PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 23937324-1 2013 The regulation of protein kinase C (PKC) isoforms by ceramide is still controversial. Ceramides 53-61 protein kinase C alpha Homo sapiens 36-39 23937324-2 2013 In this work, the yeast Saccharomyces cerevisiae was used as a model to elucidate the effect of ceramide on the activity of mammalian PKC isoforms. Ceramides 96-104 protein kinase C alpha Homo sapiens 134-137 23937324-6 2013 Moreover, using a yeast-based assay previously developed for the screening of PKC inhibitors, it was also shown that, like the known PKC inhibitor NPC 15437, ceramide reduced the PMA-induced growth inhibition, supporting an inhibitory effect of ceramide on PKCdelta. Ceramides 158-166 protein kinase C alpha Homo sapiens 78-81 23937324-6 2013 Moreover, using a yeast-based assay previously developed for the screening of PKC inhibitors, it was also shown that, like the known PKC inhibitor NPC 15437, ceramide reduced the PMA-induced growth inhibition, supporting an inhibitory effect of ceramide on PKCdelta. Ceramides 158-166 protein kinase C alpha Homo sapiens 133-136 23937324-7 2013 Altogether, these results may indicate that ceramide distinctly interfere with the activity of PKCalpha, delta and zeta. Ceramides 44-52 protein kinase C alpha Homo sapiens 95-103 19029835-8 2009 These findings support a model in which activation of PKCalpha downregulates ATM, thus relieving CS repression by ATM and enhancing apoptosis via ceramide generation. Ceramides 146-154 protein kinase C alpha Homo sapiens 54-62 19127120-0 2009 Ceramide-mediated apoptosis following ionizing radiation in human prostate cancer cells: PKCalpha joins the fray. Ceramides 0-8 protein kinase C alpha Homo sapiens 89-97 17504762-0 2007 Mechanism of inhibition of sequestration of protein kinase C alpha/betaII by ceramide. Ceramides 77-85 protein kinase C alpha Homo sapiens 44-66 17504762-3 2007 In MCF-7 human breast cancer cells, the action of the PKC activator 4beta-phorbol-12-myristate-13-acetate (PMA) evokes ceramide formation, which in turn prevents PKCalpha/betaII translocation to the pericentrion. Ceramides 119-127 protein kinase C alpha Homo sapiens 54-57 17504762-3 2007 In MCF-7 human breast cancer cells, the action of the PKC activator 4beta-phorbol-12-myristate-13-acetate (PMA) evokes ceramide formation, which in turn prevents PKCalpha/betaII translocation to the pericentrion. Ceramides 119-127 protein kinase C alpha Homo sapiens 162-177 17504762-4 2007 In this study we investigated the mechanisms by which ceramide negatively regulates this translocation of PKCalpha/betaII. Ceramides 54-62 protein kinase C alpha Homo sapiens 106-121 17504762-6 2007 Inhibition of ceramide synthesis by fumonisin B1 overcame the defect in PKC phosphorylation and restored translocation of PKCalpha/betaII to the pericentrion. Ceramides 14-22 protein kinase C alpha Homo sapiens 72-75 17504762-6 2007 Inhibition of ceramide synthesis by fumonisin B1 overcame the defect in PKC phosphorylation and restored translocation of PKCalpha/betaII to the pericentrion. Ceramides 14-22 protein kinase C alpha Homo sapiens 122-130 17504762-10 2007 Reciprocally, a point mutation of Thr-641 to Glu, which mimics phosphorylation, in PKCbetaII overcame the inhibitory effects of ceramide on PKC translocation in PMA-stimulated MCF-7 cells. Ceramides 128-136 protein kinase C alpha Homo sapiens 83-86 17504762-11 2007 Therefore, the results demonstrate a novel role for carboxyl-terminal phosphorylation of PKCalpha/betaII in the translocation of PKC to the pericentrion, and they disclose specific regulation of PKC autophosphorylation by ceramide through the activation of specific isoforms of protein phosphatase 1. Ceramides 222-230 protein kinase C alpha Homo sapiens 89-104 17504762-11 2007 Therefore, the results demonstrate a novel role for carboxyl-terminal phosphorylation of PKCalpha/betaII in the translocation of PKC to the pericentrion, and they disclose specific regulation of PKC autophosphorylation by ceramide through the activation of specific isoforms of protein phosphatase 1. Ceramides 222-230 protein kinase C alpha Homo sapiens 89-92 17504762-11 2007 Therefore, the results demonstrate a novel role for carboxyl-terminal phosphorylation of PKCalpha/betaII in the translocation of PKC to the pericentrion, and they disclose specific regulation of PKC autophosphorylation by ceramide through the activation of specific isoforms of protein phosphatase 1. Ceramides 222-230 protein kinase C alpha Homo sapiens 129-132 16479073-0 2006 Ceramides and cell signaling molecules in psoriatic epidermis: reduced levels of ceramides, PKC-alpha, and JNK. Ceramides 0-9 protein kinase C alpha Homo sapiens 92-101 16479073-7 2006 The ceramide level was reduced significantly, and this was associated with the downregulation of apoptotic signaling molecules, such as PKC-alpha and JNK, in the lesional epidermis of psoriasis patients. Ceramides 4-12 protein kinase C alpha Homo sapiens 136-145 15322180-3 2004 We found that ceramide inhibited protein kinase C (PKC)-mediated activation of NF-kappaB. Ceramides 14-22 protein kinase C alpha Homo sapiens 51-54 15322180-4 2004 Ceramide was found to significantly reduce the kinase activity of PKCtheta as well as PKCalpha, the critical PKC isozymes involved in TCR-induced NF-kappaB activation. Ceramides 0-8 protein kinase C alpha Homo sapiens 86-94 15322180-4 2004 Ceramide was found to significantly reduce the kinase activity of PKCtheta as well as PKCalpha, the critical PKC isozymes involved in TCR-induced NF-kappaB activation. Ceramides 0-8 protein kinase C alpha Homo sapiens 66-69 15322180-8 2004 Inhibition of IL-2 production by ceramide was partially overcome when NF-kappaB nuclear translocation was reconstituted with activation of a PKC-independent pathway by TNF-alpha or when PKCtheta was overexpressed. Ceramides 33-41 protein kinase C alpha Homo sapiens 141-144 15322180-10 2004 These results indicate that ceramide plays a negative regulatory role in the activation of NF-kappaB and its targets as a result of inhibition of PKC. Ceramides 28-36 protein kinase C alpha Homo sapiens 146-149 14563411-1 2003 Ceramide is a lipid second messenger produced by sphingolipid metabolism in cells exposed to a limited number of agonists and in turn triggers important cell responses including protein kinase C (PKC)-alpha activation. Ceramides 0-8 protein kinase C alpha Homo sapiens 196-206 14563411-2 2003 Using a fusion protein comprising bovine PKCalpha and the green fluorescent protein (GFP), we transfected human embryonic kidney (HEK) cells and investigated to which subcellular compartment ceramide triggers PKCalpha redistribution. Ceramides 191-199 protein kinase C alpha Homo sapiens 209-217 14563411-3 2003 Stimulation of HEK cells with exogenous C16-ceramide or bacterial sphingomyelinase (bSMase), which leads to increased endogenous ceramide formation, evokes a translocation of PKCalpha to the Golgi compartment. Ceramides 44-52 protein kinase C alpha Homo sapiens 175-183 14563411-4 2003 By using deletion mutants of PKCalpha lacking distinct domains in the regulatory region, it is shown that the Ca(2+)-dependent lipid binding C2 domain, but not one of the C1 domains is essentially required for the ceramide-triggered translocation of PKCalpha to the Golgi complex. Ceramides 214-222 protein kinase C alpha Homo sapiens 29-37 14563411-4 2003 By using deletion mutants of PKCalpha lacking distinct domains in the regulatory region, it is shown that the Ca(2+)-dependent lipid binding C2 domain, but not one of the C1 domains is essentially required for the ceramide-triggered translocation of PKCalpha to the Golgi complex. Ceramides 214-222 protein kinase C alpha Homo sapiens 250-258 14563411-6 2003 In addition, evidence is provided that TPA requires only one of the two C1 subdomains to trigger translocation to the plasma membrane.In summary, our data provide evidence that ceramide either directly or indirectly interacts with the Ca(2+)-dependent lipid binding C2 domain of PKCalpha and thereby induces translocation of the enzyme to the Golgi compartment. Ceramides 177-185 protein kinase C alpha Homo sapiens 279-287 12699912-8 2003 Fumonisin B(1) (10 microM), sphinganine, sphingosine and ceramide (1 microM each) significantly repressed PKC-alpha and -delta isoforms at 48 h, whereas all the exogenously added sphingolipids significantly repressed PKC- epsilon and zeta similar to fumonisin B(1). Ceramides 57-65 protein kinase C alpha Homo sapiens 106-143 11480555-13 2001 Ceramide activation of protein phosphatases has been shown to promote inactivation of a number of pro-growth cellular regulators including the kinases PKC alpha and Akt, Bcl2 and the retinoblastoma protein. Ceramides 0-8 protein kinase C alpha Homo sapiens 151-160 11404253-0 2001 CTP:phosphocholine cytidylyltransferase inhibition by ceramide via PKC-alpha, p38 MAPK, cPLA2, and 5-lipoxygenase. Ceramides 54-62 protein kinase C alpha Homo sapiens 67-76 9657740-10 1998 Because ceramide has been shown to affect PKCalpha subcellular distribution, these data implicate a role for ceramide in mediating the rapid postirradiation translocation and inhibition of PKCalpha in TF-1 cells not rescued from apoptosis by GM-CSF. Ceramides 8-16 protein kinase C alpha Homo sapiens 42-50 9657740-10 1998 Because ceramide has been shown to affect PKCalpha subcellular distribution, these data implicate a role for ceramide in mediating the rapid postirradiation translocation and inhibition of PKCalpha in TF-1 cells not rescued from apoptosis by GM-CSF. Ceramides 109-117 protein kinase C alpha Homo sapiens 189-197 8798752-10 1996 Taken together, these data show that ceramide interferes with PKC-mediated activation of PLD. Ceramides 37-45 protein kinase C alpha Homo sapiens 62-65 8662781-3 1996 In Molt-4 cells, phorbol 12-myristate 13-acetate (PMA) induced retinoblastoma gene product (Rb) phosphorylation, and ceramide inhibited this effect, suggesting an inhibitory effect of ceramide on the protein kinase C (PKC) pathway, the primary target of PMA. Ceramides 117-125 protein kinase C alpha Homo sapiens 218-221 8662781-5 1996 To determine the effects of ceramide on PKC, we developed an immunoprecipitation assay for PKCalpha activity. Ceramides 28-36 protein kinase C alpha Homo sapiens 91-99 8662781-7 1996 Initial inhibition was observed as early as 4.5 h after treatment of cells with C6-ceramide, and the activity was completely lost by 13 h. Inhibition of PKCalpha activity was seen at concentrations of ceramide as low as 5 microM with maximal effects occurring at a concentration of 15 microM. Ceramides 83-91 protein kinase C alpha Homo sapiens 153-161 8662781-11 1996 Taken together, these results suggested that ceramide caused inactivation of PKCalpha. Ceramides 45-53 protein kinase C alpha Homo sapiens 77-85 8662781-12 1996 Since PKC requires phosphorylation for activity, we determined the effects of ceramide on phosphorylation of PKCalpha. Ceramides 78-86 protein kinase C alpha Homo sapiens 6-9 8662781-12 1996 Since PKC requires phosphorylation for activity, we determined the effects of ceramide on phosphorylation of PKCalpha. Ceramides 78-86 protein kinase C alpha Homo sapiens 109-117 8662781-14 1996 In addition, okadaic acid, a potent phosphatase inhibitor, slightly stimulated PKC activity and blocked the effects of ceramide on PKCalpha inhibition. Ceramides 119-127 protein kinase C alpha Homo sapiens 131-139 8662781-15 1996 These results demonstrate that ceramide causes inhibition/inactivation of PKCalpha and suggest these effects of ceramide may be mediated by a protein phosphatase. Ceramides 31-39 protein kinase C alpha Homo sapiens 74-82