PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 8568825-3 1996 Conformationally constrained analogues of diacylglycerol (DAG) built on a 5(-)[(acyloxy)methyl]-5-(hydroxymethyl)tetrahydro-2-furanone template (1, Chart 1) were shown previously to bind tightly to protein kinase C alpha (PK-C alpha) in a stereospecific manner. Diglycerides 42-56 protein kinase C, alpha Mus musculus 198-220 10036317-8 1999 Finally, the concentration of diacylglycerol in the homozygous TIFF was significantly increased and this elevation may modulate PKC distribution and function. Diglycerides 30-44 protein kinase C, alpha Mus musculus 128-131 8751970-1 1996 Treatment of mice with multiple topical applications of 12-O-tetradecanoylphorbol-13-acetate (TPA) or diacylglycerol resulted in a preferential decrease in epidermal protein kinase C-beta 2 (PKC-beta 2) compared with PKC-alpha as determined by western analysis. Diglycerides 102-116 protein kinase C, alpha Mus musculus 217-226 8751970-2 1996 When PKC-alpha was decreased by 40%, PKC-beta 2 could no longer be detected, suggesting that PKC-beta 2 is more sensitive to downregulation, and/or specific epidermal cell types that contain PKC-beta 2 are more sensitive to TPA/diacylglycerol. Diglycerides 228-242 protein kinase C, alpha Mus musculus 5-14 9001227-3 1997 Previous studies implicated hydrolysis of phosphatidylcholine (PC) in Raf activation; therefore, we investigated the role of the epsilon isotype of protein kinase C (PKC), which is stimulated by PC-derived diacylglycerol, as a Raf activator. Diglycerides 206-220 protein kinase C, alpha Mus musculus 166-169 9001227-8 1997 In addition, constitutively active mutants of both PKC alpha and PKC epsilon overcame the inhibitory effects of dominant negative mutants of the other PKC isotype, indicating that these diacylglycerol-regulated PKCs function as redundant activators of Raf-1 in vivo. Diglycerides 186-200 protein kinase C, alpha Mus musculus 51-60 9001227-8 1997 In addition, constitutively active mutants of both PKC alpha and PKC epsilon overcame the inhibitory effects of dominant negative mutants of the other PKC isotype, indicating that these diacylglycerol-regulated PKCs function as redundant activators of Raf-1 in vivo. Diglycerides 186-200 protein kinase C, alpha Mus musculus 51-54 8568825-3 1996 Conformationally constrained analogues of diacylglycerol (DAG) built on a 5(-)[(acyloxy)methyl]-5-(hydroxymethyl)tetrahydro-2-furanone template (1, Chart 1) were shown previously to bind tightly to protein kinase C alpha (PK-C alpha) in a stereospecific manner. Diglycerides 42-56 protein kinase C, alpha Mus musculus 222-232 8568825-3 1996 Conformationally constrained analogues of diacylglycerol (DAG) built on a 5(-)[(acyloxy)methyl]-5-(hydroxymethyl)tetrahydro-2-furanone template (1, Chart 1) were shown previously to bind tightly to protein kinase C alpha (PK-C alpha) in a stereospecific manner. Diglycerides 58-61 protein kinase C, alpha Mus musculus 198-220 8568825-3 1996 Conformationally constrained analogues of diacylglycerol (DAG) built on a 5(-)[(acyloxy)methyl]-5-(hydroxymethyl)tetrahydro-2-furanone template (1, Chart 1) were shown previously to bind tightly to protein kinase C alpha (PK-C alpha) in a stereospecific manner. Diglycerides 58-61 protein kinase C, alpha Mus musculus 222-232 8568825-14 1996 As expected, these DAG analogues activated PK-C alpha. Diglycerides 19-22 protein kinase C, alpha Mus musculus 43-53 8226926-9 1993 These results show for the first time that specific isoforms of PKC are down-regulated at the protein level during proliferation of murine melanocytic cells and suggest that the constitutive down-regulation of PKC in transformed melanoma cells may arise as a consequence of elevated endogenous phosphatidylinositol-derived diacylglycerol levels. Diglycerides 323-337 protein kinase C, alpha Mus musculus 210-213 8082717-8 1994 Since EGF can induce both PKC activation and cell proliferation, and because PKC activation requires membrane-derived phospholipids and diacylglycerol, these data suggest that specific fatty acid modulation of mammary epithelial cell mitogenesis is mediated through alterations in PKC alpha activation. Diglycerides 136-150 protein kinase C, alpha Mus musculus 77-80 8226926-8 1993 Hourly treatments of quiescent Mel-ab melanocytes with the synthetic diacylglycerol analogue, 1,2-dioctanoyl-sn-glycerol, for 24 h, resulted in an induction of DNA synthesis which was associated with a significant down-regulation of PKC levels mediated largely via post-translational rather than transcriptional mechanisms. Diglycerides 69-83 protein kinase C, alpha Mus musculus 233-236 8226926-9 1993 These results show for the first time that specific isoforms of PKC are down-regulated at the protein level during proliferation of murine melanocytic cells and suggest that the constitutive down-regulation of PKC in transformed melanoma cells may arise as a consequence of elevated endogenous phosphatidylinositol-derived diacylglycerol levels. Diglycerides 323-337 protein kinase C, alpha Mus musculus 64-67 29844158-1 2018 Conventional protein kinase C (PKC) family members are reversibly activated by binding to the second messengers Ca2+ and diacylglycerol, events that break autoinhibitory constraints to allow the enzyme to adopt an active, but degradation-sensitive, conformation. Diglycerides 121-135 protein kinase C, alpha Mus musculus 31-34 11278470-3 2001 Nuclear diacylglycerol provides the driving force for the nuclear translocation of protein kinase C (PKC) alpha. Diglycerides 8-22 protein kinase C, alpha Mus musculus 83-111 27226533-2 2016 Activation of conventional and novel PKC isoforms is associated with their Ca(2+)- and/or diacylglycerol (DAG)-dependent translocation to the plasma membrane. Diglycerides 90-104 protein kinase C, alpha Mus musculus 37-40 27226533-2 2016 Activation of conventional and novel PKC isoforms is associated with their Ca(2+)- and/or diacylglycerol (DAG)-dependent translocation to the plasma membrane. Diglycerides 106-109 protein kinase C, alpha Mus musculus 37-40 25157099-13 2014 Reduced activation of protein kinase Calpha (PKCalpha), which is increased by DAG and ceramides, paralleled the reductions in these lipids. Diglycerides 78-81 protein kinase C, alpha Mus musculus 22-43 25157099-13 2014 Reduced activation of protein kinase Calpha (PKCalpha), which is increased by DAG and ceramides, paralleled the reductions in these lipids. Diglycerides 78-81 protein kinase C, alpha Mus musculus 45-53 25861124-2 2014 We reported that oxidized diacylglycerol (DAG), which is an activator of PKC, had a remarkably stronger PKC-activating action than un-oxidized DAG. Diglycerides 26-40 protein kinase C, alpha Mus musculus 73-76 25861124-2 2014 We reported that oxidized diacylglycerol (DAG), which is an activator of PKC, had a remarkably stronger PKC-activating action than un-oxidized DAG. Diglycerides 26-40 protein kinase C, alpha Mus musculus 104-107 25861124-2 2014 We reported that oxidized diacylglycerol (DAG), which is an activator of PKC, had a remarkably stronger PKC-activating action than un-oxidized DAG. Diglycerides 42-45 protein kinase C, alpha Mus musculus 73-76 25861124-2 2014 We reported that oxidized diacylglycerol (DAG), which is an activator of PKC, had a remarkably stronger PKC-activating action than un-oxidized DAG. Diglycerides 42-45 protein kinase C, alpha Mus musculus 104-107 25861124-2 2014 We reported that oxidized diacylglycerol (DAG), which is an activator of PKC, had a remarkably stronger PKC-activating action than un-oxidized DAG. Diglycerides 143-146 protein kinase C, alpha Mus musculus 73-76 25861124-10 2014 The above results strongly suggested that oxidized DAG, which is increased by augmented oxidative stress, activated PKCalpha, betaI, betaII and delta molecular species and that these molecular species in turn stimulated the phosphorylation of MAP kinases including ERK and JNK, resulting in enhancement of hepatic fibrogenesis. Diglycerides 51-54 protein kinase C, alpha Mus musculus 116-124 23525016-4 2013 We show transient translocation of PKCalpha to the IS, mediated by DAG generation at the contact area. Diglycerides 67-70 protein kinase C, alpha Mus musculus 35-43 23525016-7 2013 Analysis of DGKzeta-deficient mice further showed that increased DAG signaling is translated to downstream elements of this pathway, as reflected by enhanced PKCalpha-dependent L-selectin shedding. Diglycerides 65-68 protein kinase C, alpha Mus musculus 158-166 21232169-1 2012 Protein kinase C (PKC) is a family of Ser/Thr protein kinases that can be activated by Ca2+, phospholipid and diacylglycerol. Diglycerides 110-124 protein kinase C, alpha Mus musculus 18-21 19580852-10 2009 Calcium and DAG together activate PKCalpha which switches the disinhibition to increased inhibition of mitral cells. Diglycerides 12-15 protein kinase C, alpha Mus musculus 34-42 26586831-4 2015 Here, we analyzed the role of diacylglycerol kinase zeta (DGKzeta), a kinase that physically interacts with PKCalpha as well as postsynaptic density protein 95 (PSD-95) family proteins and functionally suppresses PKCalpha by metabolizing diacylglycerol (DAG), in the regulation of cerebellar LTD. Diglycerides 30-44 protein kinase C, alpha Mus musculus 108-116 26586831-4 2015 Here, we analyzed the role of diacylglycerol kinase zeta (DGKzeta), a kinase that physically interacts with PKCalpha as well as postsynaptic density protein 95 (PSD-95) family proteins and functionally suppresses PKCalpha by metabolizing diacylglycerol (DAG), in the regulation of cerebellar LTD. Diglycerides 30-44 protein kinase C, alpha Mus musculus 213-221 22484374-3 2012 LPL activates phospholipase C (PLC), and resulting inositol trisphosphate (IP(3)) and diacylglycerol contribute to PKCalpha activation and downstream activation of ERK1/2. Diglycerides 86-100 protein kinase C, alpha Mus musculus 115-123 15198639-4 2004 The zinc-finger motifs modulate diacylglycerol binding; thus, intracellular zinc concentrations could influence the activity and localization of PKC family members. Diglycerides 32-46 protein kinase C, alpha Mus musculus 145-148 12417016-1 2002 The gamma isotype of protein kinase C (PKC gamma) is a member of the classical PKC (cPKC) subfamily which is activated by Ca(2+) and diacylglycerol in the presence of phosphatidylserine. Diglycerides 133-147 protein kinase C, alpha Mus musculus 39-42 11923480-2 2002 The role of diacylglycerol-sensitive PKC isoforms is less clear as they have been suggested to be both activated by insulin and yet inhibit insulin signaling to PI3K. Diglycerides 12-26 protein kinase C, alpha Mus musculus 37-40 10887171-6 2000 Since PKC is activated directly by diacylglycerol and inactivated indirectly by ceramide, we next examined the roles of these lipid mediators in the regulation of PKC alpha. Diglycerides 35-49 protein kinase C, alpha Mus musculus 6-9 10887171-9 2000 The diacylglycerol mimic phorbol 12-myristate 13-acetate was sufficient to cause translocation of PKC alpha, but not the mobility shift. Diglycerides 4-18 protein kinase C, alpha Mus musculus 98-107 10706086-3 2000 In insulin-like growth factor (IGF)-I-stimulated Swiss 3T3 cells, a transient elevation of intranuclear DAG levels is essential for attracting the alpha isoform of protein kinase C (PKC) to the nucleus. Diglycerides 104-107 protein kinase C, alpha Mus musculus 182-185 10706086-4 2000 Previous evidence has shown that the nucleus also contains DAG kinase, i.e., the enzyme that yields phosphatidic acid from DAG, thus terminating PKC-mediated signaling events. Diglycerides 59-62 protein kinase C, alpha Mus musculus 145-148 10571540-4 1999 We now demonstrate changes in the level, activity, or both of several signaling components, including changes in the amount and hormone responsiveness of phospholipase Cbeta enzymes, in the basal level of diacylglycerol (which predominantly reflects activation of phospholipase D), in the amount or distribution of protein kinase C (PKC) isoforms (PKCalpha, PKCdelta, and PKCepsilon), and in the amount of several endogenous G proteins. Diglycerides 205-219 protein kinase C, alpha Mus musculus 333-336 10571540-4 1999 We now demonstrate changes in the level, activity, or both of several signaling components, including changes in the amount and hormone responsiveness of phospholipase Cbeta enzymes, in the basal level of diacylglycerol (which predominantly reflects activation of phospholipase D), in the amount or distribution of protein kinase C (PKC) isoforms (PKCalpha, PKCdelta, and PKCepsilon), and in the amount of several endogenous G proteins. Diglycerides 205-219 protein kinase C, alpha Mus musculus 348-356