PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 28671468-2 2017 PKC is regulated by binding of the second messenger sn-1,2-diacylglycerol (DAG) to its tandem C1 domains, designated C1a and C1b, leading both to PKC activation and to its translocation to the plasma membrane and to internal organelles. Diglycerides 75-78 proline rich transmembrane protein 2 Homo sapiens 0-3 32345612-3 2020 Diacylglycerol (DAG), the product of the PLC-catalyzed PI(4,5)P2 hydrolysis, activates protein kinase C (PKC). Diglycerides 0-14 proline rich transmembrane protein 2 Homo sapiens 87-103 32345612-3 2020 Diacylglycerol (DAG), the product of the PLC-catalyzed PI(4,5)P2 hydrolysis, activates protein kinase C (PKC). Diglycerides 0-14 proline rich transmembrane protein 2 Homo sapiens 105-108 32345612-3 2020 Diacylglycerol (DAG), the product of the PLC-catalyzed PI(4,5)P2 hydrolysis, activates protein kinase C (PKC). Diglycerides 16-19 proline rich transmembrane protein 2 Homo sapiens 87-103 32345612-3 2020 Diacylglycerol (DAG), the product of the PLC-catalyzed PI(4,5)P2 hydrolysis, activates protein kinase C (PKC). Diglycerides 16-19 proline rich transmembrane protein 2 Homo sapiens 105-108 29513138-2 2018 For conventional and novel isozymes, this is effected by binding the lipid second messenger, diacylglycerol, but for atypical PKC isozymes, this is effected by binding protein scaffolds. Diglycerides 93-107 proline rich transmembrane protein 2 Homo sapiens 126-129 29513138-3 2018 PKC shot into the limelight following the discovery in the 1980s that the diacylglycerol-sensitive isozymes are "receptors" for the potent tumor-promoting phorbol esters. Diglycerides 74-88 proline rich transmembrane protein 2 Homo sapiens 0-3 33617877-8 2021 Overexpression of a PKC regulatory domain fusion suppressed both basal and agonist-induced endogenous PKC activity, acting in a dominant-negative manner by competing for diacylglycerol. Diglycerides 170-184 proline rich transmembrane protein 2 Homo sapiens 20-23 33617877-8 2021 Overexpression of a PKC regulatory domain fusion suppressed both basal and agonist-induced endogenous PKC activity, acting in a dominant-negative manner by competing for diacylglycerol. Diglycerides 170-184 proline rich transmembrane protein 2 Homo sapiens 102-105 32466765-0 2020 Diacylglycerol-evoked activation of PKC and PKD isoforms in regulation of glucose and lipid metabolism: a review. Diglycerides 0-14 proline rich transmembrane protein 2 Homo sapiens 36-39 32466765-1 2020 Protein kinase C (PKC) and Protein kinase D (PKD) isoforms can sense diacylglycerol (DAG) generated in the different cellular compartments in various physiological processes. Diglycerides 69-83 proline rich transmembrane protein 2 Homo sapiens 0-16 32466765-1 2020 Protein kinase C (PKC) and Protein kinase D (PKD) isoforms can sense diacylglycerol (DAG) generated in the different cellular compartments in various physiological processes. Diglycerides 69-83 proline rich transmembrane protein 2 Homo sapiens 18-21 32466765-1 2020 Protein kinase C (PKC) and Protein kinase D (PKD) isoforms can sense diacylglycerol (DAG) generated in the different cellular compartments in various physiological processes. Diglycerides 85-88 proline rich transmembrane protein 2 Homo sapiens 0-16 32466765-1 2020 Protein kinase C (PKC) and Protein kinase D (PKD) isoforms can sense diacylglycerol (DAG) generated in the different cellular compartments in various physiological processes. Diglycerides 85-88 proline rich transmembrane protein 2 Homo sapiens 18-21 32466765-4 2020 DAG-sensing PKC and PKD isoforms play a crucial role in the regulation of metabolic homeostasis and therefore might serve as targets for the treatment of metabolic disorders such as obesity and diabetes. Diglycerides 0-3 proline rich transmembrane protein 2 Homo sapiens 12-15 28671468-2 2017 PKC is regulated by binding of the second messenger sn-1,2-diacylglycerol (DAG) to its tandem C1 domains, designated C1a and C1b, leading both to PKC activation and to its translocation to the plasma membrane and to internal organelles. Diglycerides 75-78 proline rich transmembrane protein 2 Homo sapiens 146-149 28112438-2 2017 As major cellular targets for the phorbol ester tumor promoters and diacylglycerol (DAG), a second messenger generated by stimulation of membrane receptors, PKC isozymes play major roles in the control of signaling pathways associated with proliferation, migration, invasion, tumorigenesis, and metastasis. Diglycerides 68-82 proline rich transmembrane protein 2 Homo sapiens 157-160 28112438-2 2017 As major cellular targets for the phorbol ester tumor promoters and diacylglycerol (DAG), a second messenger generated by stimulation of membrane receptors, PKC isozymes play major roles in the control of signaling pathways associated with proliferation, migration, invasion, tumorigenesis, and metastasis. Diglycerides 84-87 proline rich transmembrane protein 2 Homo sapiens 157-160 23818610-2 2013 This polarization response is driven by the localized accumulation of diacylglycerol, which recruits multiple protein kinase (PK)C isozymes to the synaptic membrane. Diglycerides 70-84 proline rich transmembrane protein 2 Homo sapiens 126-130 26420215-4 2015 Activation of protein kinase C (PKC) by the diacylglycerol mimic phorbol-myristic acid resulted in specific and dose-responsive increases in APOBEC3B expression and activity, which could then be strongly suppressed by PKC or NF-kappaB inhibition. Diglycerides 44-58 proline rich transmembrane protein 2 Homo sapiens 14-30 26420215-4 2015 Activation of protein kinase C (PKC) by the diacylglycerol mimic phorbol-myristic acid resulted in specific and dose-responsive increases in APOBEC3B expression and activity, which could then be strongly suppressed by PKC or NF-kappaB inhibition. Diglycerides 44-58 proline rich transmembrane protein 2 Homo sapiens 32-35 26420215-4 2015 Activation of protein kinase C (PKC) by the diacylglycerol mimic phorbol-myristic acid resulted in specific and dose-responsive increases in APOBEC3B expression and activity, which could then be strongly suppressed by PKC or NF-kappaB inhibition. Diglycerides 44-58 proline rich transmembrane protein 2 Homo sapiens 218-221 32714576-5 2017 This review presents an overview of signaling by diacylglycerol (DG)-dependent PKC isozymes in the brain, and focuses on the role of the Ca2+-sensitive conventional PKC isozymes in neurodegeneration. Diglycerides 49-63 proline rich transmembrane protein 2 Homo sapiens 79-82 27994151-4 2017 PKC inhibition or the exchange of threonine for alanine in the C-terminal PDZ-binding motif conferred DAG sensitivity to the channel. Diglycerides 102-105 proline rich transmembrane protein 2 Homo sapiens 0-3 22188925-4 2012 Here, agonist-dependent increases in diacylglycerol accumulation lead to the activation of protein kinase C (PKC) and PKC-dependent phosphorylation of PKD1 at two highly conserved serine residues in the activation loop; this modification increases PKD1 catalytic activity, as assessed by PKD1 autophosphorylation at a consensus phosphorylation motif at the extreme C terminus. Diglycerides 37-51 proline rich transmembrane protein 2 Homo sapiens 91-107 23514610-6 2013 LY333531 blocked NET induction by the diacylglycerol analogue OAG (conventional PKC activator) (p<0.001). Diglycerides 38-52 proline rich transmembrane protein 2 Homo sapiens 80-83 22520069-1 2012 In patients with diabetes, hyperglycemia is known to promote high levels of diacylglycerol which activates protein kinase C (PKC) in the vascular tissues and leads to the production of vascular endothelial growth factor (VEGF) in the retina. Diglycerides 76-90 proline rich transmembrane protein 2 Homo sapiens 107-123 22520069-1 2012 In patients with diabetes, hyperglycemia is known to promote high levels of diacylglycerol which activates protein kinase C (PKC) in the vascular tissues and leads to the production of vascular endothelial growth factor (VEGF) in the retina. Diglycerides 76-90 proline rich transmembrane protein 2 Homo sapiens 125-128 23249278-0 2013 A functional interaction between TRPC/NCKX induced by DAG plays a role in determining calcium influx independently from PKC activation. Diglycerides 54-57 proline rich transmembrane protein 2 Homo sapiens 120-123 22609963-0 2012 Diacylglycerol stimulates acrosomal exocytosis by feeding into a PKC- and PLD1-dependent positive loop that continuously supplies phosphatidylinositol 4,5-bisphosphate. Diglycerides 0-14 proline rich transmembrane protein 2 Homo sapiens 65-68 22609963-5 2012 Addition of diacylglycerol promotes the PKC-dependent activation of PLD1. Diglycerides 12-26 proline rich transmembrane protein 2 Homo sapiens 40-43 22188925-4 2012 Here, agonist-dependent increases in diacylglycerol accumulation lead to the activation of protein kinase C (PKC) and PKC-dependent phosphorylation of PKD1 at two highly conserved serine residues in the activation loop; this modification increases PKD1 catalytic activity, as assessed by PKD1 autophosphorylation at a consensus phosphorylation motif at the extreme C terminus. Diglycerides 37-51 proline rich transmembrane protein 2 Homo sapiens 109-112 22188925-4 2012 Here, agonist-dependent increases in diacylglycerol accumulation lead to the activation of protein kinase C (PKC) and PKC-dependent phosphorylation of PKD1 at two highly conserved serine residues in the activation loop; this modification increases PKD1 catalytic activity, as assessed by PKD1 autophosphorylation at a consensus phosphorylation motif at the extreme C terminus. Diglycerides 37-51 proline rich transmembrane protein 2 Homo sapiens 118-121 30934385-5 2010 All of these properties are abnormal in diabetes and are correlated with increased diacylglycerol-PKC pathway and PKCalpha, beta1/2 and delta isoforms activation in the retina, aorta, heart and renal glomeruli. Diglycerides 83-97 proline rich transmembrane protein 2 Homo sapiens 98-101 19934406-5 2010 This review introduces the PKC family and then focuses on recent advances in understanding the cellular regulation of its diacylglycerol-regulated members. Diglycerides 122-136 proline rich transmembrane protein 2 Homo sapiens 27-30 21975067-2 2011 The endogenous PKC activator diacylglycerol contains two long carbon chains, which are attached to the glycerol moiety via ester linkage. Diglycerides 29-43 proline rich transmembrane protein 2 Homo sapiens 15-18 20715268-1 2010 Synthetic diacylglycerol-lactones (DAG-lactones) are effective modulators of critical cellular signaling pathways, downstream of the lipophilic second messenger diacylglycerol, that activate a host of protein kinase C (PKC) isozymes and other nonkinase proteins that share similar C1 membrane-targeting domains with PKC. Diglycerides 10-24 proline rich transmembrane protein 2 Homo sapiens 201-217 20715268-1 2010 Synthetic diacylglycerol-lactones (DAG-lactones) are effective modulators of critical cellular signaling pathways, downstream of the lipophilic second messenger diacylglycerol, that activate a host of protein kinase C (PKC) isozymes and other nonkinase proteins that share similar C1 membrane-targeting domains with PKC. Diglycerides 10-24 proline rich transmembrane protein 2 Homo sapiens 219-222 20715268-1 2010 Synthetic diacylglycerol-lactones (DAG-lactones) are effective modulators of critical cellular signaling pathways, downstream of the lipophilic second messenger diacylglycerol, that activate a host of protein kinase C (PKC) isozymes and other nonkinase proteins that share similar C1 membrane-targeting domains with PKC. Diglycerides 10-24 proline rich transmembrane protein 2 Homo sapiens 316-319 20715268-1 2010 Synthetic diacylglycerol-lactones (DAG-lactones) are effective modulators of critical cellular signaling pathways, downstream of the lipophilic second messenger diacylglycerol, that activate a host of protein kinase C (PKC) isozymes and other nonkinase proteins that share similar C1 membrane-targeting domains with PKC. Diglycerides 161-175 proline rich transmembrane protein 2 Homo sapiens 201-217 20715268-1 2010 Synthetic diacylglycerol-lactones (DAG-lactones) are effective modulators of critical cellular signaling pathways, downstream of the lipophilic second messenger diacylglycerol, that activate a host of protein kinase C (PKC) isozymes and other nonkinase proteins that share similar C1 membrane-targeting domains with PKC. Diglycerides 161-175 proline rich transmembrane protein 2 Homo sapiens 219-222 20715268-1 2010 Synthetic diacylglycerol-lactones (DAG-lactones) are effective modulators of critical cellular signaling pathways, downstream of the lipophilic second messenger diacylglycerol, that activate a host of protein kinase C (PKC) isozymes and other nonkinase proteins that share similar C1 membrane-targeting domains with PKC. Diglycerides 161-175 proline rich transmembrane protein 2 Homo sapiens 316-319 19961537-1 2010 Synthetic diacylglycerol lactones (DAG lactones) are effective modulators of critical cellular signaling pathways downstream of the lipophilic second messenger diacylglycerol that activate a host of protein kinase C (PKC) isozymes as well as other non-kinase proteins that share with PKC similar C1 membrane-targeting domains. Diglycerides 10-24 proline rich transmembrane protein 2 Homo sapiens 199-215 19961537-1 2010 Synthetic diacylglycerol lactones (DAG lactones) are effective modulators of critical cellular signaling pathways downstream of the lipophilic second messenger diacylglycerol that activate a host of protein kinase C (PKC) isozymes as well as other non-kinase proteins that share with PKC similar C1 membrane-targeting domains. Diglycerides 10-24 proline rich transmembrane protein 2 Homo sapiens 217-220 19961537-1 2010 Synthetic diacylglycerol lactones (DAG lactones) are effective modulators of critical cellular signaling pathways downstream of the lipophilic second messenger diacylglycerol that activate a host of protein kinase C (PKC) isozymes as well as other non-kinase proteins that share with PKC similar C1 membrane-targeting domains. Diglycerides 10-24 proline rich transmembrane protein 2 Homo sapiens 284-287 18326666-0 2008 Amplification of diacylglycerol activation of protein kinase C by cholesterol. Diglycerides 17-31 proline rich transmembrane protein 2 Homo sapiens 46-62 18514071-1 2008 Ras association domain family 1A (RASSF1A) is a tumour suppressor that contains an amino-terminal cysteine-rich region, similar to the diacylglycerol (DAG)-binding domain (C1 domain) found in the protein kinase C (PKC) family of proteins, and a carboxy-terminal Ras-association (RA) domain. Diglycerides 135-149 proline rich transmembrane protein 2 Homo sapiens 196-212 18514071-1 2008 Ras association domain family 1A (RASSF1A) is a tumour suppressor that contains an amino-terminal cysteine-rich region, similar to the diacylglycerol (DAG)-binding domain (C1 domain) found in the protein kinase C (PKC) family of proteins, and a carboxy-terminal Ras-association (RA) domain. Diglycerides 135-149 proline rich transmembrane protein 2 Homo sapiens 214-217 18514071-1 2008 Ras association domain family 1A (RASSF1A) is a tumour suppressor that contains an amino-terminal cysteine-rich region, similar to the diacylglycerol (DAG)-binding domain (C1 domain) found in the protein kinase C (PKC) family of proteins, and a carboxy-terminal Ras-association (RA) domain. Diglycerides 151-154 proline rich transmembrane protein 2 Homo sapiens 196-212 18514071-1 2008 Ras association domain family 1A (RASSF1A) is a tumour suppressor that contains an amino-terminal cysteine-rich region, similar to the diacylglycerol (DAG)-binding domain (C1 domain) found in the protein kinase C (PKC) family of proteins, and a carboxy-terminal Ras-association (RA) domain. Diglycerides 151-154 proline rich transmembrane protein 2 Homo sapiens 214-217 19628710-2 2009 Whereas protein kinase C (PKC) family members were discovered as the targets of DAG, little is known about the molecular identity of the main Ca(2+) sensor(s). Diglycerides 80-83 proline rich transmembrane protein 2 Homo sapiens 26-29 18326666-1 2008 The combined effects of cholesterol, a major cell membrane component, and the lipid second messenger diacylglycerol on the activity of protein kinase C (PK-C) and the structure of phosphatidylcholine/phosphatidylserine bilayers were investigated using specific PK-C assays and (2)H NMR. Diglycerides 101-115 proline rich transmembrane protein 2 Homo sapiens 135-151 18326666-1 2008 The combined effects of cholesterol, a major cell membrane component, and the lipid second messenger diacylglycerol on the activity of protein kinase C (PK-C) and the structure of phosphatidylcholine/phosphatidylserine bilayers were investigated using specific PK-C assays and (2)H NMR. Diglycerides 101-115 proline rich transmembrane protein 2 Homo sapiens 153-157 18326666-2 2008 Whereas the classical activation of PK-C was observed as an effect of diacylglycerol, in the absence of this second messenger, cholesterol did not affect PK-C activity. Diglycerides 70-84 proline rich transmembrane protein 2 Homo sapiens 36-40 18326666-3 2008 A novel effect of amplified PK-C activation was observed in the presence of both cholesterol and diacylglycerol concentrations within the physiological range of each of these components. Diglycerides 97-111 proline rich transmembrane protein 2 Homo sapiens 28-32 17442248-4 2007 First, we confirm that DAG analogs indeed continue to potentiate transmission after PKC inhibition (the Munc13 pathway), but only in neurons that previously experienced DAG analogs, before PKC inhibition started. Diglycerides 23-26 proline rich transmembrane protein 2 Homo sapiens 84-87 17583896-6 2007 Although diacylglycerol is an activator of protein kinase C (PKC) in mammalian cells, there is some question about activation of fungal PKCs. Diglycerides 9-23 proline rich transmembrane protein 2 Homo sapiens 43-59 17583896-6 2007 Although diacylglycerol is an activator of protein kinase C (PKC) in mammalian cells, there is some question about activation of fungal PKCs. Diglycerides 9-23 proline rich transmembrane protein 2 Homo sapiens 61-64 17583896-7 2007 A mutant strain deleted for PKC1 responded to farnesol and the diacylglycerol analogue similar to wild-type, suggesting that PKC is not the target of the diacylglycerol analogue. Diglycerides 63-77 proline rich transmembrane protein 2 Homo sapiens 28-31 17442248-8 2007 These data show that activation of both PKC-dependent and -independent pathways (via Munc13) are required for DAG-induced potentiation. Diglycerides 110-113 proline rich transmembrane protein 2 Homo sapiens 40-43 17007743-1 2006 AIM: Protein kinase C (PKC) is as a family of serine/threonine kinases that can be activated by Ca2+, phospholipid and diacylglycerol. Diglycerides 119-133 proline rich transmembrane protein 2 Homo sapiens 5-21 17380065-9 2007 One important pathomechanism in the development of diabetic retinopathy is the activation of PKC induced by high glucose due to an increased diacylglycerol level. Diglycerides 141-155 proline rich transmembrane protein 2 Homo sapiens 93-96 17245085-6 2007 One important pathomechanism in the development of diabetic retinopathy is the activation of PKC induced by high glucose due to an increased diacylglycerol level. Diglycerides 141-155 proline rich transmembrane protein 2 Homo sapiens 93-96 17007743-1 2006 AIM: Protein kinase C (PKC) is as a family of serine/threonine kinases that can be activated by Ca2+, phospholipid and diacylglycerol. Diglycerides 119-133 proline rich transmembrane protein 2 Homo sapiens 23-26 15765405-6 2005 DCA also caused dramatic translocation of PH-PLCdelta-GFP, and conventional, Ca2+/diacylglycerol (DAG)-dependent isoforms of PKC (PKC-betaI and PKC-alpha), and MARCKS-GFP, but only in Ca2+-containing solutions. Diglycerides 82-96 proline rich transmembrane protein 2 Homo sapiens 125-128 15924269-1 2005 Diacylglycerol (DAG) was discovered as a potent lipid second messenger with protein kinase C (PKC) as its major cellular target more than 25 years ago. Diglycerides 0-14 proline rich transmembrane protein 2 Homo sapiens 76-92 15924269-1 2005 Diacylglycerol (DAG) was discovered as a potent lipid second messenger with protein kinase C (PKC) as its major cellular target more than 25 years ago. Diglycerides 0-14 proline rich transmembrane protein 2 Homo sapiens 94-97 15924269-1 2005 Diacylglycerol (DAG) was discovered as a potent lipid second messenger with protein kinase C (PKC) as its major cellular target more than 25 years ago. Diglycerides 16-19 proline rich transmembrane protein 2 Homo sapiens 76-92 15924269-1 2005 Diacylglycerol (DAG) was discovered as a potent lipid second messenger with protein kinase C (PKC) as its major cellular target more than 25 years ago. Diglycerides 16-19 proline rich transmembrane protein 2 Homo sapiens 94-97 15924269-3 2005 Multiple layers of regulation exist among PKC- and DAG-metabolizing enzymes such as phosphatidylcholine (PC)-specific phospholipase D, and cross-talk exists between the glycerolipid and sphingolipid pathways, with PKC at the center. Diglycerides 51-54 proline rich transmembrane protein 2 Homo sapiens 214-217 15924269-4 2005 Currently, there is intense interest in the question of whether DAG derived from PC can function as a lipid second messenger and regulate PKC analogous to DAG derived from phosphatidylinositol-4,5-bisphosphate (PIP2). Diglycerides 64-67 proline rich transmembrane protein 2 Homo sapiens 138-141 15986138-1 2005 Protein kinase C (PKC) is activated by diacylglycerol generated by receptor-mediated hydrolysis of membrane phospholipids to mediate signals for cell growth and plays as a target of tumor-promoting phorbol esters in malignant transformation. Diglycerides 39-53 proline rich transmembrane protein 2 Homo sapiens 0-16 15986138-1 2005 Protein kinase C (PKC) is activated by diacylglycerol generated by receptor-mediated hydrolysis of membrane phospholipids to mediate signals for cell growth and plays as a target of tumor-promoting phorbol esters in malignant transformation. Diglycerides 39-53 proline rich transmembrane protein 2 Homo sapiens 18-21 16195316-6 2006 It is apparent that G-protein-coupled pathways linked to stimulation of phospholipase activity have a profound effect on regulating channel activity and that generation of diacylglycerol (DAG) is a central event in these signalling cascades with this triglyceride having a pivotal role in gating cation channels via both PKC-independent and -dependent mechanisms. Diglycerides 172-186 proline rich transmembrane protein 2 Homo sapiens 321-324 16195316-6 2006 It is apparent that G-protein-coupled pathways linked to stimulation of phospholipase activity have a profound effect on regulating channel activity and that generation of diacylglycerol (DAG) is a central event in these signalling cascades with this triglyceride having a pivotal role in gating cation channels via both PKC-independent and -dependent mechanisms. Diglycerides 188-191 proline rich transmembrane protein 2 Homo sapiens 321-324 15765405-6 2005 DCA also caused dramatic translocation of PH-PLCdelta-GFP, and conventional, Ca2+/diacylglycerol (DAG)-dependent isoforms of PKC (PKC-betaI and PKC-alpha), and MARCKS-GFP, but only in Ca2+-containing solutions. Diglycerides 82-96 proline rich transmembrane protein 2 Homo sapiens 130-133 15572354-6 2005 Together these results indicate that diacylglycerol-responsive PKC isoforms differentially influence CaR agonist-induced release of Ca2+ from internal stores. Diglycerides 37-51 proline rich transmembrane protein 2 Homo sapiens 63-66 12757721-1 2003 Effect on protein kinase C (PK-C) binding by the isosteric replacement of sn-1 and sn-2 esters in DAG-lactones. Diglycerides 98-101 proline rich transmembrane protein 2 Homo sapiens 10-26 15369389-2 2004 Hydrophobic ligand-protein interactions versus ligand-lipid interactions of DAG-lactones with protein kinase C (PK-C). Diglycerides 76-79 proline rich transmembrane protein 2 Homo sapiens 94-110 15369389-2 2004 Hydrophobic ligand-protein interactions versus ligand-lipid interactions of DAG-lactones with protein kinase C (PK-C). Diglycerides 76-79 proline rich transmembrane protein 2 Homo sapiens 112-116 15369389-3 2004 The constrained glycerol backbone of DAG-lactones, when combined with highly branched alkyl chains, has engendered a series of DAG-lactone ligands capable of binding protein kinase C (PK-C) with affinities that approximate those of phorbol esters. Diglycerides 37-40 proline rich transmembrane protein 2 Homo sapiens 166-182 15369389-3 2004 The constrained glycerol backbone of DAG-lactones, when combined with highly branched alkyl chains, has engendered a series of DAG-lactone ligands capable of binding protein kinase C (PK-C) with affinities that approximate those of phorbol esters. Diglycerides 37-40 proline rich transmembrane protein 2 Homo sapiens 184-188 15110845-0 2004 3D-QSAR analysis of conformationally constrained diacylglycerol (DAG) analogues as potent protein kinase C (PK-C) ligands. Diglycerides 49-63 proline rich transmembrane protein 2 Homo sapiens 90-106 15110845-0 2004 3D-QSAR analysis of conformationally constrained diacylglycerol (DAG) analogues as potent protein kinase C (PK-C) ligands. Diglycerides 49-63 proline rich transmembrane protein 2 Homo sapiens 108-112 15110845-0 2004 3D-QSAR analysis of conformationally constrained diacylglycerol (DAG) analogues as potent protein kinase C (PK-C) ligands. Diglycerides 65-68 proline rich transmembrane protein 2 Homo sapiens 90-106 15110845-0 2004 3D-QSAR analysis of conformationally constrained diacylglycerol (DAG) analogues as potent protein kinase C (PK-C) ligands. Diglycerides 65-68 proline rich transmembrane protein 2 Homo sapiens 108-112 14993731-5 2004 Like PKC, diacylglycerol kinase (DGK), which phosphorylates diacylglycerol resulting in attenuation of PKC, subtype-specifically translocates to particular subcellular compartments including the plasma membrane and Golgi complex. Diglycerides 10-24 proline rich transmembrane protein 2 Homo sapiens 5-8 14993731-5 2004 Like PKC, diacylglycerol kinase (DGK), which phosphorylates diacylglycerol resulting in attenuation of PKC, subtype-specifically translocates to particular subcellular compartments including the plasma membrane and Golgi complex. Diglycerides 10-24 proline rich transmembrane protein 2 Homo sapiens 103-106 12973696-4 2003 PKC isoforms are catalytically activated by several lipid cofactors, including diacylglycerol. Diglycerides 79-93 proline rich transmembrane protein 2 Homo sapiens 0-3 12809530-0 2003 Synthetic diacylglycerols (DAG) and DAG-lactones as activators of protein kinase C (PK-C). Diglycerides 10-25 proline rich transmembrane protein 2 Homo sapiens 66-82 12809530-0 2003 Synthetic diacylglycerols (DAG) and DAG-lactones as activators of protein kinase C (PK-C). Diglycerides 10-25 proline rich transmembrane protein 2 Homo sapiens 84-88 12809530-0 2003 Synthetic diacylglycerols (DAG) and DAG-lactones as activators of protein kinase C (PK-C). Diglycerides 27-30 proline rich transmembrane protein 2 Homo sapiens 66-82 12809530-0 2003 Synthetic diacylglycerols (DAG) and DAG-lactones as activators of protein kinase C (PK-C). Diglycerides 27-30 proline rich transmembrane protein 2 Homo sapiens 84-88 12809530-6 2003 Depending on the specific pattern of hydrophobic substitution, some DAG-lactones are able to induce selective translocation of individual PK-C isozymes to different cellular compartments, and since the specific nature of these hydrophobic interactions influences biological outcome, some of these compounds exhibit cell-specific antitumor activity. Diglycerides 68-71 proline rich transmembrane protein 2 Homo sapiens 138-142 15456534-9 2004 The proliferation and collagen synthesis were enhanced by PKC activator (containing phosphatidylserine, diacylglycerol and Ca2+) and PKA inhibitor [H(7)250 micromol/L, 1-(5-isoquinolinylsulfonyl)-2-methyl piperazine], and inhibited by PKC inhibitor (GF109 250 micromol/L) and PKA activator (cAMP 25 micromol/L) (P<0.01). Diglycerides 104-118 proline rich transmembrane protein 2 Homo sapiens 58-61 15098066-3 2004 The identification of protein kinase C (PKC) as a major cellular target for tumor-promoting phorbol esters suggested the involvement of this enzyme in the regulation of keratinocyte proliferation and tumorigenesis; however, results have demonstrated the existence in keratinocytes and other cell types of another diacylglycerol/phorbol ester-responsive protein kinase: protein kinase D (PKD) in mouse, also known as PKC micro in humans. Diglycerides 313-327 proline rich transmembrane protein 2 Homo sapiens 40-43 12757721-1 2003 Effect on protein kinase C (PK-C) binding by the isosteric replacement of sn-1 and sn-2 esters in DAG-lactones. Diglycerides 98-101 proline rich transmembrane protein 2 Homo sapiens 28-32 12506120-3 2003 PKCnu has two putative diacylglycerol binding C1 domains, suggesting that it may participate in a novel diacylglycerol-mediated signaling pathway. Diglycerides 23-37 proline rich transmembrane protein 2 Homo sapiens 0-5 12699375-0 2003 Differential binding modes of diacylglycerol (DAG) and DAG lactones to protein kinase C (PK-C). Diglycerides 30-44 proline rich transmembrane protein 2 Homo sapiens 71-87 12699375-0 2003 Differential binding modes of diacylglycerol (DAG) and DAG lactones to protein kinase C (PK-C). Diglycerides 30-44 proline rich transmembrane protein 2 Homo sapiens 89-93 12699375-0 2003 Differential binding modes of diacylglycerol (DAG) and DAG lactones to protein kinase C (PK-C). Diglycerides 46-49 proline rich transmembrane protein 2 Homo sapiens 71-87 12699375-0 2003 Differential binding modes of diacylglycerol (DAG) and DAG lactones to protein kinase C (PK-C). Diglycerides 46-49 proline rich transmembrane protein 2 Homo sapiens 89-93 12699375-0 2003 Differential binding modes of diacylglycerol (DAG) and DAG lactones to protein kinase C (PK-C). Diglycerides 55-58 proline rich transmembrane protein 2 Homo sapiens 71-87 12699375-0 2003 Differential binding modes of diacylglycerol (DAG) and DAG lactones to protein kinase C (PK-C). Diglycerides 55-58 proline rich transmembrane protein 2 Homo sapiens 89-93 12699375-1 2003 Diacylglycerol lactones (DAG lactones), analogous to highly potent diacylglycerols (DAGs) were synthesized to demonstrate the ability of PK-C to discriminate between two differential binding modes, sn-1 and sn-2. Diglycerides 25-28 proline rich transmembrane protein 2 Homo sapiens 137-141 12699375-1 2003 Diacylglycerol lactones (DAG lactones), analogous to highly potent diacylglycerols (DAGs) were synthesized to demonstrate the ability of PK-C to discriminate between two differential binding modes, sn-1 and sn-2. Diglycerides 84-88 proline rich transmembrane protein 2 Homo sapiens 137-141 12506120-3 2003 PKCnu has two putative diacylglycerol binding C1 domains, suggesting that it may participate in a novel diacylglycerol-mediated signaling pathway. Diglycerides 104-118 proline rich transmembrane protein 2 Homo sapiens 0-5 12506120-4 2003 Here we show that both endogenous and recombinant PKCnu are trans-located to the plasma membrane and activated by the diacylglycerol mimic phorbol 12-myristate 13-acetate. Diglycerides 118-132 proline rich transmembrane protein 2 Homo sapiens 50-55 12213816-2 2002 We report that two alternate signaling pathways of protein kinase C (PKC) activation involving either the lipid second messengers (diacylglycerol and its mimetics, the phorbol esters) or reactive oxygen converge at the zinc finger of the regulatory domain. Diglycerides 131-145 proline rich transmembrane protein 2 Homo sapiens 51-67 15981946-2 2003 Although the mechanisms underlying this phenomenon are likely to be multifactorial, recent in vivo and in vitro studies have indicated a crucial role of the diacylglycerol (DAG)-protein kinase C (PKC) pathway in mediating this phenomenon. Diglycerides 157-171 proline rich transmembrane protein 2 Homo sapiens 196-199 15981946-2 2003 Although the mechanisms underlying this phenomenon are likely to be multifactorial, recent in vivo and in vitro studies have indicated a crucial role of the diacylglycerol (DAG)-protein kinase C (PKC) pathway in mediating this phenomenon. Diglycerides 173-176 proline rich transmembrane protein 2 Homo sapiens 196-199 12213816-2 2002 We report that two alternate signaling pathways of protein kinase C (PKC) activation involving either the lipid second messengers (diacylglycerol and its mimetics, the phorbol esters) or reactive oxygen converge at the zinc finger of the regulatory domain. Diglycerides 131-145 proline rich transmembrane protein 2 Homo sapiens 69-72 12213816-7 2002 Furthermore, purified recombinant PKC protein fragments shed stoichiometric amounts of Zn(2+) upon reaction with diacylglycerol, phorbol ester, or reactive oxygen in vitro. Diglycerides 113-127 proline rich transmembrane protein 2 Homo sapiens 34-37 11689442-1 2001 The generation of diacylglycerol (DAG) in response to receptor stimulation is a well-documented signalling mechanism that leads to activation of protein kinase C (PKC). Diglycerides 18-32 proline rich transmembrane protein 2 Homo sapiens 145-161 12417013-3 2002 Upon stimulation of various receptors, PKC is catalytically activated by several activators including diacylglycerol. Diglycerides 102-116 proline rich transmembrane protein 2 Homo sapiens 39-42 11728178-2 2001 The incorporation of a hydroxamate moiety into diacylglycerol-lactones reduces lipophilicity and helps discriminate between sn-1 and sn-2 binding modes to protein kinase C (PK-C). Diglycerides 47-61 proline rich transmembrane protein 2 Homo sapiens 155-171 11728178-2 2001 The incorporation of a hydroxamate moiety into diacylglycerol-lactones reduces lipophilicity and helps discriminate between sn-1 and sn-2 binding modes to protein kinase C (PK-C). Diglycerides 47-61 proline rich transmembrane protein 2 Homo sapiens 173-177 11728178-4 2001 An approach to reduce the log P in a series of diacylglycerol (DAG)-lactones known for their high binding affinity for protein kinase C (PK-C) is presented. Diglycerides 47-61 proline rich transmembrane protein 2 Homo sapiens 119-135 11728178-4 2001 An approach to reduce the log P in a series of diacylglycerol (DAG)-lactones known for their high binding affinity for protein kinase C (PK-C) is presented. Diglycerides 47-61 proline rich transmembrane protein 2 Homo sapiens 137-141 11728178-4 2001 An approach to reduce the log P in a series of diacylglycerol (DAG)-lactones known for their high binding affinity for protein kinase C (PK-C) is presented. Diglycerides 63-66 proline rich transmembrane protein 2 Homo sapiens 119-135 11728178-4 2001 An approach to reduce the log P in a series of diacylglycerol (DAG)-lactones known for their high binding affinity for protein kinase C (PK-C) is presented. Diglycerides 63-66 proline rich transmembrane protein 2 Homo sapiens 137-141 11689442-1 2001 The generation of diacylglycerol (DAG) in response to receptor stimulation is a well-documented signalling mechanism that leads to activation of protein kinase C (PKC). Diglycerides 34-37 proline rich transmembrane protein 2 Homo sapiens 145-161 11689442-1 2001 The generation of diacylglycerol (DAG) in response to receptor stimulation is a well-documented signalling mechanism that leads to activation of protein kinase C (PKC). Diglycerides 34-37 proline rich transmembrane protein 2 Homo sapiens 163-166 11689442-3 2001 We have identified a Dictyostelium gene encoding a novel protein which contains a domain with high identity to the DAG-binding domain of PKC. Diglycerides 115-118 proline rich transmembrane protein 2 Homo sapiens 137-140 11689442-1 2001 The generation of diacylglycerol (DAG) in response to receptor stimulation is a well-documented signalling mechanism that leads to activation of protein kinase C (PKC). Diglycerides 18-32 proline rich transmembrane protein 2 Homo sapiens 163-166 11377832-5 2001 DAG, in turn, is known to activate several members of the protein kinase C (PKC) family. Diglycerides 0-3 proline rich transmembrane protein 2 Homo sapiens 58-74 11438442-3 2001 The above mentioned biochemical processes involve signal transduction pathways that are well known in other cell systems, and require mediation of second messengers like Ca2+ and diacylglycerol (DAG) which are protein kinase C (PKC) activators. Diglycerides 179-193 proline rich transmembrane protein 2 Homo sapiens 210-226 11438442-3 2001 The above mentioned biochemical processes involve signal transduction pathways that are well known in other cell systems, and require mediation of second messengers like Ca2+ and diacylglycerol (DAG) which are protein kinase C (PKC) activators. Diglycerides 179-193 proline rich transmembrane protein 2 Homo sapiens 228-231 11438442-3 2001 The above mentioned biochemical processes involve signal transduction pathways that are well known in other cell systems, and require mediation of second messengers like Ca2+ and diacylglycerol (DAG) which are protein kinase C (PKC) activators. Diglycerides 195-198 proline rich transmembrane protein 2 Homo sapiens 210-226 11438442-3 2001 The above mentioned biochemical processes involve signal transduction pathways that are well known in other cell systems, and require mediation of second messengers like Ca2+ and diacylglycerol (DAG) which are protein kinase C (PKC) activators. Diglycerides 195-198 proline rich transmembrane protein 2 Homo sapiens 228-231 11377832-5 2001 DAG, in turn, is known to activate several members of the protein kinase C (PKC) family. Diglycerides 0-3 proline rich transmembrane protein 2 Homo sapiens 76-79 11465069-6 2000 Phorbol esters such as the tumor-promoter 12-O-tetradecanoylphorbol-13-acetate (TPA) or diacylglycerol (DAG) activate classical and novel PKC isoforms. Diglycerides 88-102 proline rich transmembrane protein 2 Homo sapiens 138-141 11465069-6 2000 Phorbol esters such as the tumor-promoter 12-O-tetradecanoylphorbol-13-acetate (TPA) or diacylglycerol (DAG) activate classical and novel PKC isoforms. Diglycerides 104-107 proline rich transmembrane protein 2 Homo sapiens 138-141 10715158-3 2000 The design of potent protein kinase C (PK-C) ligands with low nanomolar binding affinities was accomplished by the combined use of pharmacophore- and receptor-guided approaches based on the structure of the physiological enzyme activator, diacylglycerol (DAG). Diglycerides 239-253 proline rich transmembrane protein 2 Homo sapiens 21-37 10966739-10 2000 The sn-1 DAG lactones were less effective as PK-C ligands than the sn-2 DAG lactones despite having a similar array of linear or branched acyl and alpha-alkylidene chains Diglycerides 9-12 proline rich transmembrane protein 2 Homo sapiens 45-49 10837365-7 2000 Because DAG formed by action of PC-PLC can activate protein kinase C (PKC), involvement of PKC was investigated. Diglycerides 8-11 proline rich transmembrane protein 2 Homo sapiens 52-68 10837365-7 2000 Because DAG formed by action of PC-PLC can activate protein kinase C (PKC), involvement of PKC was investigated. Diglycerides 8-11 proline rich transmembrane protein 2 Homo sapiens 70-73 10966739-3 2000 In previous work, we have obtained potent protein kinase C (PK-C) ligands with low-namomolar binding affinities by constructing diacylglycerol (DAG) mimetics in which the sn-2 carbonyl of DAG was constrained into a lactone ring. Diglycerides 128-142 proline rich transmembrane protein 2 Homo sapiens 42-58 10966739-3 2000 In previous work, we have obtained potent protein kinase C (PK-C) ligands with low-namomolar binding affinities by constructing diacylglycerol (DAG) mimetics in which the sn-2 carbonyl of DAG was constrained into a lactone ring. Diglycerides 128-142 proline rich transmembrane protein 2 Homo sapiens 60-64 10966739-3 2000 In previous work, we have obtained potent protein kinase C (PK-C) ligands with low-namomolar binding affinities by constructing diacylglycerol (DAG) mimetics in which the sn-2 carbonyl of DAG was constrained into a lactone ring. Diglycerides 144-147 proline rich transmembrane protein 2 Homo sapiens 42-58 10966739-3 2000 In previous work, we have obtained potent protein kinase C (PK-C) ligands with low-namomolar binding affinities by constructing diacylglycerol (DAG) mimetics in which the sn-2 carbonyl of DAG was constrained into a lactone ring. Diglycerides 144-147 proline rich transmembrane protein 2 Homo sapiens 60-64 10966739-3 2000 In previous work, we have obtained potent protein kinase C (PK-C) ligands with low-namomolar binding affinities by constructing diacylglycerol (DAG) mimetics in which the sn-2 carbonyl of DAG was constrained into a lactone ring. Diglycerides 188-191 proline rich transmembrane protein 2 Homo sapiens 42-58 10966739-3 2000 In previous work, we have obtained potent protein kinase C (PK-C) ligands with low-namomolar binding affinities by constructing diacylglycerol (DAG) mimetics in which the sn-2 carbonyl of DAG was constrained into a lactone ring. Diglycerides 188-191 proline rich transmembrane protein 2 Homo sapiens 60-64 10762046-0 2000 Diacylglycerols with lipophilically equivalent branched acyl chains display high affinity for protein kinase C (PK-C). Diglycerides 0-15 proline rich transmembrane protein 2 Homo sapiens 94-110 10762046-0 2000 Diacylglycerols with lipophilically equivalent branched acyl chains display high affinity for protein kinase C (PK-C). Diglycerides 0-15 proline rich transmembrane protein 2 Homo sapiens 112-116 10715158-3 2000 The design of potent protein kinase C (PK-C) ligands with low nanomolar binding affinities was accomplished by the combined use of pharmacophore- and receptor-guided approaches based on the structure of the physiological enzyme activator, diacylglycerol (DAG). Diglycerides 239-253 proline rich transmembrane protein 2 Homo sapiens 39-43 10715158-3 2000 The design of potent protein kinase C (PK-C) ligands with low nanomolar binding affinities was accomplished by the combined use of pharmacophore- and receptor-guided approaches based on the structure of the physiological enzyme activator, diacylglycerol (DAG). Diglycerides 255-258 proline rich transmembrane protein 2 Homo sapiens 21-37 10715158-3 2000 The design of potent protein kinase C (PK-C) ligands with low nanomolar binding affinities was accomplished by the combined use of pharmacophore- and receptor-guided approaches based on the structure of the physiological enzyme activator, diacylglycerol (DAG). Diglycerides 255-258 proline rich transmembrane protein 2 Homo sapiens 39-43 10715158-16 2000 Our present approach should facilitate the generation of multiple libraries of structurally similar DAG-lactones to help exploit molecular diversity for PK-C and other high-affinity receptors for DAG and the phorbol esters. Diglycerides 100-103 proline rich transmembrane protein 2 Homo sapiens 153-157 10715158-16 2000 Our present approach should facilitate the generation of multiple libraries of structurally similar DAG-lactones to help exploit molecular diversity for PK-C and other high-affinity receptors for DAG and the phorbol esters. Diglycerides 196-199 proline rich transmembrane protein 2 Homo sapiens 153-157 10588370-3 1999 The activation of PKC induced by hyperglycemia appears to be due to an increase in diacylglycerol (DAG) levels, a physiological activator of PKC. Diglycerides 83-97 proline rich transmembrane protein 2 Homo sapiens 18-21 10629766-1 1999 Protein kinase C (PKC) is reversibly activated at the plasma membrane by the generation of diacylglycerol (DAG) coupled with the release of Ca2+ from intracellular stores. Diglycerides 91-105 proline rich transmembrane protein 2 Homo sapiens 0-16 10629766-1 1999 Protein kinase C (PKC) is reversibly activated at the plasma membrane by the generation of diacylglycerol (DAG) coupled with the release of Ca2+ from intracellular stores. Diglycerides 91-105 proline rich transmembrane protein 2 Homo sapiens 18-21 10629766-1 1999 Protein kinase C (PKC) is reversibly activated at the plasma membrane by the generation of diacylglycerol (DAG) coupled with the release of Ca2+ from intracellular stores. Diglycerides 107-110 proline rich transmembrane protein 2 Homo sapiens 0-16 10629766-1 1999 Protein kinase C (PKC) is reversibly activated at the plasma membrane by the generation of diacylglycerol (DAG) coupled with the release of Ca2+ from intracellular stores. Diglycerides 107-110 proline rich transmembrane protein 2 Homo sapiens 18-21 10629766-4 1999 We examined the downstream consequences of PKC activation by the phorbol ester TPA and by ionophore A23187-mediated calcium influx (which experimentally correspond to DAG-mediated and calpain-mediated activation, respectively) on phosphorylation of the microtubule-associated protein tau. Diglycerides 167-170 proline rich transmembrane protein 2 Homo sapiens 43-46 10588370-3 1999 The activation of PKC induced by hyperglycemia appears to be due to an increase in diacylglycerol (DAG) levels, a physiological activator of PKC. Diglycerides 83-97 proline rich transmembrane protein 2 Homo sapiens 141-144 10588370-3 1999 The activation of PKC induced by hyperglycemia appears to be due to an increase in diacylglycerol (DAG) levels, a physiological activator of PKC. Diglycerides 99-102 proline rich transmembrane protein 2 Homo sapiens 18-21 10588370-3 1999 The activation of PKC induced by hyperglycemia appears to be due to an increase in diacylglycerol (DAG) levels, a physiological activator of PKC. Diglycerides 99-102 proline rich transmembrane protein 2 Homo sapiens 141-144 10380910-7 1999 MM6 phagocytosis was inhibited with staurosporine and activated with diacylglycerol, supporting a role for protein kinase C (PKC) in this process. Diglycerides 69-83 proline rich transmembrane protein 2 Homo sapiens 107-123 10380910-7 1999 MM6 phagocytosis was inhibited with staurosporine and activated with diacylglycerol, supporting a role for protein kinase C (PKC) in this process. Diglycerides 69-83 proline rich transmembrane protein 2 Homo sapiens 125-128 9814702-0 1998 Protein kinase C as a molecular machine for decoding calcium and diacylglycerol signals. Diglycerides 65-79 proline rich transmembrane protein 2 Homo sapiens 0-16 10209246-4 1999 Phosphoinositide (PI)-coupled muscarinic acetylcholine receptor (mAchR) activation would be expected to increase PKC activity through production of the second messenger, diacylglycerol. Diglycerides 170-184 proline rich transmembrane protein 2 Homo sapiens 113-116 9814702-2 1998 Here we found a molecular mechanism which guarantees that conventional protein kinase C (PKC) isoforms are sequentially activated by calcium and diacylglycerol signals. Diglycerides 145-159 proline rich transmembrane protein 2 Homo sapiens 71-87 9814702-2 1998 Here we found a molecular mechanism which guarantees that conventional protein kinase C (PKC) isoforms are sequentially activated by calcium and diacylglycerol signals. Diglycerides 145-159 proline rich transmembrane protein 2 Homo sapiens 89-92 9670214-1 1998 Protein kinase C (PKC), activated by either diacylglycerol and/or arachidonic acid, through the activation of presynaptic receptors or nerve or nerve depolarization is involved is involved in the enhancement of transmitter release from many neural types. Diglycerides 44-58 proline rich transmembrane protein 2 Homo sapiens 0-16 9670214-1 1998 Protein kinase C (PKC), activated by either diacylglycerol and/or arachidonic acid, through the activation of presynaptic receptors or nerve or nerve depolarization is involved is involved in the enhancement of transmitter release from many neural types. Diglycerides 44-58 proline rich transmembrane protein 2 Homo sapiens 18-21 9237245-9 1997 The products of phosphatidyl-inositol bisphosphate (PIP2) hydrolysis by PLC diacylglycerol (DAG) and inositol-trisphosphate (IP3) will lead to PKC translocation to the plasma membrane and its activation. Diglycerides 76-90 proline rich transmembrane protein 2 Homo sapiens 143-146 9617479-2 1998 PKC is activated by increases in diacylglycerol produced in response to agonist-induced hydrolysis of inositol phospholipids. Diglycerides 33-47 proline rich transmembrane protein 2 Homo sapiens 0-3 9446641-7 1998 Immunoblot analysis using PKC isotype-specific antibodies showed that TPO treatment led to a marked increase of the Ca2+/diacylglycerol-sensitive PKC isoforms alpha and beta found in the membrane fraction. Diglycerides 121-135 proline rich transmembrane protein 2 Homo sapiens 26-29 9269538-3 1997 In noradrenergic nerves it appears to be tonically activated by diacylglycerol (DAG) to facilitate transmitter release and the steps in this involve activation of phospholipase C, generation of DAG and activation of PKC. Diglycerides 64-78 proline rich transmembrane protein 2 Homo sapiens 216-219 9269538-3 1997 In noradrenergic nerves it appears to be tonically activated by diacylglycerol (DAG) to facilitate transmitter release and the steps in this involve activation of phospholipase C, generation of DAG and activation of PKC. Diglycerides 80-83 proline rich transmembrane protein 2 Homo sapiens 216-219 9099897-10 1997 The results suggest that the diacylglycerol-PKC signal transduction system mediates the prolactin effect on mAAT. Diglycerides 29-43 proline rich transmembrane protein 2 Homo sapiens 44-47 9510544-6 1998 Although PKC activity is clearly inducible in vitro by diacylglycerol and a tumour promoting phorbol ester, structural features detected in the regulatory domains of HvPKC1a and 1b indicate that endogenous activators for Hydra PKC might differ from those of other organisms. Diglycerides 55-69 proline rich transmembrane protein 2 Homo sapiens 9-12 9237245-9 1997 The products of phosphatidyl-inositol bisphosphate (PIP2) hydrolysis by PLC diacylglycerol (DAG) and inositol-trisphosphate (IP3) will lead to PKC translocation to the plasma membrane and its activation. Diglycerides 92-95 proline rich transmembrane protein 2 Homo sapiens 143-146 8960550-10 1996 With these results, the order of importance of five-membered ring lactones as competent templates for the construction of semirigid DAG surrogates with effective PK-C binding affinity can be established as II >> I approximately III > IV. Diglycerides 132-135 proline rich transmembrane protein 2 Homo sapiens 162-166 8805373-4 1996 PKC is acutely regulated by the second messenger diacylglycerol; however, it is also known to undergo multisite phosphorylation. Diglycerides 49-63 proline rich transmembrane protein 2 Homo sapiens 0-3 8876672-2 1996 It was previously suggested that elevated levels of diacylglycerol in ras-transformed fibroblasts lead to activation-induced proteolysis of cellular PKC. Diglycerides 52-66 proline rich transmembrane protein 2 Homo sapiens 149-152 8712775-4 1996 The intracellular signaling pathway involves a phospholipase, either C or D, which metabolizes membrane phospholipids to produce diacylglycerol, a necessary endogenous cofactor for PKC activation. Diglycerides 129-143 proline rich transmembrane protein 2 Homo sapiens 181-184 8700857-2 1996 In particular, a synthetic phospholipid, dansyl-phosphatidylethanolamine, proved to be fully functional in the association of PKC with lipid bilayers and in mediating the interaction of this enzyme with diacylglycerol. Diglycerides 203-217 proline rich transmembrane protein 2 Homo sapiens 126-129 8820410-0 1996 Reorientational properties of fluorescent analogues of the protein kinase C cofactors diacylglycerol and phorbol ester. Diglycerides 86-100 proline rich transmembrane protein 2 Homo sapiens 59-75 8820410-1 1996 The reorientational properties of the fluorescently labelled protein kinase C (PKC) cofactors diacylglycerol (DG) and phorbol ester (PMA) in vesicles and mixed micelles have been investigated using time-resolved polarised fluorescence. Diglycerides 94-108 proline rich transmembrane protein 2 Homo sapiens 61-77 8820410-1 1996 The reorientational properties of the fluorescently labelled protein kinase C (PKC) cofactors diacylglycerol (DG) and phorbol ester (PMA) in vesicles and mixed micelles have been investigated using time-resolved polarised fluorescence. Diglycerides 94-108 proline rich transmembrane protein 2 Homo sapiens 79-82 8568819-3 1996 Conformationally constrained analogues of diacylglycerol (DAG) built on a racemic 5(-)[(acyloxy)-methyl]-5-(hydroxymethyl)tetrahydro-2-furanone template were shown previously to have excellent binding affinities for protein kinase C (PK-C). Diglycerides 42-56 proline rich transmembrane protein 2 Homo sapiens 216-232 8568819-3 1996 Conformationally constrained analogues of diacylglycerol (DAG) built on a racemic 5(-)[(acyloxy)-methyl]-5-(hydroxymethyl)tetrahydro-2-furanone template were shown previously to have excellent binding affinities for protein kinase C (PK-C). Diglycerides 42-56 proline rich transmembrane protein 2 Homo sapiens 234-238 8568819-3 1996 Conformationally constrained analogues of diacylglycerol (DAG) built on a racemic 5(-)[(acyloxy)-methyl]-5-(hydroxymethyl)tetrahydro-2-furanone template were shown previously to have excellent binding affinities for protein kinase C (PK-C). Diglycerides 58-61 proline rich transmembrane protein 2 Homo sapiens 216-232 8568819-3 1996 Conformationally constrained analogues of diacylglycerol (DAG) built on a racemic 5(-)[(acyloxy)-methyl]-5-(hydroxymethyl)tetrahydro-2-furanone template were shown previously to have excellent binding affinities for protein kinase C (PK-C). Diglycerides 58-61 proline rich transmembrane protein 2 Homo sapiens 234-238 8568819-4 1996 Since the interaction of PK-C with DAG is stereospecific, it was anticipated that PK-C would bind tightly to only one enantiomeric form of the compounds constructed with this new lactone template. Diglycerides 35-38 proline rich transmembrane protein 2 Homo sapiens 25-29 8568819-4 1996 Since the interaction of PK-C with DAG is stereospecific, it was anticipated that PK-C would bind tightly to only one enantiomeric form of the compounds constructed with this new lactone template. Diglycerides 35-38 proline rich transmembrane protein 2 Homo sapiens 82-86 8613911-7 1996 Hydrolysis of PIP2 by PIP2-specific phospholipase C produces equimolar amounts of inositol 1,4,5-triphosphate and diacylglycerol, which may interact synergistically to activate PKC and develop tone. Diglycerides 114-128 proline rich transmembrane protein 2 Homo sapiens 177-180 8613911-8 1996 Furthermore, PKC-mediated contraction may be augmented by additional diacylglycerol production arising from the hydrolysis of phosphatidylcholine by phosphatidylcholine-specific phospholipase C. Diglycerides 69-83 proline rich transmembrane protein 2 Homo sapiens 13-16 9015863-4 1996 PKC-mediated phosphorylation of profilin was observed only in the presence of phosphoinositides; phosphatidylserine and diacylglycerol (known activators of PKC) and other lipids, including phosphatidic acid and phosphatidylglycerol phosphate, did not activate the phosphorylation. Diglycerides 120-134 proline rich transmembrane protein 2 Homo sapiens 0-3 9015863-4 1996 PKC-mediated phosphorylation of profilin was observed only in the presence of phosphoinositides; phosphatidylserine and diacylglycerol (known activators of PKC) and other lipids, including phosphatidic acid and phosphatidylglycerol phosphate, did not activate the phosphorylation. Diglycerides 120-134 proline rich transmembrane protein 2 Homo sapiens 156-159 12232621-5 1996 The accumulation of DAG and the activation of PKC induced by high K(+) exposure suggest a possible role of the pathway of DAG/PKC in the regulation of the excitation-contraction coupling in skeletal muscle fibres. Diglycerides 20-23 proline rich transmembrane protein 2 Homo sapiens 126-129 12232621-5 1996 The accumulation of DAG and the activation of PKC induced by high K(+) exposure suggest a possible role of the pathway of DAG/PKC in the regulation of the excitation-contraction coupling in skeletal muscle fibres. Diglycerides 122-125 proline rich transmembrane protein 2 Homo sapiens 46-49 12232621-5 1996 The accumulation of DAG and the activation of PKC induced by high K(+) exposure suggest a possible role of the pathway of DAG/PKC in the regulation of the excitation-contraction coupling in skeletal muscle fibres. Diglycerides 122-125 proline rich transmembrane protein 2 Homo sapiens 126-129 7803515-10 1994 In gastric chief cells, translocation and activation of alpha PKC occurs in response to agonist-induced increases in calcium and diacylglycerol. Diglycerides 129-143 proline rich transmembrane protein 2 Homo sapiens 62-65 8519996-6 1995 The DAG-induced changes in alpha-deuteron splittings were found to correlate with DAG-enhanced protein kinase C (PK-C) activity, suggesting that the DAG-induced conformational changes of the phosphatidylcholine headgroups are either directly or indirectly related to a mechanism of PK-C activation. Diglycerides 4-7 proline rich transmembrane protein 2 Homo sapiens 95-111 8519996-6 1995 The DAG-induced changes in alpha-deuteron splittings were found to correlate with DAG-enhanced protein kinase C (PK-C) activity, suggesting that the DAG-induced conformational changes of the phosphatidylcholine headgroups are either directly or indirectly related to a mechanism of PK-C activation. Diglycerides 4-7 proline rich transmembrane protein 2 Homo sapiens 113-117 8519996-6 1995 The DAG-induced changes in alpha-deuteron splittings were found to correlate with DAG-enhanced protein kinase C (PK-C) activity, suggesting that the DAG-induced conformational changes of the phosphatidylcholine headgroups are either directly or indirectly related to a mechanism of PK-C activation. Diglycerides 4-7 proline rich transmembrane protein 2 Homo sapiens 282-286 8519996-6 1995 The DAG-induced changes in alpha-deuteron splittings were found to correlate with DAG-enhanced protein kinase C (PK-C) activity, suggesting that the DAG-induced conformational changes of the phosphatidylcholine headgroups are either directly or indirectly related to a mechanism of PK-C activation. Diglycerides 82-85 proline rich transmembrane protein 2 Homo sapiens 95-111 8519996-6 1995 The DAG-induced changes in alpha-deuteron splittings were found to correlate with DAG-enhanced protein kinase C (PK-C) activity, suggesting that the DAG-induced conformational changes of the phosphatidylcholine headgroups are either directly or indirectly related to a mechanism of PK-C activation. Diglycerides 82-85 proline rich transmembrane protein 2 Homo sapiens 113-117 8519996-6 1995 The DAG-induced changes in alpha-deuteron splittings were found to correlate with DAG-enhanced protein kinase C (PK-C) activity, suggesting that the DAG-induced conformational changes of the phosphatidylcholine headgroups are either directly or indirectly related to a mechanism of PK-C activation. Diglycerides 82-85 proline rich transmembrane protein 2 Homo sapiens 282-286 8519996-6 1995 The DAG-induced changes in alpha-deuteron splittings were found to correlate with DAG-enhanced protein kinase C (PK-C) activity, suggesting that the DAG-induced conformational changes of the phosphatidylcholine headgroups are either directly or indirectly related to a mechanism of PK-C activation. Diglycerides 82-85 proline rich transmembrane protein 2 Homo sapiens 95-111 8519996-6 1995 The DAG-induced changes in alpha-deuteron splittings were found to correlate with DAG-enhanced protein kinase C (PK-C) activity, suggesting that the DAG-induced conformational changes of the phosphatidylcholine headgroups are either directly or indirectly related to a mechanism of PK-C activation. Diglycerides 82-85 proline rich transmembrane protein 2 Homo sapiens 113-117 8519996-6 1995 The DAG-induced changes in alpha-deuteron splittings were found to correlate with DAG-enhanced protein kinase C (PK-C) activity, suggesting that the DAG-induced conformational changes of the phosphatidylcholine headgroups are either directly or indirectly related to a mechanism of PK-C activation. Diglycerides 82-85 proline rich transmembrane protein 2 Homo sapiens 282-286 7493994-11 1995 These results suggest two modes of stimulating pleckstrin phosphorylation: a rapid activation of PKC (via diacylglycerol and calcium) followed by a slower activation of calcium-independent PKCs via PtdIns-3,4-P2. Diglycerides 106-120 proline rich transmembrane protein 2 Homo sapiens 97-100 7485441-5 1995 Phorbol ester activators of PKC mimicked the stretch response as did platelet-derived growth factor (PDGF), which acts, in part, through generation of endogenous diacylglycerols. Diglycerides 162-177 proline rich transmembrane protein 2 Homo sapiens 28-31 7783402-3 1995 We tested the hypothesis that only those PKC isoforms binding to diacylglycerol (DAG) are activated by high glucose. Diglycerides 65-79 proline rich transmembrane protein 2 Homo sapiens 41-44 7783402-3 1995 We tested the hypothesis that only those PKC isoforms binding to diacylglycerol (DAG) are activated by high glucose. Diglycerides 81-84 proline rich transmembrane protein 2 Homo sapiens 41-44 8532710-3 1995 PKC activation is also implicated in tumor promotion of colonic epithelial cells by endogenous and dietary factors such as bile acids, free fatty acids, and diacylglycerols, suggesting that suppression of the inappropriate activation of colonic epithelial PKC by these factors could be an effective strategy of chemoprevention. Diglycerides 157-172 proline rich transmembrane protein 2 Homo sapiens 0-3 8074672-1 1994 The purified preparation showed typical characteristics of the conventional type of mammalian PKC that responds to Ca2+, phosphatidylserine, and diacylglycerol or the tumor-promoting phorbol ester, phorbol 12-myristate 13-acetate. Diglycerides 145-159 proline rich transmembrane protein 2 Homo sapiens 94-97 7712599-2 1994 Reversible activation of PKC by the second messengers diacylglycerol and calcium is an established model for the short term regulation of PKC in the immediate events of signal transduction. Diglycerides 54-68 proline rich transmembrane protein 2 Homo sapiens 25-28 7712599-2 1994 Reversible activation of PKC by the second messengers diacylglycerol and calcium is an established model for the short term regulation of PKC in the immediate events of signal transduction. Diglycerides 54-68 proline rich transmembrane protein 2 Homo sapiens 138-141 28305948-6 1994 Bacterial induction of metamorphosis of Hydractinia echinata caused an increase in endogenous diacylglycerol, the physiological activator of PKC, suggesting that the bacterial inducer acts by activating receptor-regulated phospholipid metabolism. Diglycerides 94-108 proline rich transmembrane protein 2 Homo sapiens 141-144 28305948-7 1994 Exogenous diacylglycerol leads to membrane translocation of PKC, indicative of an activation. Diglycerides 10-24 proline rich transmembrane protein 2 Homo sapiens 60-63 8130278-3 1994 In the presence of calcium, phosphatidylserine and diacylglycerol, both palmitoyl-CoA (Pal-CoA) and oleoyl-CoA (Ole-CoA) enhanced particulate PK-C activity by approx. Diglycerides 51-65 proline rich transmembrane protein 2 Homo sapiens 142-146 8130278-11 1994 Activation of PK-C in stimulated fibroblasts, i.e., in the presence of an elevated diacylglycerol concentration, is less pronounced. Diglycerides 83-97 proline rich transmembrane protein 2 Homo sapiens 14-18 8344386-2 1993 PKC activity is stimulated physiologically by diacylglycerol and experimentally by phorbol esters. Diglycerides 46-60 proline rich transmembrane protein 2 Homo sapiens 0-3 8405692-2 1993 Since the physiological activator of pkC is diacylglycerol (DG), we examined the DG content of the oocytes before and during germinal vesicle breakdown (GVBD). Diglycerides 44-58 proline rich transmembrane protein 2 Homo sapiens 37-40 1303731-1 1992 Activation of protein kinase C (PKC) is regulated by dual second messengers; diacylglycerol (DG) produced by receptor mediated hydrolysis of phosphatidylinositol and Ca2+ which is released by inositol 1,4,5-triphosphate (IP3) from intracellular stores in the endoplasmic reticulum. Diglycerides 77-91 proline rich transmembrane protein 2 Homo sapiens 14-30 8374745-2 1993 When 10 micrograms/ml of GGF was added to the culture medium, Schwann cell division was activated by about 3-fold, while protein kinase C (PKC) activity was translocated from the cytosol to the particulate fraction, and diacylglycerol (DG) production was increased in the cells. Diglycerides 220-234 proline rich transmembrane protein 2 Homo sapiens 139-142 8390801-1 1993 Previous work has shown that PMA and diacylglycerols, activators of protein kinase C (PKC) can suppress cell polarity and locomotor activity of Walker carcinosarcoma cells in vitro, suggesting that PKC activation may result in a stop signal for tumor cell locomotion. Diglycerides 37-52 proline rich transmembrane protein 2 Homo sapiens 68-84 8390801-1 1993 Previous work has shown that PMA and diacylglycerols, activators of protein kinase C (PKC) can suppress cell polarity and locomotor activity of Walker carcinosarcoma cells in vitro, suggesting that PKC activation may result in a stop signal for tumor cell locomotion. Diglycerides 37-52 proline rich transmembrane protein 2 Homo sapiens 86-89 8390801-1 1993 Previous work has shown that PMA and diacylglycerols, activators of protein kinase C (PKC) can suppress cell polarity and locomotor activity of Walker carcinosarcoma cells in vitro, suggesting that PKC activation may result in a stop signal for tumor cell locomotion. Diglycerides 37-52 proline rich transmembrane protein 2 Homo sapiens 198-201 8430818-7 1993 In contrast, treatment with either TNF (1,000 U/ml for 15 min) or 1,2-dioctanoylglycerol (4 x 10(-5) M for 5 min), a diacylglycerol that activates PKC, resulted in translocation of fluorescence to the cell periphery; fine, punctate PKC-associated fluorescence was localized to the margins of cells. Diglycerides 117-131 proline rich transmembrane protein 2 Homo sapiens 147-150 8430818-7 1993 In contrast, treatment with either TNF (1,000 U/ml for 15 min) or 1,2-dioctanoylglycerol (4 x 10(-5) M for 5 min), a diacylglycerol that activates PKC, resulted in translocation of fluorescence to the cell periphery; fine, punctate PKC-associated fluorescence was localized to the margins of cells. Diglycerides 117-131 proline rich transmembrane protein 2 Homo sapiens 232-235 8430818-8 1993 The TNF-induced translocation of PKC was inhibited using either IP-300 polyclonal anti-TNF antibody (indicating that the TNF effect was not due to the vehicle or contaminating endotoxin) or calphostin C (10(-6) M for 15 min), which inhibits PKC activation by interacting with the regulatory diacylglycerol-binding domain. Diglycerides 291-305 proline rich transmembrane protein 2 Homo sapiens 33-36 1335820-0 1992 Evidence for hippocampal calcium channel regulation by PKC based on comparison of diacylglycerols and phorbol esters. Diglycerides 82-97 proline rich transmembrane protein 2 Homo sapiens 55-58 1335820-2 1992 We have tested the hypothesis that PKC modulates Ca2+ channel activity in hippocampal neurons by conducting a detailed comparison of the effects of the diacylglycerols, diC8 and OAG, with those of the phorbol ester, PDBu, on whole-cell and single-channel Ca2+ currents. Diglycerides 152-167 proline rich transmembrane protein 2 Homo sapiens 35-38 8440177-4 1993 Both DAG and Ca2+i activate PKC. Diglycerides 5-8 proline rich transmembrane protein 2 Homo sapiens 28-31 8432785-6 1993 The PKC stimulatory factor in amnion cytosol was stable to heat treatment at 80-90 C for 2 min (control + heat-treated CS, 23.20 +/- 1.2; control + heat-treated SL, 24.49 +/- 1.0 pmol/min) and substituted for phosphatidylserine and diacylglycerol in the PKC assay (control, no lipids, 0.05 +/- 0.04 pmol/min; control + amnion cytosol, no lipids, 9.60 +/- 1.06 pmol/min). Diglycerides 232-246 proline rich transmembrane protein 2 Homo sapiens 4-7 8480534-1 1993 The serine/threonine protein kinase, protein kinase C (PKC) is a family of closely related isoforms which are physiologically activated by diacylglycerol generated by the binding of a variety of agonists to their cellular receptors. Diglycerides 139-153 proline rich transmembrane protein 2 Homo sapiens 37-53 8480534-1 1993 The serine/threonine protein kinase, protein kinase C (PKC) is a family of closely related isoforms which are physiologically activated by diacylglycerol generated by the binding of a variety of agonists to their cellular receptors. Diglycerides 139-153 proline rich transmembrane protein 2 Homo sapiens 55-58 1303731-1 1992 Activation of protein kinase C (PKC) is regulated by dual second messengers; diacylglycerol (DG) produced by receptor mediated hydrolysis of phosphatidylinositol and Ca2+ which is released by inositol 1,4,5-triphosphate (IP3) from intracellular stores in the endoplasmic reticulum. Diglycerides 77-91 proline rich transmembrane protein 2 Homo sapiens 32-35 1498520-3 1992 PKC is involved in many cell processes such as the transduction of hormonal signals and the machinery of cellular secretion and is activated by diacylglycerol and by a number of phorbol esters, including phorbol myristic acid (PMA). Diglycerides 144-158 proline rich transmembrane protein 2 Homo sapiens 0-3 1468079-0 1992 Synthesis of diacylglycerol analogues as potential second-messenger antagonists and inhibitors of protein kinase C. Diglycerides 13-27 proline rich transmembrane protein 2 Homo sapiens 98-114 1468079-1 1992 A series of analogues of diacylglycerol has been prepared and tested as inhibitors of protein kinase C (PKC). Diglycerides 25-39 proline rich transmembrane protein 2 Homo sapiens 86-102 1468079-1 1992 A series of analogues of diacylglycerol has been prepared and tested as inhibitors of protein kinase C (PKC). Diglycerides 25-39 proline rich transmembrane protein 2 Homo sapiens 104-107 1528172-1 1992 Cerebral ischemia leads to a number of biochemical and molecular changes which include increase in intracellular calcium, arachidonic acid, and diacylglycerol, all of which are capable of activating protein kinase C (PKC). Diglycerides 144-158 proline rich transmembrane protein 2 Homo sapiens 199-215 1528172-1 1992 Cerebral ischemia leads to a number of biochemical and molecular changes which include increase in intracellular calcium, arachidonic acid, and diacylglycerol, all of which are capable of activating protein kinase C (PKC). Diglycerides 144-158 proline rich transmembrane protein 2 Homo sapiens 217-220 1323204-6 1992 Treatment of platelets with inhibitors of PKC potentiates DAG mass formation in response to thrombin while prior activation of PKC with phorbol esters blocks DAG mass formation, consistent with PKC playing a negative feedback role, inhibiting inositol phospholipid breakdown. Diglycerides 58-61 proline rich transmembrane protein 2 Homo sapiens 42-45 1370476-11 1992 Furthermore, in the absence of PMA, activation of PKC by diacylglycerol provides a negative feedback signal responsible for reducing the phosphotyrosine contents of PLC-gamma 1. Diglycerides 57-71 proline rich transmembrane protein 2 Homo sapiens 50-53 1736894-3 1992 Addition of phorbol 12-myristate-13-acetate or the membrane-permeant diacylglycerol analogue 1-oleoyl-2-acetylglycerol, which are potent activators of PKC, to bovine spermatozoa resulted in stimulation of the acrosome reaction. Diglycerides 69-83 proline rich transmembrane protein 2 Homo sapiens 151-154 1323204-6 1992 Treatment of platelets with inhibitors of PKC potentiates DAG mass formation in response to thrombin while prior activation of PKC with phorbol esters blocks DAG mass formation, consistent with PKC playing a negative feedback role, inhibiting inositol phospholipid breakdown. Diglycerides 158-161 proline rich transmembrane protein 2 Homo sapiens 127-130 1323204-6 1992 Treatment of platelets with inhibitors of PKC potentiates DAG mass formation in response to thrombin while prior activation of PKC with phorbol esters blocks DAG mass formation, consistent with PKC playing a negative feedback role, inhibiting inositol phospholipid breakdown. Diglycerides 158-161 proline rich transmembrane protein 2 Homo sapiens 127-130 1323204-9 1992 We have found that fibroblasts which overexpress the beta 1 isozyme of PKC display greatly enhanced DAG formation and phospholipase D activation in response to phorbol ester treatment. Diglycerides 100-103 proline rich transmembrane protein 2 Homo sapiens 71-74 1820763-1 1991 A model for the binding of two activators of protein kinase C (PKC), the phorbol ester 12-O-tetradecanoylphorbol-13-acetate (TPA) and diacylglycerol, to the enzyme is proposed. Diglycerides 134-148 proline rich transmembrane protein 2 Homo sapiens 45-61 1660266-2 1991 Diacylglycerol (DG) and its analogue phorbol 12-myristate 13-acetate (PMA) activate the ubiquitous phospholipid/Ca2(+)-dependent protein kinase, protein kinase C (PKC), and cause it to become tightly associated with membranes. Diglycerides 0-14 proline rich transmembrane protein 2 Homo sapiens 145-161 1660266-2 1991 Diacylglycerol (DG) and its analogue phorbol 12-myristate 13-acetate (PMA) activate the ubiquitous phospholipid/Ca2(+)-dependent protein kinase, protein kinase C (PKC), and cause it to become tightly associated with membranes. Diglycerides 0-14 proline rich transmembrane protein 2 Homo sapiens 163-166 1928372-8 1991 In this report, we show that an increase in medium glucose concentration resulted in an increase in diacylglycerol (DAG) mass and transiently increased protein kinase C (PKC) activity as assessed by the translocation of PKC from the soluble to the particulate fraction. Diglycerides 116-119 proline rich transmembrane protein 2 Homo sapiens 220-223 1908797-5 1991 The result implies that, in addition to diacylglycerol, the receptor-mediated release of unsaturated FFA"s from membrane phospholipids may also take part in the activation of PKC. Diglycerides 40-54 proline rich transmembrane protein 2 Homo sapiens 175-178 1915590-5 1991 Chloroform was the most potent activator stimulating PKC phosphotransferase activity up to a level 40% of that obtained by the endogenous activator, diacylglycerol. Diglycerides 149-163 proline rich transmembrane protein 2 Homo sapiens 53-56 1850993-1 1991 Phosphatidylinositol 4,5-bisphosphate (PIP2) as well as diacylglycerol (DG) activate protein kinase C (PKC) in the presence of calcium and phosphatidylserine. Diglycerides 56-70 proline rich transmembrane protein 2 Homo sapiens 103-106 2043240-2 1991 Diacylglycerols (DAGs, the endogenous PKC activators) are generated in response to insulin secretagogues, although nutrient and non-nutrient secretagogues generate DAGs of different compositions and of different potencies as PKC activators. Diglycerides 0-15 proline rich transmembrane protein 2 Homo sapiens 38-41 2043240-2 1991 Diacylglycerols (DAGs, the endogenous PKC activators) are generated in response to insulin secretagogues, although nutrient and non-nutrient secretagogues generate DAGs of different compositions and of different potencies as PKC activators. Diglycerides 17-21 proline rich transmembrane protein 2 Homo sapiens 38-41 2043240-2 1991 Diacylglycerols (DAGs, the endogenous PKC activators) are generated in response to insulin secretagogues, although nutrient and non-nutrient secretagogues generate DAGs of different compositions and of different potencies as PKC activators. Diglycerides 17-21 proline rich transmembrane protein 2 Homo sapiens 225-228 1820763-1 1991 A model for the binding of two activators of protein kinase C (PKC), the phorbol ester 12-O-tetradecanoylphorbol-13-acetate (TPA) and diacylglycerol, to the enzyme is proposed. Diglycerides 134-148 proline rich transmembrane protein 2 Homo sapiens 63-66 2246518-3 1990 This priming event induces the following changes in signal transduction between the opsonin receptors (in particular the CR3 receptor) and activation of the respiratory burst: 1) an enhanced activation of protein kinase C (PK-C): the initiation of the respiratory burst in untreated eosinophils is not sensitive to PK-C inhibition (via staurosporine) and is not accompanied by accumulation of diglycerides and changes in [Ca2+]i. Diglycerides 393-405 proline rich transmembrane protein 2 Homo sapiens 205-221 1985909-6 1991 PKC associated to the lipid layer exhibited the expected catalytic property and was fully activated when diacylglycerol or TPA was included in the membrane. Diglycerides 105-119 proline rich transmembrane protein 2 Homo sapiens 0-3 1985909-8 1991 Study of the compression isotherm of various diacylglycerol structures revealed that all potent PKC agonists exhibited an expanded liquid phase behavior with collapse pressure below 40 dynes/cm, in contrast to weak activators which showed condensed isotherms with high collapse pressure (approximately equal to 60 dynes/cm). Diglycerides 45-59 proline rich transmembrane protein 2 Homo sapiens 96-99 1985909-10 1991 They are in line with the suggestion of a major role of Ca2+ in the association (translocation) of PKC to membrane in living cell and suggest that diacylglycerol (and TPA) might activate membrane-associated PKC through local change in the surrounding lipid phase organization. Diglycerides 147-161 proline rich transmembrane protein 2 Homo sapiens 99-102 1985909-10 1991 They are in line with the suggestion of a major role of Ca2+ in the association (translocation) of PKC to membrane in living cell and suggest that diacylglycerol (and TPA) might activate membrane-associated PKC through local change in the surrounding lipid phase organization. Diglycerides 147-161 proline rich transmembrane protein 2 Homo sapiens 207-210 2268301-5 1990 This region of PKC has been implicated in the binding of diacylglycerol and phorbol esters in a phospholipid-dependent fashion. Diglycerides 57-71 proline rich transmembrane protein 2 Homo sapiens 15-18 2246518-3 1990 This priming event induces the following changes in signal transduction between the opsonin receptors (in particular the CR3 receptor) and activation of the respiratory burst: 1) an enhanced activation of protein kinase C (PK-C): the initiation of the respiratory burst in untreated eosinophils is not sensitive to PK-C inhibition (via staurosporine) and is not accompanied by accumulation of diglycerides and changes in [Ca2+]i. Diglycerides 393-405 proline rich transmembrane protein 2 Homo sapiens 223-227 2165391-5 1990 To determine the threshold values of the concentrations of Ca2+ and diacylglycerol required to produce a redistribution of PKC, the hepatocytes were treated with the Ca2+ ionophore ionomycin, and with permeant diacylglycerol derivatives. Diglycerides 68-82 proline rich transmembrane protein 2 Homo sapiens 123-126 1976320-2 1990 Evoked acetylcholine release was increased by a diacylglycerol analog that activates PKC and was decreased by H-7, a blocker of PKC. Diglycerides 48-62 proline rich transmembrane protein 2 Homo sapiens 85-88 1976320-2 1990 Evoked acetylcholine release was increased by a diacylglycerol analog that activates PKC and was decreased by H-7, a blocker of PKC. Diglycerides 48-62 proline rich transmembrane protein 2 Homo sapiens 128-131 2271522-12 1990 These studies also suggested that calcium-dependent PKC-membrane binding and PKC function could be regulated by a number of factors in addition to calcium levels and diacylglycerol content of the membrane. Diglycerides 166-180 proline rich transmembrane protein 2 Homo sapiens 52-55 2271522-12 1990 These studies also suggested that calcium-dependent PKC-membrane binding and PKC function could be regulated by a number of factors in addition to calcium levels and diacylglycerol content of the membrane. Diglycerides 166-180 proline rich transmembrane protein 2 Homo sapiens 77-80 2335502-5 1990 The factor in the soluble fraction that activated the membrane-associated oxidase was demonstrated to be protein kinase C (PKC) by several criteria, including its Ca2+/phophatidylserine/diacyl-glycerol-stimulated histone kinase activity, its response to phorbol ester, its inhibition by a PKC pseudosubstrate peptide, and its replacement by purified mammalian PKC. Diglycerides 186-201 proline rich transmembrane protein 2 Homo sapiens 105-121 2335502-5 1990 The factor in the soluble fraction that activated the membrane-associated oxidase was demonstrated to be protein kinase C (PKC) by several criteria, including its Ca2+/phophatidylserine/diacyl-glycerol-stimulated histone kinase activity, its response to phorbol ester, its inhibition by a PKC pseudosubstrate peptide, and its replacement by purified mammalian PKC. Diglycerides 186-201 proline rich transmembrane protein 2 Homo sapiens 123-126 2173467-11 1990 Another hydrolysis product is diacylglycerol (DAG) that binds principally to protein kinase C (PKC). Diglycerides 30-44 proline rich transmembrane protein 2 Homo sapiens 77-93 2400822-2 1990 Protein kinase C (PKC) belongs to the inositol 1, 4, 5 trisphosphate/diacylglycerol (IP3/DG) pathway and plays a key role in cell regulation. Diglycerides 69-83 proline rich transmembrane protein 2 Homo sapiens 0-16 2400822-2 1990 Protein kinase C (PKC) belongs to the inositol 1, 4, 5 trisphosphate/diacylglycerol (IP3/DG) pathway and plays a key role in cell regulation. Diglycerides 69-83 proline rich transmembrane protein 2 Homo sapiens 18-21 2173467-11 1990 Another hydrolysis product is diacylglycerol (DAG) that binds principally to protein kinase C (PKC). Diglycerides 30-44 proline rich transmembrane protein 2 Homo sapiens 95-98 2173467-11 1990 Another hydrolysis product is diacylglycerol (DAG) that binds principally to protein kinase C (PKC). Diglycerides 46-49 proline rich transmembrane protein 2 Homo sapiens 77-93 2173467-11 1990 Another hydrolysis product is diacylglycerol (DAG) that binds principally to protein kinase C (PKC). Diglycerides 46-49 proline rich transmembrane protein 2 Homo sapiens 95-98 2173467-16 1990 DAG can also induce LH secretion, this mechanism uses PKC activation and requires gonadotrophin neosynthesis. Diglycerides 0-3 proline rich transmembrane protein 2 Homo sapiens 54-57 2697470-3 1989 PKC is directly activated in vivo by the second messenger diacylglycerol, a lipid produced by phospholipase C-catalyzed hydrolysis of phosphatidylinositol and polyphosphoinositides. Diglycerides 58-72 proline rich transmembrane protein 2 Homo sapiens 0-3 35492590-13 2022 Upon extracellular stimulation, diacylglycerol (DAG) and calcium ion (Ca2+) generated at the membrane bind PKC. Diglycerides 32-46 proline rich transmembrane protein 2 Homo sapiens 107-110 35492590-13 2022 Upon extracellular stimulation, diacylglycerol (DAG) and calcium ion (Ca2+) generated at the membrane bind PKC. Diglycerides 48-51 proline rich transmembrane protein 2 Homo sapiens 107-110 2697470-4 1989 Diacylglycerol activates PKC by reducing the enzyme"s requirement for Ca2+. Diglycerides 0-14 proline rich transmembrane protein 2 Homo sapiens 25-28 2697470-5 1989 Phorbol ester tumor promoters and related agents potently activate PKC by a mechanism analogous to that of diacylglycerol, providing evidence that PKC activation is a critical event in tumor promotion. Diglycerides 107-121 proline rich transmembrane protein 2 Homo sapiens 147-150 2583546-3 1989 However, a significant increase in diacylglycerol (DAG) levels due to 5-HPETE was observed, which in turn activated the protein kinase C (PKC). Diglycerides 35-49 proline rich transmembrane protein 2 Homo sapiens 120-136 2611232-0 1989 Differences in the effects of phorbol esters and diacylglycerols on protein kinase C. Diglycerides 49-64 proline rich transmembrane protein 2 Homo sapiens 68-84 2611232-6 1989 Diacylglycerols (DAG) participated in forming an active PKC which was reversibly bound to the membrane. Diglycerides 0-15 proline rich transmembrane protein 2 Homo sapiens 56-59 2611232-6 1989 Diacylglycerols (DAG) participated in forming an active PKC which was reversibly bound to the membrane. Diglycerides 17-20 proline rich transmembrane protein 2 Homo sapiens 56-59 2611232-8 1989 DAG functioned poorly in generating the constitutively active, irreversible PKC-membrane complex. Diglycerides 0-3 proline rich transmembrane protein 2 Homo sapiens 76-79 2611232-12 1989 Despite these striking differences, DAG prevented binding of phorbol esters to high-affinity sites on the PKC-membrane complex. Diglycerides 36-39 proline rich transmembrane protein 2 Homo sapiens 106-109 2561951-3 1989 The effect appeared to be mediated by PKC since diacylglycerols caused the same amplification as did TPA while inactive phorbol esters were without effect. Diglycerides 48-63 proline rich transmembrane protein 2 Homo sapiens 38-41 2653649-8 1989 These studies suggested that, although PK-C was activated by diacylglycerol, another kinase, S6 kinase, was the effector enzyme involved in the phosphorylation of the 40S protein. Diglycerides 61-75 proline rich transmembrane protein 2 Homo sapiens 39-43 2583546-3 1989 However, a significant increase in diacylglycerol (DAG) levels due to 5-HPETE was observed, which in turn activated the protein kinase C (PKC). Diglycerides 35-49 proline rich transmembrane protein 2 Homo sapiens 138-141 2583546-3 1989 However, a significant increase in diacylglycerol (DAG) levels due to 5-HPETE was observed, which in turn activated the protein kinase C (PKC). Diglycerides 51-54 proline rich transmembrane protein 2 Homo sapiens 120-136 2583546-3 1989 However, a significant increase in diacylglycerol (DAG) levels due to 5-HPETE was observed, which in turn activated the protein kinase C (PKC). Diglycerides 51-54 proline rich transmembrane protein 2 Homo sapiens 138-141 25291103-1 1986 Protein kinase C (PKC) is activated when a T cell is stimulated by antigen or mitogen: the binding of receptor and ligand induces hydrolysis of phosphatidylinositol phosphates and production of the PKC activating substance diacylglycerol. Diglycerides 223-237 proline rich transmembrane protein 2 Homo sapiens 0-16 25291103-1 1986 Protein kinase C (PKC) is activated when a T cell is stimulated by antigen or mitogen: the binding of receptor and ligand induces hydrolysis of phosphatidylinositol phosphates and production of the PKC activating substance diacylglycerol. Diglycerides 223-237 proline rich transmembrane protein 2 Homo sapiens 18-21 25291103-1 1986 Protein kinase C (PKC) is activated when a T cell is stimulated by antigen or mitogen: the binding of receptor and ligand induces hydrolysis of phosphatidylinositol phosphates and production of the PKC activating substance diacylglycerol. Diglycerides 223-237 proline rich transmembrane protein 2 Homo sapiens 198-201 2836072-5 1988 The diacylglycerol derivative OAG increased NK cell killing and activated PKC from human lymphocytes. Diglycerides 4-18 proline rich transmembrane protein 2 Homo sapiens 74-77 3128979-6 1988 PKC may be a long-term cell regulator which becomes inserted into the membrane upon appearance of the second messengers, calcium and diacylglycerol, and remains in an active membrane-bound state when the second messengers have been removed. Diglycerides 133-147 proline rich transmembrane protein 2 Homo sapiens 0-3