PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 10593877-1 1999 We and others have previously demonstrated the existence of an autonomous nuclear polyphosphoinositide cycle that generates second messengers such as diacylglycerol (DAG), capable of attracting to the nucleus specific protein kinase C (PKC) isoforms (Neri et al. Diglycerides 150-164 protein kinase C, alpha Rattus norvegicus 236-239 10593877-1 1999 We and others have previously demonstrated the existence of an autonomous nuclear polyphosphoinositide cycle that generates second messengers such as diacylglycerol (DAG), capable of attracting to the nucleus specific protein kinase C (PKC) isoforms (Neri et al. Diglycerides 166-169 protein kinase C, alpha Rattus norvegicus 236-239 9538007-3 1998 For PKC-alpha, diacylglycerol (DG) specifically enhanced the binding of PKC-alpha to phosphatidylserine (PS)-containing vesicles by 2 orders of magnitude, allowing PKC-alpha high specificity for PS. Diglycerides 15-29 protein kinase C, alpha Rattus norvegicus 4-13 10444518-2 1999 Such agents include 12-O-tetradecanoylphorbol 13-acetate (TPA) and cell-permeable diacylglycerols that directly activate PKC. Diglycerides 82-97 protein kinase C, alpha Rattus norvegicus 121-124 10444518-3 1999 Other agents include ATP and UTP, which act at P2Y(2) receptors coupled to phosphoinositide-specific phospholipase C, activation of which leads to formation of diacylglycerols and consequent activation of PKC. Diglycerides 160-175 protein kinase C, alpha Rattus norvegicus 205-208 10444518-10 1999 The data show that direct activators and agents that generate endogenous diacylglycerols have different PKC activation patterns. Diglycerides 73-88 protein kinase C, alpha Rattus norvegicus 104-107 9604867-9 1998 By Western blotting analysis, carbachol selectively translocated the conventional PKC isozymes alpha and beta (the activation of which is dependent on Ca2+ and DAG) from the cytosol to the membrane. Diglycerides 160-163 protein kinase C, alpha Rattus norvegicus 82-85 9538007-3 1998 For PKC-alpha, diacylglycerol (DG) specifically enhanced the binding of PKC-alpha to phosphatidylserine (PS)-containing vesicles by 2 orders of magnitude, allowing PKC-alpha high specificity for PS. Diglycerides 15-29 protein kinase C, alpha Rattus norvegicus 72-81 9538007-3 1998 For PKC-alpha, diacylglycerol (DG) specifically enhanced the binding of PKC-alpha to phosphatidylserine (PS)-containing vesicles by 2 orders of magnitude, allowing PKC-alpha high specificity for PS. Diglycerides 15-29 protein kinase C, alpha Rattus norvegicus 72-81 9568702-2 1998 This study was designed to identify the expression of diacylglycerol (DAG)-sensitive PKC-alpha, -betaII, -delta, and -epsilon isoforms in normal and diabetic rat glomerular cells and to determine the effects of high glucose and insulin on PKC isoform cellular compartmentalization and PKC activity. Diglycerides 54-68 protein kinase C, alpha Rattus norvegicus 85-94 9568702-2 1998 This study was designed to identify the expression of diacylglycerol (DAG)-sensitive PKC-alpha, -betaII, -delta, and -epsilon isoforms in normal and diabetic rat glomerular cells and to determine the effects of high glucose and insulin on PKC isoform cellular compartmentalization and PKC activity. Diglycerides 54-68 protein kinase C, alpha Rattus norvegicus 85-88 9568702-2 1998 This study was designed to identify the expression of diacylglycerol (DAG)-sensitive PKC-alpha, -betaII, -delta, and -epsilon isoforms in normal and diabetic rat glomerular cells and to determine the effects of high glucose and insulin on PKC isoform cellular compartmentalization and PKC activity. Diglycerides 54-68 protein kinase C, alpha Rattus norvegicus 239-242 9568702-2 1998 This study was designed to identify the expression of diacylglycerol (DAG)-sensitive PKC-alpha, -betaII, -delta, and -epsilon isoforms in normal and diabetic rat glomerular cells and to determine the effects of high glucose and insulin on PKC isoform cellular compartmentalization and PKC activity. Diglycerides 70-73 protein kinase C, alpha Rattus norvegicus 85-94 9568702-2 1998 This study was designed to identify the expression of diacylglycerol (DAG)-sensitive PKC-alpha, -betaII, -delta, and -epsilon isoforms in normal and diabetic rat glomerular cells and to determine the effects of high glucose and insulin on PKC isoform cellular compartmentalization and PKC activity. Diglycerides 70-73 protein kinase C, alpha Rattus norvegicus 85-88 9568702-2 1998 This study was designed to identify the expression of diacylglycerol (DAG)-sensitive PKC-alpha, -betaII, -delta, and -epsilon isoforms in normal and diabetic rat glomerular cells and to determine the effects of high glucose and insulin on PKC isoform cellular compartmentalization and PKC activity. Diglycerides 70-73 protein kinase C, alpha Rattus norvegicus 239-242 9568702-12 1998 In conclusion, DAG-sensitive PKC-alpha, -betaII, -delta, and -epsilon isoforms are all found in the three major glomerular cell types in rats, and the expression, compartmentalization, and activity are modulated independently by high glucose and insulin. Diglycerides 15-18 protein kinase C, alpha Rattus norvegicus 29-38 9447980-6 1998 Diacylglycerol, the physiological activator of PKC, also stimulated ubiquitination and degradation of PKC, suggesting that ubiquitination is a physiological response to PKC activation. Diglycerides 0-14 protein kinase C, alpha Rattus norvegicus 47-50 9447980-6 1998 Diacylglycerol, the physiological activator of PKC, also stimulated ubiquitination and degradation of PKC, suggesting that ubiquitination is a physiological response to PKC activation. Diglycerides 0-14 protein kinase C, alpha Rattus norvegicus 102-105 9447980-6 1998 Diacylglycerol, the physiological activator of PKC, also stimulated ubiquitination and degradation of PKC, suggesting that ubiquitination is a physiological response to PKC activation. Diglycerides 0-14 protein kinase C, alpha Rattus norvegicus 102-105 9447980-7 1998 Compounds that inhibit activation of PKC prevented both TPA- and diacylglycerol-induced PKC depletion and ubiquitination. Diglycerides 65-79 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. Diglycerides 65-79 protein kinase C, alpha Rattus norvegicus 88-91 9458268-0 1997 Activation of protein kinase C alpha and delta by bile acids: correlation with bile acid structure and diacylglycerol formation. Diglycerides 103-117 protein kinase C, alpha Rattus norvegicus 14-36 9000691-2 1997 Lipid measurements showed that triglyceride and diacylglycerol, an activator of PKC, were elevated four- and twofold, respectively. Diglycerides 48-62 protein kinase C, alpha Rattus norvegicus 80-83 9313873-2 1997 The binding of endogenous diacyl glycerol (DAG) to the cysteine-rich domain (CRD) of PKC is associated with normal cell signaling and function. Diglycerides 26-41 protein kinase C, alpha Rattus norvegicus 85-88 9313873-2 1997 The binding of endogenous diacyl glycerol (DAG) to the cysteine-rich domain (CRD) of PKC is associated with normal cell signaling and function. Diglycerides 43-46 protein kinase C, alpha Rattus norvegicus 85-88 9202063-4 1997 Hyperglycemia increased diacylglycerol (DAG) level in cultured mesangial cells exposed to high concentrations of glucose and activated PKC alpha and beta1 isoforms in the renal glomeruli of diabetic rats. Diglycerides 40-43 protein kinase C, alpha Rattus norvegicus 135-144 7665577-12 1995 In addition, alkenyl,acylglycerols inhibit diacylglycerol-stimulated immunoprecipitated protein kinase C alpha activity in vitro and total protein kinase C activity in permeabilized mesangial cells ex vivo. Diglycerides 43-57 protein kinase C, alpha Rattus norvegicus 88-110 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. Diglycerides 203-217 protein kinase C, alpha Rattus norvegicus 0-3 8826977-5 1996 These increases in membrane PKC (alpha, beta, epsilon, and delta) could not be accounted for by alterations in PKC mRNA or total PKC levels but were associated with increases in membrane diacylglycerol (DAG) and therefore appeared to reflect translocative activation of PKC. Diglycerides 187-201 protein kinase C, alpha Rattus norvegicus 28-64 8826977-5 1996 These increases in membrane PKC (alpha, beta, epsilon, and delta) could not be accounted for by alterations in PKC mRNA or total PKC levels but were associated with increases in membrane diacylglycerol (DAG) and therefore appeared to reflect translocative activation of PKC. Diglycerides 187-201 protein kinase C, alpha Rattus norvegicus 28-31 8826977-5 1996 These increases in membrane PKC (alpha, beta, epsilon, and delta) could not be accounted for by alterations in PKC mRNA or total PKC levels but were associated with increases in membrane diacylglycerol (DAG) and therefore appeared to reflect translocative activation of PKC. Diglycerides 203-206 protein kinase C, alpha Rattus norvegicus 28-64 8826977-5 1996 These increases in membrane PKC (alpha, beta, epsilon, and delta) could not be accounted for by alterations in PKC mRNA or total PKC levels but were associated with increases in membrane diacylglycerol (DAG) and therefore appeared to reflect translocative activation of PKC. Diglycerides 203-206 protein kinase C, alpha Rattus norvegicus 28-31 7524684-8 1994 Each receptor-mediated agonist that caused translocation of PKC also increased DAG, and with CCK-8 and carbachol cycling of PKC-epsilon between cytosol and membrane was accompanied by corresponding cyclic changes in cellular DAG. Diglycerides 79-82 protein kinase C, alpha Rattus norvegicus 60-63 7752575-12 1995 The results show cell-specific and developmentally-dependent expression of three types of PKC isoforms with different responses to diacylglycerol and calcium. Diglycerides 131-145 protein kinase C, alpha Rattus norvegicus 90-93 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. Diglycerides 372-386 protein kinase C, alpha Rattus norvegicus 87-96 7524684-10 1994 Translocation of a PKC isoform could be accounted for by whether the increased DAG originated from PIP2 (accompanied by translocation) or from phosphatidylcholine (no accompanying translocation). Diglycerides 79-82 protein kinase C, alpha Rattus norvegicus 19-22 8080473-9 1993 Phosphorylation of RC3 by PKC alpha, beta, or gamma was stimulated by Ca2+, phospholipid, and diacylglycerol. Diglycerides 94-108 protein kinase C, alpha Rattus norvegicus 26-35 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. Diglycerides 159-173 protein kinase C, alpha Rattus norvegicus 205-208 8021256-8 1994 Such enhancement in transcriptional activation by overexpression of cPKC alpha, nPKC delta, or nPKC epsilon was also observed in response to diacylglycerol, indicating that all these PKC species are activated by diacylglycerol in cells. Diglycerides 141-155 protein kinase C, alpha Rattus norvegicus 69-72 8021256-8 1994 Such enhancement in transcriptional activation by overexpression of cPKC alpha, nPKC delta, or nPKC epsilon was also observed in response to diacylglycerol, indicating that all these PKC species are activated by diacylglycerol in cells. Diglycerides 212-226 protein kinase C, alpha Rattus norvegicus 69-72 8182122-2 1994 Presently, we examined the major subcellular site of PKC translocation/activation in response to glucose-induced DAG. Diglycerides 113-116 protein kinase C, alpha Rattus norvegicus 53-56 8182122-4 1994 This glucose-induced increase in microsomal DAG was attended by increases in immunoreactive PKC alpha, beta, and epsilon. Diglycerides 44-47 protein kinase C, alpha Rattus norvegicus 92-101 8404676-2 1993 The activation of protein kinase-C (PKC) in rat skeletal muscle is mediated by insulin stimulation of diacylglycerol (DAG) levels. Diglycerides 102-116 protein kinase C, alpha Rattus norvegicus 36-39 8404676-2 1993 The activation of protein kinase-C (PKC) in rat skeletal muscle is mediated by insulin stimulation of diacylglycerol (DAG) levels. Diglycerides 118-121 protein kinase C, alpha Rattus norvegicus 36-39 8404676-3 1993 Defects in the activation of PKC in the heart and liver of obese Zucker rats indicate that an abnormality in either stimulation of DAG or PKC occurs in obese tissues. Diglycerides 131-134 protein kinase C, alpha Rattus norvegicus 29-32 8404676-13 1993 Thus, levels of common PKC isozyme mRNA, protein, and enzyme activity in soleus muscle of the obese Zucker rat are decreased even though levels of the endogenous PKC activator DAG are elevated. Diglycerides 176-179 protein kinase C, alpha Rattus norvegicus 162-165 27413044-9 2016 We then tested a potential role for PEDF receptor-mediated effects on upregulation of protein kinase C (PKC) and found evidence of signaling through the diacylglycerol/PKCalpha pathway. Diglycerides 153-167 protein kinase C, alpha Rattus norvegicus 168-176 2280899-6 1990 The redistribution of PKC to the cell membranes during and following ischemia could be due to ischemia induced receptor activation, increased levels of diacylglycerols, arachidonate and intracellular calcium, and may be of importance for the development of ischemic neuronal damage. Diglycerides 152-167 protein kinase C, alpha Rattus norvegicus 22-25 8354345-2 1993 In lung, frontal cerebral cortex and cerebellum cytosols (enriched in PKC alpha, beta and gamma, respectively) displacement of specific binding by phorbol 12,13-dibutyrate or diacylglycerols containing unsaturated acyl chains was of similar potency for each tissue. Diglycerides 175-190 protein kinase C, alpha Rattus norvegicus 70-79 1538715-3 1992 Protein kinase C (PKC) is a family of Ca(2+)- and phosphatidylserine-dependent protein kinases that are activated in vivo by the second messenger diacylglycerol. Diglycerides 146-160 protein kinase C, alpha Rattus norvegicus 18-21 1516148-2 1992 Stimulation of kinase activity by diacylglycerol and calcium often leads to translocation of PKC from the cytosol to a particulate fraction (Kraft and Anderson: Nature 301:621-623, 1983). Diglycerides 34-48 protein kinase C, alpha Rattus norvegicus 93-96 2244886-5 1990 AF binds to PKC presumably at the DAG binding site as suggested by the competition between phorbol dibutyrate and AF for binding to the kinase. Diglycerides 34-37 protein kinase C, alpha Rattus norvegicus 12-15 14563700-8 2004 PI3-kinase products could induce PLC-gamma activation, whose hydrolytic activity could activate the DAG-dependent isoforms PKC alpha, theta, and epsilon. Diglycerides 100-103 protein kinase C, alpha Rattus norvegicus 123-132 21132404-2 2011 A key step in the activation of PKC is translocation to membranes and binding of membrane-associated activators including diacylglycerol (DAG). Diglycerides 122-136 protein kinase C, alpha Rattus norvegicus 32-35 21132404-2 2011 A key step in the activation of PKC is translocation to membranes and binding of membrane-associated activators including diacylglycerol (DAG). Diglycerides 138-141 protein kinase C, alpha Rattus norvegicus 32-35 21132404-3 2011 Interaction of novel and conventional isotypes of PKC with DAG and phorbol esters occurs through the two C1 regulatory domains (C1A and C1B), which exhibit distinct ligand binding selectivity that likely controls enzyme activation by different co-activators. Diglycerides 59-62 protein kinase C, alpha Rattus norvegicus 50-53 16043888-7 2005 DAG concentration exhibited a significant decline by d 5, consistent with the decrease in maximal PKC activity. Diglycerides 0-3 protein kinase C, alpha Rattus norvegicus 98-101 23207450-2 2013 PKC depends on diacylglycerol (DAG) for its activation in vivo We have previously reported that DAG peroxides (DAG-O(O)H) activate PKC in vitro more strongly than unoxidized DAG, suggesting that DAG-O(O)H, if generated in vivo under oxidative stress, would act as an aberrant signal transducer. Diglycerides 15-29 protein kinase C, alpha Rattus norvegicus 0-3 23207450-2 2013 PKC depends on diacylglycerol (DAG) for its activation in vivo We have previously reported that DAG peroxides (DAG-O(O)H) activate PKC in vitro more strongly than unoxidized DAG, suggesting that DAG-O(O)H, if generated in vivo under oxidative stress, would act as an aberrant signal transducer. Diglycerides 15-29 protein kinase C, alpha Rattus norvegicus 131-134 23207450-2 2013 PKC depends on diacylglycerol (DAG) for its activation in vivo We have previously reported that DAG peroxides (DAG-O(O)H) activate PKC in vitro more strongly than unoxidized DAG, suggesting that DAG-O(O)H, if generated in vivo under oxidative stress, would act as an aberrant signal transducer. Diglycerides 31-34 protein kinase C, alpha Rattus norvegicus 0-3 23207450-2 2013 PKC depends on diacylglycerol (DAG) for its activation in vivo We have previously reported that DAG peroxides (DAG-O(O)H) activate PKC in vitro more strongly than unoxidized DAG, suggesting that DAG-O(O)H, if generated in vivo under oxidative stress, would act as an aberrant signal transducer. Diglycerides 31-34 protein kinase C, alpha Rattus norvegicus 131-134 23207450-2 2013 PKC depends on diacylglycerol (DAG) for its activation in vivo We have previously reported that DAG peroxides (DAG-O(O)H) activate PKC in vitro more strongly than unoxidized DAG, suggesting that DAG-O(O)H, if generated in vivo under oxidative stress, would act as an aberrant signal transducer. Diglycerides 96-99 protein kinase C, alpha Rattus norvegicus 0-3 23207450-2 2013 PKC depends on diacylglycerol (DAG) for its activation in vivo We have previously reported that DAG peroxides (DAG-O(O)H) activate PKC in vitro more strongly than unoxidized DAG, suggesting that DAG-O(O)H, if generated in vivo under oxidative stress, would act as an aberrant signal transducer. Diglycerides 96-99 protein kinase C, alpha Rattus norvegicus 131-134 15476589-5 2004 Diacylglycerol (DAG) generation from phospholipase D (PLD) is one pathway of PKC activation, and PTH-mediated PLD activity is dependent on small G-proteins of the Rho family. Diglycerides 0-14 protein kinase C, alpha Rattus norvegicus 77-80 15476589-5 2004 Diacylglycerol (DAG) generation from phospholipase D (PLD) is one pathway of PKC activation, and PTH-mediated PLD activity is dependent on small G-proteins of the Rho family. Diglycerides 16-19 protein kinase C, alpha Rattus norvegicus 77-80 15476589-12 2004 Rho seemed to be acting at a step before production of diacylglycerol (DAG), because the stimulation of PKCalpha translocation by the DAG mimetic phorbol 12,13 dibutyrate (PDBu) was unaffected by C. difficile toxin B or Y27632. Diglycerides 71-74 protein kinase C, alpha Rattus norvegicus 104-112 15476589-12 2004 Rho seemed to be acting at a step before production of diacylglycerol (DAG), because the stimulation of PKCalpha translocation by the DAG mimetic phorbol 12,13 dibutyrate (PDBu) was unaffected by C. difficile toxin B or Y27632. Diglycerides 134-137 protein kinase C, alpha Rattus norvegicus 104-112 12566467-2 2003 Because PKC beta2 can be activated by fatty acids and diacylglycerol, we hypothesized that altering the level and type of dietary fat might modulate cardiac PKC activation and stimulate hypertrophy in otherwise normal rat myocardium. Diglycerides 54-68 protein kinase C, alpha Rattus norvegicus 8-11 11576956-2 2001 Although PKC activation under hyperglycemia largely is related to an increase in de novo synthesis of diacylglycerol (DAG), activation of PKC can be regulated sensitively by oxidative stress. Diglycerides 102-116 protein kinase C, alpha Rattus norvegicus 9-12 11576956-2 2001 Although PKC activation under hyperglycemia largely is related to an increase in de novo synthesis of diacylglycerol (DAG), activation of PKC can be regulated sensitively by oxidative stress. Diglycerides 118-121 protein kinase C, alpha Rattus norvegicus 9-12 11576956-7 2001 DAG-dependent PKC isoforms PKC-alpha, PKC-betaI, PKC-betaII, PKC-delta, and PKC-epsilon and DAG-independent PKC-zeta all were detected in control rat glomeruli and tubules. Diglycerides 0-3 protein kinase C, alpha Rattus norvegicus 14-17 11576956-7 2001 DAG-dependent PKC isoforms PKC-alpha, PKC-betaI, PKC-betaII, PKC-delta, and PKC-epsilon and DAG-independent PKC-zeta all were detected in control rat glomeruli and tubules. Diglycerides 0-3 protein kinase C, alpha Rattus norvegicus 27-36 11095914-2 2000 Inositol 1,4,5 trisphosphate increases the intracellular Ca(2+)concentration ([Ca2(+)](i)) while diacylglycerol activates protein kinase C (PKC). Diglycerides 97-111 protein kinase C, alpha Rattus norvegicus 140-143