthermore, the phenylephrine concentration-response curve was potentiated in the presence of phorbol 12-myristate13-acetate (PMA) (0.1 microM), a PKC activator (EC50: phenylephrine 1.0 +/- 0.8 microM vs phenylephrine + PMA 0.3 +/- 0.1 microM) and inhibited in the presence of chelerythrine chloride (30 microM), a PKC inhibitor (EC50: phenylephrine 1.0 +/- 0.8 microM vs phenylephrine + chelerythrine chloride 5.7 +/- 2.4 microM). Tetradecanoylphorbol Acetate 127-130 protein kinase C, alpha Rattus norvegicus 148-151 14966080-5 2004 The PKC activators phorbol myristate acetate (PMA) and thymeleatoxin opened BK(Ca) channels in single Sprague-Dawley rat PASMC. Tetradecanoylphorbol Acetate 19-44 protein kinase C, alpha Rattus norvegicus 4-7 14966080-5 2004 The PKC activators phorbol myristate acetate (PMA) and thymeleatoxin opened BK(Ca) channels in single Sprague-Dawley rat PASMC. Tetradecanoylphorbol Acetate 46-49 protein kinase C, alpha Rattus norvegicus 4-7 14670076-9 2004 In addition, rat embryo fibroblasts overexpressing syndecan-4 exhibited a slowed down-regulation of PKC-alpha in response either to a prolonged treatment with PMA or to maintaining cells in suspension culture. Tetradecanoylphorbol Acetate 159-162 protein kinase C, alpha Rattus norvegicus 100-109 14638691-4 2004 In the current study, comparative analysis of PKCalpha processing induced by the PKC agonists phorbol 12-myristate 13-acetate and bryostatin 1 in IEC-18 rat intestinal epithelial cells demonstrates that: (a) at least two pathways of PKCalpha down-regulation can co-exist within cells, and (b) a single PKC agonist can activate both pathways at the same time. Tetradecanoylphorbol Acetate 94-125 protein kinase C, alpha Rattus norvegicus 46-49 14638691-4 2004 In the current study, comparative analysis of PKCalpha processing induced by the PKC agonists phorbol 12-myristate 13-acetate and bryostatin 1 in IEC-18 rat intestinal epithelial cells demonstrates that: (a) at least two pathways of PKCalpha down-regulation can co-exist within cells, and (b) a single PKC agonist can activate both pathways at the same time. Tetradecanoylphorbol Acetate 94-125 protein kinase C, alpha Rattus norvegicus 81-84 15763930-7 2004 Injection of a PKC activator, phorbol 12-myristate 13-acetate (PMA), at late postnatal days, slightly accelerated first mandibular molar eruption. Tetradecanoylphorbol Acetate 30-61 protein kinase C, alpha Rattus norvegicus 15-18 15763930-7 2004 Injection of a PKC activator, phorbol 12-myristate 13-acetate (PMA), at late postnatal days, slightly accelerated first mandibular molar eruption. Tetradecanoylphorbol Acetate 63-66 protein kinase C, alpha Rattus norvegicus 15-18 12606313-2 2003 We previously showed that SERCA2 downregulation can be simulated in cultured neonatal rat ventricular myocytes (NRVM) by treatment with the protein kinase C (PKC) activator phorbol 12-myristate 13-acetate (PMA). Tetradecanoylphorbol Acetate 173-204 protein kinase C, alpha Rattus norvegicus 158-161 15136882-5 2004 Treatment of NPVSM with 10 nM 4-beta phorbol myristate acetate (PMA), a PKC activator, induced translocation of PKCalpha, and PKCdelta from the soluble to the particulate fraction, while exposure to 10 nM endothelin-1 (ET-1), a potent vasoconstrictor and mitogenic substance, caused translocation of PKCdelta and PKCiota from the soluble to the particulate fraction. Tetradecanoylphorbol Acetate 64-67 protein kinase C, alpha Rattus norvegicus 112-120 14693697-3 2004 In contrast, responses to the pharmacologic activator 12-O-tetradecanoylphorbol-13-acetate (TPA) were reciprocally modulated by overexpression of the PKC alpha WT or PKC alpha KD but not the corresponding PKC delta adenoviruses. Tetradecanoylphorbol Acetate 54-90 protein kinase C, alpha Rattus norvegicus 150-159 14693697-3 2004 In contrast, responses to the pharmacologic activator 12-O-tetradecanoylphorbol-13-acetate (TPA) were reciprocally modulated by overexpression of the PKC alpha WT or PKC alpha KD but not the corresponding PKC delta adenoviruses. Tetradecanoylphorbol Acetate 54-90 protein kinase C, alpha Rattus norvegicus 166-175 15136882-5 2004 Treatment of NPVSM with 10 nM 4-beta phorbol myristate acetate (PMA), a PKC activator, induced translocation of PKCalpha, and PKCdelta from the soluble to the particulate fraction, while exposure to 10 nM endothelin-1 (ET-1), a potent vasoconstrictor and mitogenic substance, caused translocation of PKCdelta and PKCiota from the soluble to the particulate fraction. Tetradecanoylphorbol Acetate 64-67 protein kinase C, alpha Rattus norvegicus 72-75 12874194-7 2003 The PKC activator phorbol myristate acetate significantly increased vascular O2*- production, which was inhibited by superoxide dismutase, diphenyleneiodonium, chelerythrine, or removal of extracellular Ca2+. Tetradecanoylphorbol Acetate 18-43 protein kinase C, alpha Rattus norvegicus 4-7 12807762-2 2003 Treatment of cells with TPA results in the activation and subsequent depletion of the TPA-responsive protein kinase C (PKC) isoforms. Tetradecanoylphorbol Acetate 24-27 protein kinase C, alpha Rattus norvegicus 119-122 12807762-2 2003 Treatment of cells with TPA results in the activation and subsequent depletion of the TPA-responsive protein kinase C (PKC) isoforms. Tetradecanoylphorbol Acetate 86-89 protein kinase C, alpha Rattus norvegicus 119-122 12807762-6 2003 Prolonged TPA treatment induced down-regulation of PKCalpha, delta and epsilon and a reduction in the total PKC activity, which was associated with recovery of GJIC. Tetradecanoylphorbol Acetate 10-13 protein kinase C, alpha Rattus norvegicus 51-59 12807762-6 2003 Prolonged TPA treatment induced down-regulation of PKCalpha, delta and epsilon and a reduction in the total PKC activity, which was associated with recovery of GJIC. Tetradecanoylphorbol Acetate 10-13 protein kinase C, alpha Rattus norvegicus 51-54 12807762-7 2003 Co-treatment of IAR20 cells with TPA and the proteasomal inhibitor MG132 suppressed down-regulation of PKCalpha, delta and epsilon and caused prolonged PKC activity. Tetradecanoylphorbol Acetate 33-36 protein kinase C, alpha Rattus norvegicus 103-111 12807762-7 2003 Co-treatment of IAR20 cells with TPA and the proteasomal inhibitor MG132 suppressed down-regulation of PKCalpha, delta and epsilon and caused prolonged PKC activity. Tetradecanoylphorbol Acetate 33-36 protein kinase C, alpha Rattus norvegicus 103-106 12807762-9 2003 The general PKC inhibitor GF109203X reversed the effect of MG132, indicating that the prolonged TPA-induced inhibition of GJIC caused by MG132 was due to the prolonged PKC activity. Tetradecanoylphorbol Acetate 96-99 protein kinase C, alpha Rattus norvegicus 12-15 12807762-9 2003 The general PKC inhibitor GF109203X reversed the effect of MG132, indicating that the prolonged TPA-induced inhibition of GJIC caused by MG132 was due to the prolonged PKC activity. Tetradecanoylphorbol Acetate 96-99 protein kinase C, alpha Rattus norvegicus 168-171 12807762-10 2003 These results indicate that proteasomal degradation of PKC is one mechanism by which the recovery of GJIC after TPA treatment is regulated. Tetradecanoylphorbol Acetate 112-115 protein kinase C, alpha Rattus norvegicus 55-58 12453641-10 2002 The present study focused on the glypican-1, syndecan-1 and syndecan-4 mRNA expression and regulation under PKC activation by the phorbol myristate acetate (PMA) in 10-30 day-old Sertoli cells. Tetradecanoylphorbol Acetate 130-155 protein kinase C, alpha Rattus norvegicus 108-111 12651935-2 2003 To examine this regulation at the signal transduction level, we treated cultured dental follicle cells with either phorbolmyristate acetate (PMA) or dibutyryl cyclic AMP (dbcAMP) to activate either protein kinase C (PKC) or protein kinase A (PKA). Tetradecanoylphorbol Acetate 115-139 protein kinase C, alpha Rattus norvegicus 216-219 12359735-6 2002 In vivo phosphorylation studies using (32)P(i)-labeled mesangial cells revealed that TPA, PDGF, angiotensin II, and ATP trigger an increased phosphorylation of the neutral ceramidase, which is blocked by the broad spectrum PKC inhibitor Ro-31 8220 but not by CGP 41251, which has a preferential action on Ca(2+)-dependent isoforms, thus suggesting the involvement of a Ca(2+)-independent PKC isoform. Tetradecanoylphorbol Acetate 85-88 protein kinase C, alpha Rattus norvegicus 223-226 12359735-6 2002 In vivo phosphorylation studies using (32)P(i)-labeled mesangial cells revealed that TPA, PDGF, angiotensin II, and ATP trigger an increased phosphorylation of the neutral ceramidase, which is blocked by the broad spectrum PKC inhibitor Ro-31 8220 but not by CGP 41251, which has a preferential action on Ca(2+)-dependent isoforms, thus suggesting the involvement of a Ca(2+)-independent PKC isoform. Tetradecanoylphorbol Acetate 85-88 protein kinase C, alpha Rattus norvegicus 388-391 12639716-3 2003 In the present study we show that treatment of intact mouse islets and RINm5F cells with protein kinase C (PKC) activator phorbol 12-myristate 13-acetate (PMA) or protein kinase A (PKA) activator forskolin promoted insulin secretion with no changes of [Ca(2+)](i). Tetradecanoylphorbol Acetate 122-153 protein kinase C, alpha Rattus norvegicus 107-110 12639716-3 2003 In the present study we show that treatment of intact mouse islets and RINm5F cells with protein kinase C (PKC) activator phorbol 12-myristate 13-acetate (PMA) or protein kinase A (PKA) activator forskolin promoted insulin secretion with no changes of [Ca(2+)](i). Tetradecanoylphorbol Acetate 155-158 protein kinase C, alpha Rattus norvegicus 107-110 12639716-6 2003 PMA treatment caused translocation of PKC-alpha and PKC- epsilon from cytosol to membrane, implying that selectively PKC-alpha and PKC- epsilon isoforms might be important for insulin secretion. Tetradecanoylphorbol Acetate 0-3 protein kinase C, alpha Rattus norvegicus 38-47 12639716-6 2003 PMA treatment caused translocation of PKC-alpha and PKC- epsilon from cytosol to membrane, implying that selectively PKC-alpha and PKC- epsilon isoforms might be important for insulin secretion. Tetradecanoylphorbol Acetate 0-3 protein kinase C, alpha Rattus norvegicus 117-126 12118064-1 2002 Downregulation of protein kinase Calpha (PKCalpha) following long-term exposure to phorbol esters such as TPA is traffic dependent and involves delivery of the active, membrane-associated PKCalpha to endosomes. Tetradecanoylphorbol Acetate 106-109 protein kinase C, alpha Rattus norvegicus 18-39 12118064-1 2002 Downregulation of protein kinase Calpha (PKCalpha) following long-term exposure to phorbol esters such as TPA is traffic dependent and involves delivery of the active, membrane-associated PKCalpha to endosomes. Tetradecanoylphorbol Acetate 106-109 protein kinase C, alpha Rattus norvegicus 41-49 12118064-1 2002 Downregulation of protein kinase Calpha (PKCalpha) following long-term exposure to phorbol esters such as TPA is traffic dependent and involves delivery of the active, membrane-associated PKCalpha to endosomes. Tetradecanoylphorbol Acetate 106-109 protein kinase C, alpha Rattus norvegicus 188-196 12118064-2 2002 In this study, we show that synaptotagmin II (Syt II), a member of the Syt family of proteins, is required for TPA-induced degradation of PKCalpha. Tetradecanoylphorbol Acetate 111-114 protein kinase C, alpha Rattus norvegicus 138-146 12118064-4 2002 We demonstrate that in TPA-treated RBL cells, PKCalpha travels from the cytosol to the plasma membrane, where it is delivered to early endosomes on its route to degradation. Tetradecanoylphorbol Acetate 23-26 protein kinase C, alpha Rattus norvegicus 46-54 12118064-5 2002 By contrast, in TPA-treated RBL-Syt II(-) cells, PKCalpha is diverted to recycling endosomes and remains distributed between the plasma membrane and the perinuclear recycling endocytic compartment. Tetradecanoylphorbol Acetate 16-19 protein kinase C, alpha Rattus norvegicus 49-57 12080017-8 2002 PKC alpha translocation was first detected 5-10 min after exposure to TPA and reached a maximum at 20 min, whereas in eggs activated by OAG, translocation of PKC alpha was observed almost immediately and reached a maximum within 5 min. Tetradecanoylphorbol Acetate 70-73 protein kinase C, alpha Rattus norvegicus 0-9 12453641-10 2002 The present study focused on the glypican-1, syndecan-1 and syndecan-4 mRNA expression and regulation under PKC activation by the phorbol myristate acetate (PMA) in 10-30 day-old Sertoli cells. Tetradecanoylphorbol Acetate 157-160 protein kinase C, alpha Rattus norvegicus 108-111 11832354-5 2002 Phorbol 12-myristate 13-acetate (PMA) stimulated PKC-alpha translocation from the cytosol to the membrane and inhibited approximately 50% of the PTH-(1-34), forskolin, and 8-bromoadenosine 3",5"-cyclic monophosphate-stimulated IGFBP-5 mRNA levels, suggesting that PKC-alpha negatively regulates protein kinase A (PKA)-mediated induction of IGFBP-5 mRNA. Tetradecanoylphorbol Acetate 0-31 protein kinase C, alpha Rattus norvegicus 49-58 11897696-3 2002 In whole cell lysates, proteasome inhibitors (proteasome inhibitor I and II, Lactacystin, beta-Lactone, Calpain inhibitor I) prevented in both gonadotrope cell lines the TPA-induced depletion of PKC alpha, epsilon, and the GnRH-elicited PKC epsilon down-regulation; they counteracted in mixed pituitary cell cultures as well, the TPA-evoked PKC alpha, epsilon depletion. Tetradecanoylphorbol Acetate 170-173 protein kinase C, alpha Rattus norvegicus 195-204 11897696-3 2002 In whole cell lysates, proteasome inhibitors (proteasome inhibitor I and II, Lactacystin, beta-Lactone, Calpain inhibitor I) prevented in both gonadotrope cell lines the TPA-induced depletion of PKC alpha, epsilon, and the GnRH-elicited PKC epsilon down-regulation; they counteracted in mixed pituitary cell cultures as well, the TPA-evoked PKC alpha, epsilon depletion. Tetradecanoylphorbol Acetate 170-173 protein kinase C, alpha Rattus norvegicus 341-350 11897696-7 2002 Inhibition of PKC catalytic activity (GF109203X, Go6976), selectively prevented the TPA-evoked PKC alpha depletion in both mixed pituitary cells and alpha T(3)-1 gonadotropes; in alpha T(3)-1 subcellular fractions, PKC alpha inactivation overcame the TPA-evoked isoenzyme degradation by inducing a pronounced membrane accumulation of the isoform without affecting its membrane relocalization. Tetradecanoylphorbol Acetate 84-87 protein kinase C, alpha Rattus norvegicus 14-17 11897696-7 2002 Inhibition of PKC catalytic activity (GF109203X, Go6976), selectively prevented the TPA-evoked PKC alpha depletion in both mixed pituitary cells and alpha T(3)-1 gonadotropes; in alpha T(3)-1 subcellular fractions, PKC alpha inactivation overcame the TPA-evoked isoenzyme degradation by inducing a pronounced membrane accumulation of the isoform without affecting its membrane relocalization. Tetradecanoylphorbol Acetate 84-87 protein kinase C, alpha Rattus norvegicus 95-104 11897696-7 2002 Inhibition of PKC catalytic activity (GF109203X, Go6976), selectively prevented the TPA-evoked PKC alpha depletion in both mixed pituitary cells and alpha T(3)-1 gonadotropes; in alpha T(3)-1 subcellular fractions, PKC alpha inactivation overcame the TPA-evoked isoenzyme degradation by inducing a pronounced membrane accumulation of the isoform without affecting its membrane relocalization. Tetradecanoylphorbol Acetate 84-87 protein kinase C, alpha Rattus norvegicus 215-224 11897696-7 2002 Inhibition of PKC catalytic activity (GF109203X, Go6976), selectively prevented the TPA-evoked PKC alpha depletion in both mixed pituitary cells and alpha T(3)-1 gonadotropes; in alpha T(3)-1 subcellular fractions, PKC alpha inactivation overcame the TPA-evoked isoenzyme degradation by inducing a pronounced membrane accumulation of the isoform without affecting its membrane relocalization. Tetradecanoylphorbol Acetate 251-254 protein kinase C, alpha Rattus norvegicus 14-17 11832354-5 2002 Phorbol 12-myristate 13-acetate (PMA) stimulated PKC-alpha translocation from the cytosol to the membrane and inhibited approximately 50% of the PTH-(1-34), forskolin, and 8-bromoadenosine 3",5"-cyclic monophosphate-stimulated IGFBP-5 mRNA levels, suggesting that PKC-alpha negatively regulates protein kinase A (PKA)-mediated induction of IGFBP-5 mRNA. Tetradecanoylphorbol Acetate 33-36 protein kinase C, alpha Rattus norvegicus 49-58 11832354-5 2002 Phorbol 12-myristate 13-acetate (PMA) stimulated PKC-alpha translocation from the cytosol to the membrane and inhibited approximately 50% of the PTH-(1-34), forskolin, and 8-bromoadenosine 3",5"-cyclic monophosphate-stimulated IGFBP-5 mRNA levels, suggesting that PKC-alpha negatively regulates protein kinase A (PKA)-mediated induction of IGFBP-5 mRNA. Tetradecanoylphorbol Acetate 33-36 protein kinase C, alpha Rattus norvegicus 264-273 11832354-5 2002 Phorbol 12-myristate 13-acetate (PMA) stimulated PKC-alpha translocation from the cytosol to the membrane and inhibited approximately 50% of the PTH-(1-34), forskolin, and 8-bromoadenosine 3",5"-cyclic monophosphate-stimulated IGFBP-5 mRNA levels, suggesting that PKC-alpha negatively regulates protein kinase A (PKA)-mediated induction of IGFBP-5 mRNA. Tetradecanoylphorbol Acetate 0-31 protein kinase C, alpha Rattus norvegicus 264-273 11896487-7 2002 RESULTS: PMA (200 nM) induced maximal translocation of ventricular PKCalpha from the cytosol to the membranes within 10 min. Tetradecanoylphorbol Acetate 9-12 protein kinase C, alpha Rattus norvegicus 67-75 11873046-11 2002 PKC activation with phorbol myristate acetate attenuated isoproterenol-stimulated cAMP production. Tetradecanoylphorbol Acetate 20-45 protein kinase C, alpha Rattus norvegicus 0-3 11779137-4 2002 Treatment with the phorbol ester TPA caused translocation of PKC alpha, beta2, and epsilon to the plasma membrane. Tetradecanoylphorbol Acetate 33-36 protein kinase C, alpha Rattus norvegicus 61-70