PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 15250540-2 2004 The present study tested the hypothesis that lindane and the phorbol ester 12-O-tetradecanoylphorbol-13-acetate (TPA) inhibit gap junction communication in rat myometrial and liver WBr-F344 cells by the common mechanism of increasing phosphorylation of the gap junction protein connexin43. Tetradecanoylphorbol Acetate 75-111 gap junction protein, alpha 1 Rattus norvegicus 278-288 15250540-2 2004 The present study tested the hypothesis that lindane and the phorbol ester 12-O-tetradecanoylphorbol-13-acetate (TPA) inhibit gap junction communication in rat myometrial and liver WBr-F344 cells by the common mechanism of increasing phosphorylation of the gap junction protein connexin43. Tetradecanoylphorbol Acetate 113-116 gap junction protein, alpha 1 Rattus norvegicus 278-288 15250540-5 2004 However, TPA increased punctate immunofluorescence staining of phospho-connexin43 (S368) in myometrial cells whereas lindane had no such effect. Tetradecanoylphorbol Acetate 9-12 gap junction protein, alpha 1 Rattus norvegicus 71-81 15250540-8 2004 TPA intensified a slower migrating connexin43 band and increased phospho-connexin43 (S368) in immunoblots, and intensified phospho-connexin43 immunostaining at WBr-F344 cell interfaces and nuclear regions. Tetradecanoylphorbol Acetate 0-3 gap junction protein, alpha 1 Rattus norvegicus 35-45 15250540-8 2004 TPA intensified a slower migrating connexin43 band and increased phospho-connexin43 (S368) in immunoblots, and intensified phospho-connexin43 immunostaining at WBr-F344 cell interfaces and nuclear regions. Tetradecanoylphorbol Acetate 0-3 gap junction protein, alpha 1 Rattus norvegicus 73-83 15250540-8 2004 TPA intensified a slower migrating connexin43 band and increased phospho-connexin43 (S368) in immunoblots, and intensified phospho-connexin43 immunostaining at WBr-F344 cell interfaces and nuclear regions. Tetradecanoylphorbol Acetate 0-3 gap junction protein, alpha 1 Rattus norvegicus 73-83 11532878-0 2001 Role of PKC and MAP kinase in EGF- and TPA-induced connexin43 phosphorylation and inhibition of gap junction intercellular communication in rat liver epithelial cells. Tetradecanoylphorbol Acetate 39-42 gap junction protein, alpha 1 Rattus norvegicus 51-61 12807762-5 2003 TPA exposure of IAR20 cells induced hyperphosphorylation of gap junction protein connexin43 and inhibition of GJIC. Tetradecanoylphorbol Acetate 0-3 gap junction protein, alpha 1 Rattus norvegicus 81-91 12110373-9 2002 Such a delocalization of Cx43 proteins was not observed when TPA was coincubated with the flavonoids, (-)-epicatechin or genistein. Tetradecanoylphorbol Acetate 61-64 gap junction protein, alpha 1 Rattus norvegicus 25-29 12110373-10 2002 It is concluded that TPA affects Cx43 trafficking between cellular compartments, and that this effect is counteracted by (-)-epicatechin or genistein. Tetradecanoylphorbol Acetate 21-24 gap junction protein, alpha 1 Rattus norvegicus 33-37 11532878-4 2001 The induced inhibition of communication by TPA and EGF in IAR6.1 cells is associated with hyperphosphorylation of connexin43, the connexin responsible for GJIC. Tetradecanoylphorbol Acetate 43-46 gap junction protein, alpha 1 Rattus norvegicus 114-124 11532878-8 2001 Connexin43 hyperphosphorylation induced by TPA is, as for EGF, mediated through MAP kinase, while PKC seems to block GJIC either through other substrates or induces a type of connexin43 phosphorylation that causes no significant electrophoresis mobility shift. Tetradecanoylphorbol Acetate 43-46 gap junction protein, alpha 1 Rattus norvegicus 0-10 11181442-1 2001 12-O:-tetradecanoylphorbol-13-acetate (TPA) inhibits gap junctional communication in many cell culture systems, but TPA-induced phosphorylation of the gap junction protein connexin43 (Cx43) varies much between systems. Tetradecanoylphorbol Acetate 116-119 gap junction protein, alpha 1 Rattus norvegicus 172-182 11500965-0 2001 Inhibition of connexin43 gap junctional intercellular communication by TPA requires ERK activation. Tetradecanoylphorbol Acetate 71-74 gap junction protein, alpha 1 Rattus norvegicus 14-24 11500965-4 2001 TPA treatment (10 ng/ml for 30 min) of WB-F344 rat liver epithelial cells strongly activated p42 and p44 ERK-1 and -2, blocked gap junction-mediated fluorescent dye-coupling, and induced connexin43 hyperphosphorylation and gap junction internalization. Tetradecanoylphorbol Acetate 0-3 gap junction protein, alpha 1 Rattus norvegicus 187-197 11331935-6 2001 Phosphorylation of Cx43 was increased upon activation of protein kinase C (PKC) by 1 microM phorbol 12-myristate 13-acetate (PMA). Tetradecanoylphorbol Acetate 92-123 gap junction protein, alpha 1 Rattus norvegicus 19-23 11331935-6 2001 Phosphorylation of Cx43 was increased upon activation of protein kinase C (PKC) by 1 microM phorbol 12-myristate 13-acetate (PMA). Tetradecanoylphorbol Acetate 125-128 gap junction protein, alpha 1 Rattus norvegicus 19-23 11181442-1 2001 12-O:-tetradecanoylphorbol-13-acetate (TPA) inhibits gap junctional communication in many cell culture systems, but TPA-induced phosphorylation of the gap junction protein connexin43 (Cx43) varies much between systems. Tetradecanoylphorbol Acetate 116-119 gap junction protein, alpha 1 Rattus norvegicus 184-188 12064601-7 2001 Treatment with kinase activators, including epidermal growth factor (EGF) and the tumor promoting phorbol ester 12-O-tetradecanylphorbol-13-acetate (TPA), caused a shift in the mobility of the Cx43CT in a manner consistent with the mobility shift observed upon increased phosphorylation of endogenous Cx43. Tetradecanoylphorbol Acetate 149-152 gap junction protein, alpha 1 Rattus norvegicus 193-197 12064601-7 2001 Treatment with kinase activators, including epidermal growth factor (EGF) and the tumor promoting phorbol ester 12-O-tetradecanylphorbol-13-acetate (TPA), caused a shift in the mobility of the Cx43CT in a manner consistent with the mobility shift observed upon increased phosphorylation of endogenous Cx43. Tetradecanoylphorbol Acetate 149-152 gap junction protein, alpha 1 Rattus norvegicus 301-305 10754211-2 2000 12-O-tetradecanoylphorbol-13-acetate (TPA) and hydrogen peroxide, known as cancer promoters, inhibited GJIC in the epithelial cells as determined by the scrape loading/dye transfer assay, fluorescence redistribution assay after photobleaching, and immunofluorescent staining of connexin 43 using a laser confocal microscope. Tetradecanoylphorbol Acetate 0-36 gap junction protein, alpha 1 Rattus norvegicus 278-289 10973802-5 2000 This recovery of GJIC from TPA inhibition was partly correlated with hindered hyperphosphorylation of Cx43. Tetradecanoylphorbol Acetate 27-30 gap junction protein, alpha 1 Rattus norvegicus 102-106 10754211-2 2000 12-O-tetradecanoylphorbol-13-acetate (TPA) and hydrogen peroxide, known as cancer promoters, inhibited GJIC in the epithelial cells as determined by the scrape loading/dye transfer assay, fluorescence redistribution assay after photobleaching, and immunofluorescent staining of connexin 43 using a laser confocal microscope. Tetradecanoylphorbol Acetate 38-41 gap junction protein, alpha 1 Rattus norvegicus 278-289 9570757-2 1998 Since both agents also modulate gap junction (GJ)-mediated cell-cell communication, we have examined the effects of all-trans retinoic acid (RA) and 12-O-tetradecanoylphorbol-13-acetate (TPA) on the expression of alpha1 (Cx43) and beta2 (Cx26) connexins, the two major gap junction gene products in mature rat epidermis. Tetradecanoylphorbol Acetate 149-185 gap junction protein, alpha 1 Rattus norvegicus 221-225 8841092-6 1996 The phosphorylation pattern of cx 43 prepared from H60- or CS52-exposed cells was different from that prepared from 12-O-tetradecanoylphobol-13-acetate (TPA)-exposed cells after 1 hr treatment. Tetradecanoylphorbol Acetate 153-156 gap junction protein, alpha 1 Rattus norvegicus 31-36 9472709-5 1998 These results indicate that the inhibitory actions of TPA and PB on GJIC are cell-specific rather than connexin-specific and that TPA inhibits connexin43 and connexin32-mediated GJIC through a protein kinase C-dependent mechanism. Tetradecanoylphorbol Acetate 130-133 gap junction protein, alpha 1 Rattus norvegicus 143-153 9281445-6 1997 Consistent with their known properties, treatment with ST reduced, and combined treatment with TPA and ST increased, the level of 32P-incorporation into Cx43. Tetradecanoylphorbol Acetate 95-98 gap junction protein, alpha 1 Rattus norvegicus 153-157 9281445-7 1997 Two-dimensional tryptic phosphopeptide maps of 32P-labeled Cx43 indicated that a distinct subset of the phosphopeptides that are present under basal conditions were affected by ST or ST/TPA treatments, with TPA-induced phosphorylation occurring at the ST-sensitive sites. Tetradecanoylphorbol Acetate 186-189 gap junction protein, alpha 1 Rattus norvegicus 59-63 9281445-7 1997 Two-dimensional tryptic phosphopeptide maps of 32P-labeled Cx43 indicated that a distinct subset of the phosphopeptides that are present under basal conditions were affected by ST or ST/TPA treatments, with TPA-induced phosphorylation occurring at the ST-sensitive sites. Tetradecanoylphorbol Acetate 207-210 gap junction protein, alpha 1 Rattus norvegicus 59-63 7634409-6 1995 Examination of the mechanism of action of these redox-active compounds demonstrated correlations between their abilities to (i) prevent TPA-induced downregulation of GJIC, (ii) abolish the accumulation of intracellular oxidants and (iii) prevent the hyper-phosphorylation and internalization of connexin 43 in the cells. Tetradecanoylphorbol Acetate 136-139 gap junction protein, alpha 1 Rattus norvegicus 295-306 7586169-11 1995 Western blot analyses of TPA-treated WB-F344 or C10 cells revealed the presence of a hyperphosphorylated form of Cx43 (Cx43-P3) and no reduction in Cx43-P2, in contrast to BHT-treated cells. Tetradecanoylphorbol Acetate 25-28 gap junction protein, alpha 1 Rattus norvegicus 113-117 7586169-11 1995 Western blot analyses of TPA-treated WB-F344 or C10 cells revealed the presence of a hyperphosphorylated form of Cx43 (Cx43-P3) and no reduction in Cx43-P2, in contrast to BHT-treated cells. Tetradecanoylphorbol Acetate 25-28 gap junction protein, alpha 1 Rattus norvegicus 119-126 7586169-11 1995 Western blot analyses of TPA-treated WB-F344 or C10 cells revealed the presence of a hyperphosphorylated form of Cx43 (Cx43-P3) and no reduction in Cx43-P2, in contrast to BHT-treated cells. Tetradecanoylphorbol Acetate 25-28 gap junction protein, alpha 1 Rattus norvegicus 119-123 7982967-8 1994 The direct PKC activator, 12-O-tetradecanoylphorbol-13-acetate (TPA), induced phosphorylation of Cx43 that was completely blocked by the protein kinase C inhibitor, staurosporine. Tetradecanoylphorbol Acetate 26-62 gap junction protein, alpha 1 Rattus norvegicus 97-101 7982967-8 1994 The direct PKC activator, 12-O-tetradecanoylphorbol-13-acetate (TPA), induced phosphorylation of Cx43 that was completely blocked by the protein kinase C inhibitor, staurosporine. Tetradecanoylphorbol Acetate 64-67 gap junction protein, alpha 1 Rattus norvegicus 97-101 7806568-7 1994 Short term TPA treatment (< 30 min) increased phosphorylation of the gap junction protein molecular weight of 43,000 (Cx43), but did not change the cellular level of Cx43. Tetradecanoylphorbol Acetate 11-14 gap junction protein, alpha 1 Rattus norvegicus 121-125 8068183-5 1994 TPA induced the appearance of a fourth connexin 43-immunoreactive band (P3) and a concomitant decrease in the relative intensity of the unphosphorylated (P0) band within 5 min of treatment. Tetradecanoylphorbol Acetate 0-3 gap junction protein, alpha 1 Rattus norvegicus 39-50 8285856-11 1993 Relative abundance of different phosphorylated Cx43 forms was increased after 1 h exposure to DDT (10 micrograms) and 30 min exposure to TPA (0.1 microgram/ml). Tetradecanoylphorbol Acetate 137-140 gap junction protein, alpha 1 Rattus norvegicus 47-51 8020150-0 1994 Two inhibitors of gap junctional intercellular communication, TPA and endosulfan: different effects on phosphorylation of connexin 43 in the rat liver epithelial cell line, IAR 20. Tetradecanoylphorbol Acetate 62-65 gap junction protein, alpha 1 Rattus norvegicus 122-133 8020150-4 1994 The communication was partially restored after 4 h of TPA exposure and almost fully restored by 24 h, whereas in endosulfan-exposed cells the communication was completely down-regulated for the whole exposure-period of 24 h. Immunoblots of IAR 20 cell extracts indicated that TPA initially caused an increased phosphorylation of cx43. Tetradecanoylphorbol Acetate 276-279 gap junction protein, alpha 1 Rattus norvegicus 329-333 8020150-11 1994 TPA causes a marked hyperphosphorylation of cx43, whereas endosulfan increases phosphorylation initially only slightly but longer exposure-periods lead to hypophosphorylation. Tetradecanoylphorbol Acetate 0-3 gap junction protein, alpha 1 Rattus norvegicus 44-48 7925494-4 1993 We now report that gap junctions between C9 cells contain at least two junctional proteins, connexin26 (Cx26) and connexin43 (Cx43), and that the TPA-induced changes in IGJC correlate temporally to changes in the state of phosphorylation of Cx43. Tetradecanoylphorbol Acetate 146-149 gap junction protein, alpha 1 Rattus norvegicus 114-124 7925494-4 1993 We now report that gap junctions between C9 cells contain at least two junctional proteins, connexin26 (Cx26) and connexin43 (Cx43), and that the TPA-induced changes in IGJC correlate temporally to changes in the state of phosphorylation of Cx43. Tetradecanoylphorbol Acetate 146-149 gap junction protein, alpha 1 Rattus norvegicus 126-130 7925494-4 1993 We now report that gap junctions between C9 cells contain at least two junctional proteins, connexin26 (Cx26) and connexin43 (Cx43), and that the TPA-induced changes in IGJC correlate temporally to changes in the state of phosphorylation of Cx43. Tetradecanoylphorbol Acetate 146-149 gap junction protein, alpha 1 Rattus norvegicus 241-245 7925494-5 1993 The latter changes were prevented by inhibition of protein kinase C. Phosphoamino acid analysis and two-dimensional tryptic peptide maps of 32P-labeled Cx43 showed that during the TPA-induced phosphorylation at least two of the phosphorylated forms of Cx43 were differentially phosphorylated in seryl residues as compared to control. Tetradecanoylphorbol Acetate 180-183 gap junction protein, alpha 1 Rattus norvegicus 152-156 7925494-5 1993 The latter changes were prevented by inhibition of protein kinase C. Phosphoamino acid analysis and two-dimensional tryptic peptide maps of 32P-labeled Cx43 showed that during the TPA-induced phosphorylation at least two of the phosphorylated forms of Cx43 were differentially phosphorylated in seryl residues as compared to control. Tetradecanoylphorbol Acetate 180-183 gap junction protein, alpha 1 Rattus norvegicus 252-256 1651733-2 1991 The effects of TPA on connexin 43 expression in IAR 20 were investigated using northern blot analysis, western blot analysis, and an immunofluorescence technique. Tetradecanoylphorbol Acetate 15-18 gap junction protein, alpha 1 Rattus norvegicus 22-33 1651733-3 1991 Gap-junctional intercellular communication (GJIC) in this cell line decreased within 60 min of 12-O-tetradecanoylphorbol-13-acetate (TPA) treatment and recovered after 24 h. The number of immunofluorescence spots of connexin 43 on IAR 20 was closely related to the change in GJIC induced by TPA. Tetradecanoylphorbol Acetate 95-131 gap junction protein, alpha 1 Rattus norvegicus 216-227 1651733-5 1991 Moreover, connexin 43 protein expression analyzed by western blotting suggests that connexin 43 proteins were still present in TPA-treated cells at a similar level. Tetradecanoylphorbol Acetate 127-130 gap junction protein, alpha 1 Rattus norvegicus 10-21 1651733-5 1991 Moreover, connexin 43 protein expression analyzed by western blotting suggests that connexin 43 proteins were still present in TPA-treated cells at a similar level. Tetradecanoylphorbol Acetate 127-130 gap junction protein, alpha 1 Rattus norvegicus 84-95 1651733-6 1991 These results suggest that GJIC of these rat liver epithelial cells was mediated by connexin 43 protein and that TPA inhibited GJIC by inhibiting posttranslational processing of connexin 43 proteins, e.g., localization or assembly. Tetradecanoylphorbol Acetate 113-116 gap junction protein, alpha 1 Rattus norvegicus 178-189 32956670-6 2020 In HeLaCx43 cells treated with PMA to activate Pyk2, a decrease in Cx43 GJ intercellular communication (GJIC) was observed when assayed by dye transfer. Tetradecanoylphorbol Acetate 31-34 gap junction protein, alpha 1 Rattus norvegicus 7-11 32956670-9 2020 The ability of Pyk2 and Src inhibitors to restore Cx43 function in the presence of PMA was also observed in NRVMs. Tetradecanoylphorbol Acetate 83-86 gap junction protein, alpha 1 Rattus norvegicus 50-54 21692984-11 2012 Addition of the PKC activator, phorbol 12-myristate 13-acetate and the specific PKC(epsilon) agonist, carbachol, blocked the effects of nicorandil on connexin43 phosphorylation and dye permeability. Tetradecanoylphorbol Acetate 31-62 gap junction protein, alpha 1 Rattus norvegicus 150-160 25625661-6 2015 Phorbol-12-myristate-13-acetate (PMA), a specific PKC activator, partially reversed the FZD-induced mitochondrial Cx43 dephosphorylation at serine 368 and mitochondrial dysfunction in the cardiomyocytes. Tetradecanoylphorbol Acetate 0-31 gap junction protein, alpha 1 Rattus norvegicus 114-118 25625661-6 2015 Phorbol-12-myristate-13-acetate (PMA), a specific PKC activator, partially reversed the FZD-induced mitochondrial Cx43 dephosphorylation at serine 368 and mitochondrial dysfunction in the cardiomyocytes. Tetradecanoylphorbol Acetate 33-36 gap junction protein, alpha 1 Rattus norvegicus 114-118 20406988-3 2010 We now show that rat epidermal keratinocytes (REK) that are reduced in Cx43 present features of epithelial-to-mesenchymal transition and are more invasive than their control counterparts, whereas overexpression of Cx43 inhibited the 12-O-tetradecanoyl-phorbol-13-acetate (TPA)- and epidermal growth factor (EGF)-induced invasive properties. Tetradecanoylphorbol Acetate 233-270 gap junction protein, alpha 1 Rattus norvegicus 214-218 21173226-4 2011 Histological analysis showed high connexin 43 coupling, few inflammatory cells, and low fibrotic markers in myocardium implanted with these phorbol myristate acetate-activated MSCs. Tetradecanoylphorbol Acetate 140-165 gap junction protein, alpha 1 Rattus norvegicus 34-45 20406988-3 2010 We now show that rat epidermal keratinocytes (REK) that are reduced in Cx43 present features of epithelial-to-mesenchymal transition and are more invasive than their control counterparts, whereas overexpression of Cx43 inhibited the 12-O-tetradecanoyl-phorbol-13-acetate (TPA)- and epidermal growth factor (EGF)-induced invasive properties. Tetradecanoylphorbol Acetate 272-275 gap junction protein, alpha 1 Rattus norvegicus 214-218 18601906-6 2008 Treatment of IAR20 rat liver epithelial cells with 12-O-tetradecanoylphorbol 13-acetate (TPA) or epidermal growth factor (EGF) caused a rapid increase in the solubility of Cx43 in Triton X-100. Tetradecanoylphorbol Acetate 51-87 gap junction protein, alpha 1 Rattus norvegicus 172-176 18601906-6 2008 Treatment of IAR20 rat liver epithelial cells with 12-O-tetradecanoylphorbol 13-acetate (TPA) or epidermal growth factor (EGF) caused a rapid increase in the solubility of Cx43 in Triton X-100. Tetradecanoylphorbol Acetate 89-92 gap junction protein, alpha 1 Rattus norvegicus 172-176 18601906-8 2008 The data suggest that loss of the detergent resistance of Cx43 is an early step in TPA- and EGF-induced endocytosis of gap junctions. Tetradecanoylphorbol Acetate 83-86 gap junction protein, alpha 1 Rattus norvegicus 58-62 18601906-0 2008 The detergent resistance of Connexin43 is lost upon TPA or EGF treatment and is an early step in gap junction endocytosis. Tetradecanoylphorbol Acetate 52-55 gap junction protein, alpha 1 Rattus norvegicus 28-38 16685461-7 2006 Western blot analysis of connexin 43 in a membrane-enriched fraction of WB-F344 cells treated with thioridazine revealed decreased amounts of unphosphorylated connexin 43, and appearance of a phosphorylated connexin 43 band that co-migrated with a "hyperphosphorylated" connexin 43 band present in TPA-inhibited cells. Tetradecanoylphorbol Acetate 298-301 gap junction protein, alpha 1 Rattus norvegicus 25-36 15561096-0 2005 Connexin43 synthesis, phosphorylation, and degradation in regulation of transient inhibition of gap junction intercellular communication by the phorbol ester TPA in rat liver epithelial cells. Tetradecanoylphorbol Acetate 158-161 gap junction protein, alpha 1 Rattus norvegicus 0-10 15561096-4 2005 The data presented suggest that restoration of GJIC during continuous TPA exposure in normal and transformed rat liver epithelial cells is dependent on synthesis of Cx43 protein, as well as the transport of already synthesized Cx43 from intracellular pools to the plasma membrane. Tetradecanoylphorbol Acetate 70-73 gap junction protein, alpha 1 Rattus norvegicus 165-169 15561096-4 2005 The data presented suggest that restoration of GJIC during continuous TPA exposure in normal and transformed rat liver epithelial cells is dependent on synthesis of Cx43 protein, as well as the transport of already synthesized Cx43 from intracellular pools to the plasma membrane. Tetradecanoylphorbol Acetate 70-73 gap junction protein, alpha 1 Rattus norvegicus 227-231 15561096-6 2005 Both PKC and MAP kinase is involved in TPA-induced degradation of Cx43 and inhibition of GJIC. Tetradecanoylphorbol Acetate 39-42 gap junction protein, alpha 1 Rattus norvegicus 66-70 15561096-8 2005 Together, the present data highlight Cx43 degradation and synthesis as critical determinants in TPA-induced modifications of cell-cell communication via gap junctions. Tetradecanoylphorbol Acetate 96-99 gap junction protein, alpha 1 Rattus norvegicus 37-41 15371442-0 2004 Ubiquitination and down-regulation of gap junction protein connexin-43 in response to 12-O-tetradecanoylphorbol 13-acetate treatment. Tetradecanoylphorbol Acetate 86-122 gap junction protein, alpha 1 Rattus norvegicus 59-70 15371442-3 2004 In the present study, we show that the tumor-promoting phorbol ester 12-O-tetradecanoylphorbol 13-acetate (TPA) induces ubiquitination of connexin-43 (Cx43) in IAR20 rat liver epithelial cells. Tetradecanoylphorbol Acetate 69-105 gap junction protein, alpha 1 Rattus norvegicus 138-149 15371442-3 2004 In the present study, we show that the tumor-promoting phorbol ester 12-O-tetradecanoylphorbol 13-acetate (TPA) induces ubiquitination of connexin-43 (Cx43) in IAR20 rat liver epithelial cells. Tetradecanoylphorbol Acetate 69-105 gap junction protein, alpha 1 Rattus norvegicus 151-155 15371442-3 2004 In the present study, we show that the tumor-promoting phorbol ester 12-O-tetradecanoylphorbol 13-acetate (TPA) induces ubiquitination of connexin-43 (Cx43) in IAR20 rat liver epithelial cells. Tetradecanoylphorbol Acetate 107-110 gap junction protein, alpha 1 Rattus norvegicus 138-149 15371442-3 2004 In the present study, we show that the tumor-promoting phorbol ester 12-O-tetradecanoylphorbol 13-acetate (TPA) induces ubiquitination of connexin-43 (Cx43) in IAR20 rat liver epithelial cells. Tetradecanoylphorbol Acetate 107-110 gap junction protein, alpha 1 Rattus norvegicus 151-155 15371442-4 2004 The accelerated ubiquitination of Cx43 in response to TPA occurred concomitantly with Cx43 hyperphosphorylation and inhibition of cell-cell communication via gap junctions. Tetradecanoylphorbol Acetate 54-57 gap junction protein, alpha 1 Rattus norvegicus 34-38 15371442-4 2004 The accelerated ubiquitination of Cx43 in response to TPA occurred concomitantly with Cx43 hyperphosphorylation and inhibition of cell-cell communication via gap junctions. Tetradecanoylphorbol Acetate 54-57 gap junction protein, alpha 1 Rattus norvegicus 86-90 15371442-5 2004 The TPA-induced ubiquitination of Cx43 was mediated via protein kinase C and partly involved the mitogen-activated protein kinase pathway. Tetradecanoylphorbol Acetate 4-7 gap junction protein, alpha 1 Rattus norvegicus 34-38 15371442-9 2004 Evidence is provided that Cx43 is modified by multiple monoubiquitins rather than a polyubiquitin chain in response to TPA. Tetradecanoylphorbol Acetate 119-122 gap junction protein, alpha 1 Rattus norvegicus 26-30 15371442-10 2004 Moreover, the TPA-induced ubiquitination of Cx43 was blocked by proteasomal inhibitors. Tetradecanoylphorbol Acetate 14-17 gap junction protein, alpha 1 Rattus norvegicus 44-48