메뉴 건너뛰기




Volumn 1, Issue C, 1996, Pages 337-366

Diacylglycerol metabolism in cellular membranes

Author keywords

[No Author keywords available]

Indexed keywords


EID: 3643084332     PISSN: 18745245     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1874-5245(96)80014-0     Document Type: Review
Times cited : (2)

References (188)
  • 1
    • 0026539220 scopus 로고
    • Selective changes in protein kinase C isoenzymes in rat liver nuclei during liver regeneration
    • Alessenko A., Khan W.A., Wetsel W.C., and Hannun Y.A. Selective changes in protein kinase C isoenzymes in rat liver nuclei during liver regeneration. Biochem. Biophys. Res. Commun. 182 (1992) 1333-1339
    • (1992) Biochem. Biophys. Res. Commun. , vol.182 , pp. 1333-1339
    • Alessenko, A.1    Khan, W.A.2    Wetsel, W.C.3    Hannun, Y.A.4
  • 2
    • 0023338803 scopus 로고
    • Metabolism of extracellular phospholipids in Tetrahymena pyriformis
    • Arai H., Nishikawa K., Inoue K., Nozawa Y., and Nojima S. Metabolism of extracellular phospholipids in Tetrahymena pyriformis. J. Biochem. Tokyo 101 (1987) 1059-1067
    • (1987) J. Biochem. Tokyo , vol.101 , pp. 1059-1067
    • Arai, H.1    Nishikawa, K.2    Inoue, K.3    Nozawa, Y.4    Nojima, S.5
  • 3
    • 0026777099 scopus 로고
    • IL-4 receptor signal transduction in human monocytes is associated with protein kinase C translocation
    • Arruda S., and Ho J.L. IL-4 receptor signal transduction in human monocytes is associated with protein kinase C translocation. J. Immunol. 149 (1992) 1258-1264
    • (1992) J. Immunol. , vol.149 , pp. 1258-1264
    • Arruda, S.1    Ho, J.L.2
  • 4
    • 0024268342 scopus 로고
    • Selective priming of rate and duration of the respiratory burst of neutrophils by 1,2-diacyl and 1-O-alkyl-2-acyl diglycerides. Possible relation to effects on protein kinase C
    • Bass D.A., McPhail L.C., Schmitt J.D., Morris-Natschke S., McCall C.E., and Wykle R.L. Selective priming of rate and duration of the respiratory burst of neutrophils by 1,2-diacyl and 1-O-alkyl-2-acyl diglycerides. Possible relation to effects on protein kinase C. J. Biol. Chem. 263 (1989) 19610-19617
    • (1989) J. Biol. Chem. , vol.263 , pp. 19610-19617
    • Bass, D.A.1    McPhail, L.C.2    Schmitt, J.D.3    Morris-Natschke, S.4    McCall, C.E.5    Wykle, R.L.6
  • 6
    • 77956911585 scopus 로고
    • Enzymes of triacylglycerol formation in mammals
    • Boyer P.D. (Ed), Academic Press, New York
    • Bell R.M., and Coleman R.A. Enzymes of triacylglycerol formation in mammals. In: Boyer P.D. (Ed). The Enzymes (1983), Academic Press, New York
    • (1983) The Enzymes
    • Bell, R.M.1    Coleman, R.A.2
  • 10
    • 0025257196 scopus 로고
    • Protein kinase C and T cell activation
    • Berry N., and Nishizuka Y. Protein kinase C and T cell activation. Eur. J. Biochem. 189 (1990) 205-214
    • (1990) Eur. J. Biochem. , vol.189 , pp. 205-214
    • Berry, N.1    Nishizuka, Y.2
  • 11
    • 0024366057 scopus 로고
    • Phosphatidylcholine hydrolysis by phospholipase D determines phosphatidate and diglyceride levels in chemotactic peptide-stimulated human neutrophils. Involvement of phosphatidate phosphohydrolase in signal transduction
    • Billah M.M., Eckel S., Mullmann T.J., Egan R.W., and Siegel M.I. Phosphatidylcholine hydrolysis by phospholipase D determines phosphatidate and diglyceride levels in chemotactic peptide-stimulated human neutrophils. Involvement of phosphatidate phosphohydrolase in signal transduction. J. Biol. Chem. 264 (1989) 17069-17077
    • (1989) J. Biol. Chem. , vol.264 , pp. 17069-17077
    • Billah, M.M.1    Eckel, S.2    Mullmann, T.J.3    Egan, R.W.4    Siegel, M.I.5
  • 12
    • 0023927373 scopus 로고
    • Functions of diacylglycerol in glycerolipid metabolism, signal transduction and cellular transformation
    • Bishop W.R., and Bell R.M. Functions of diacylglycerol in glycerolipid metabolism, signal transduction and cellular transformation. Oncogene Res. 2 (1988) 205-218
    • (1988) Oncogene Res. , vol.2 , pp. 205-218
    • Bishop, W.R.1    Bell, R.M.2
  • 13
    • 0024455864 scopus 로고
    • An early elevation of diacylglycerol and phosphatidate in regenerating liver
    • Bocckino S.B., Wilson P.B., and Exton J.H. An early elevation of diacylglycerol and phosphatidate in regenerating liver. Biochem. Biophys. Res. Commun. 164 (1989) 290-294
    • (1989) Biochem. Biophys. Res. Commun. , vol.164 , pp. 290-294
    • Bocckino, S.B.1    Wilson, P.B.2    Exton, J.H.3
  • 14
    • 0023874911 scopus 로고
    • Activators of protein kinase C potentiate electrically stimulated hormone secretion from the rat's isolated neurohypophysis
    • Bondy C.A., and Gainer H. Activators of protein kinase C potentiate electrically stimulated hormone secretion from the rat's isolated neurohypophysis. Neurosci. Lett. 89 (1988) 97-101
    • (1988) Neurosci. Lett. , vol.89 , pp. 97-101
    • Bondy, C.A.1    Gainer, H.2
  • 15
    • 0023900124 scopus 로고
    • Protein kinase C in mouse kidney: Subcellular distribution and endogenous substrates
    • Boneh A., and Tenenhouse H.S. Protein kinase C in mouse kidney: Subcellular distribution and endogenous substrates. Biochem. Cell Biol. 66 (1988) 262-272
    • (1988) Biochem. Cell Biol. , vol.66 , pp. 262-272
    • Boneh, A.1    Tenenhouse, H.S.2
  • 16
    • 0025831191 scopus 로고
    • A phosphatidic acid-sensitive intracellular pool of calcium is released by anti-CD3 in Jurkat T cells
    • Breittmayer J.P., Aussel C., Farahifar D., Cousin J.L., and Fehlmann M. A phosphatidic acid-sensitive intracellular pool of calcium is released by anti-CD3 in Jurkat T cells. Immunology 73 (1991) 134-139
    • (1991) Immunology , vol.73 , pp. 134-139
    • Breittmayer, J.P.1    Aussel, C.2    Farahifar, D.3    Cousin, J.L.4    Fehlmann, M.5
  • 17
    • 0021566523 scopus 로고
    • Intracellular translocation of phosphatidate phosphohydrolase and its possible role in the control of glycerolipid synthesis
    • Brindley D.N. Intracellular translocation of phosphatidate phosphohydrolase and its possible role in the control of glycerolipid synthesis. Prog. Lipid. Res. 23 (1984) 115-133
    • (1984) Prog. Lipid. Res. , vol.23 , pp. 115-133
    • Brindley, D.N.1
  • 18
    • 0022628210 scopus 로고
    • The activity and properties of an acidic triacylglycerol lipase from adult and fetal rat lung
    • Brooks B., and Weinhold P.A. The activity and properties of an acidic triacylglycerol lipase from adult and fetal rat lung. Biochim. Biophys. Acta 875 (1986) 39-47
    • (1986) Biochim. Biophys. Acta , vol.875 , pp. 39-47
    • Brooks, B.1    Weinhold, P.A.2
  • 19
    • 0028519115 scopus 로고
    • Isolation and characterization of a maize cDNA that complements a 1-acyl-sn-glycerol-3-phosphate acyltransferase mutant of Escherichia coli and encodes a protein which has similarities to other acyltransferases
    • Brown A.P., Coleman C., Tommey A.M., Watson M.D., and Slabas A.R. Isolation and characterization of a maize cDNA that complements a 1-acyl-sn-glycerol-3-phosphate acyltransferase mutant of Escherichia coli and encodes a protein which has similarities to other acyltransferases. Plant Mol. Biol. 26 (1994) 211-223
    • (1994) Plant Mol. Biol. , vol.26 , pp. 211-223
    • Brown, A.P.1    Coleman, C.2    Tommey, A.M.3    Watson, M.D.4    Slabas, A.R.5
  • 20
    • 0025352660 scopus 로고
    • Vasopressin signal transduction in rat type II pneumocytes
    • Brown L.A., and Chen M. Vasopressin signal transduction in rat type II pneumocytes. Am. J. Physiol. 258 (1990) L301-L307
    • (1990) Am. J. Physiol. , vol.258
    • Brown, L.A.1    Chen, M.2
  • 22
    • 0343338577 scopus 로고
    • Rapid activation of protein kinase C in isolated rat liver nuclei by prolactin, a known hepatic mitogen
    • Buckley A.R., Crowe P.D., and Russell D.H. Rapid activation of protein kinase C in isolated rat liver nuclei by prolactin, a known hepatic mitogen. Proc. Natl. Acad. Sci. USA 85 (1988) 8649-8653
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 8649-8653
    • Buckley, A.R.1    Crowe, P.D.2    Russell, D.H.3
  • 23
    • 0025779253 scopus 로고
    • Rapid activation of phosphatidate phosphohydrolase in mesangial cells by lipid A
    • Bursten S.L., and Harris W.E. Rapid activation of phosphatidate phosphohydrolase in mesangial cells by lipid A. Biochemistry 30 (1991) 6195-6203
    • (1991) Biochemistry , vol.30 , pp. 6195-6203
    • Bursten, S.L.1    Harris, W.E.2
  • 24
    • 0025746241 scopus 로고
    • Interleukin-1 rapidly stimulates lysophosphatidate acyltransferase and phosphatidate phosphohydrolase activities in human mesangial cells
    • Bursten S.L., Harris W.E., Bomsztyk K., and Lovett D. Interleukin-1 rapidly stimulates lysophosphatidate acyltransferase and phosphatidate phosphohydrolase activities in human mesangial cells. J. Biol. Chem. 266 (1991) 20732-20743
    • (1991) J. Biol. Chem. , vol.266 , pp. 20732-20743
    • Bursten, S.L.1    Harris, W.E.2    Bomsztyk, K.3    Lovett, D.4
  • 25
    • 0021687743 scopus 로고
    • Structural and chemical specificity of diradylglycerols for protein kinase C activation
    • Cabot M.C., and Jaken S. Structural and chemical specificity of diradylglycerols for protein kinase C activation. Biochem. Biophys. Res. Comm. 125 (1984) 163-169
    • (1984) Biochem. Biophys. Res. Comm. , vol.125 , pp. 163-169
    • Cabot, M.C.1    Jaken, S.2
  • 26
    • 0026688927 scopus 로고
    • Regulation of interleukin-2 responses by phosphatidic acid
    • Cano E., Munoz F.M.A., and Fresno M. Regulation of interleukin-2 responses by phosphatidic acid. Eur. J. Immunol. 22 (1992) 1883-1889
    • (1992) Eur. J. Immunol. , vol.22 , pp. 1883-1889
    • Cano, E.1    Munoz, F.M.A.2    Fresno, M.3
  • 27
    • 0023069010 scopus 로고
    • Evidence that protein kinase C is involved in regulating glucose transport in the adipocyte
    • Christensen R.L., Shade D.L., Graves C.B., and McDonald J.M. Evidence that protein kinase C is involved in regulating glucose transport in the adipocyte. Int. J. Biochem. 19 (1987) 259-265
    • (1987) Int. J. Biochem. , vol.19 , pp. 259-265
    • Christensen, R.L.1    Shade, D.L.2    Graves, C.B.3    McDonald, J.M.4
  • 28
    • 0026465955 scopus 로고
    • Changes in inositol lipid metabolism and protein kinase C translocation in nuclei of mitogen stimulated Swiss 3T3 cells
    • Cocco L., Martelli A.M., Gilmour R.S., Rana R.A., Barnabei O., and Manzoli F.A. Changes in inositol lipid metabolism and protein kinase C translocation in nuclei of mitogen stimulated Swiss 3T3 cells. Adv. Enzyme Regul. 32 (1992) 91-103
    • (1992) Adv. Enzyme Regul. , vol.32 , pp. 91-103
    • Cocco, L.1    Martelli, A.M.2    Gilmour, R.S.3    Rana, R.A.4    Barnabei, O.5    Manzoli, F.A.6
  • 29
    • 0023756946 scopus 로고
    • Hepatic sn-glycerol-3-phosphate acyltransferases: Effect of monoacylglycerol analogs on mitochondrial and microsomal activities
    • Coleman R.A. Hepatic sn-glycerol-3-phosphate acyltransferases: Effect of monoacylglycerol analogs on mitochondrial and microsomal activities. Biochim. Biophys. Acta 963 (1988) 367-374
    • (1988) Biochim. Biophys. Acta , vol.963 , pp. 367-374
    • Coleman, R.A.1
  • 30
    • 0026555853 scopus 로고
    • Diacylglycerol acyltransferase and monoacylglycerol acyltransferase from liver and intestine
    • Coleman R.A. Diacylglycerol acyltransferase and monoacylglycerol acyltransferase from liver and intestine. Meth. Enzym. 209 (1992) 98-104
    • (1992) Meth. Enzym. , vol.209 , pp. 98-104
    • Coleman, R.A.1
  • 31
    • 0020695069 scopus 로고
    • Selective changes in microsomal enzymes of triacylglycerol and phosphatidylcholine synthesis in fetal and postnatal rat liver
    • Coleman R.A., and Haynes E.B. Selective changes in microsomal enzymes of triacylglycerol and phosphatidylcholine synthesis in fetal and postnatal rat liver. J. Biol. Chem. 258 (1983) 450-456
    • (1983) J. Biol. Chem. , vol.258 , pp. 450-456
    • Coleman, R.A.1    Haynes, E.B.2
  • 32
    • 0018070657 scopus 로고
    • Selective changes in microsomal enzymes of triacylglycerol, phosphatidylcholine, and phosphatidylethanolamine biosynthesis during differentiation of 3T3-L1 preadipocytes
    • Coleman R.A., Reed B.C., Mackall J.C., Student A.K., Lane M.D., and Bell R.M. Selective changes in microsomal enzymes of triacylglycerol, phosphatidylcholine, and phosphatidylethanolamine biosynthesis during differentiation of 3T3-L1 preadipocytes. J. Biol. Chem. 253 (1978) 7256-7261
    • (1978) J. Biol. Chem. , vol.253 , pp. 7256-7261
    • Coleman, R.A.1    Reed, B.C.2    Mackall, J.C.3    Student, A.K.4    Lane, M.D.5    Bell, R.M.6
  • 33
    • 0022441839 scopus 로고
    • Stereospecificity of monoacylglycerol acyltransferase activity from rat intestine and suckling rat liver
    • Coleman R.A., Walsh J.P., Millington D.S., and Maltby D.A. Stereospecificity of monoacylglycerol acyltransferase activity from rat intestine and suckling rat liver. J. Lipid Res. 27 (1986) 158-165
    • (1986) J. Lipid Res. , vol.27 , pp. 158-165
    • Coleman, R.A.1    Walsh, J.P.2    Millington, D.S.3    Maltby, D.A.4
  • 34
    • 0026767452 scopus 로고
    • Activation of phospholipase D by protein kinase C. Evidence for a phosphorylation-independent mechanism
    • Conricode K.M., Brewer K.A., and Exton J.H. Activation of phospholipase D by protein kinase C. Evidence for a phosphorylation-independent mechanism. J. Biol. Chem. 267 (1992) 7199-7202
    • (1992) J. Biol. Chem. , vol.267 , pp. 7199-7202
    • Conricode, K.M.1    Brewer, K.A.2    Exton, J.H.3
  • 35
    • 0026734616 scopus 로고
    • Epidermal growth factor increases sn-1,2-diacylglycerol levels and activates phospholipase D-catalysed phosphatidylcholine breakdown in Swiss 3T3 cells in the absence of inositol-lipid hydrolysis
    • Cook S.J., and Wakelam M.J. Epidermal growth factor increases sn-1,2-diacylglycerol levels and activates phospholipase D-catalysed phosphatidylcholine breakdown in Swiss 3T3 cells in the absence of inositol-lipid hydrolysis. Biochem J. 285 (1992) 247-253
    • (1992) Biochem J. , vol.285 , pp. 247-253
    • Cook, S.J.1    Wakelam, M.J.2
  • 36
    • 0027070452 scopus 로고
    • Effect of tumour-promoting phorbol ester, thrombin and vasopressin on translocation of three distinct protein kinase C isoforms in human platelets and regulation by calcium
    • Crabos M., Fabbro D., Stabel S., and Erne P. Effect of tumour-promoting phorbol ester, thrombin and vasopressin on translocation of three distinct protein kinase C isoforms in human platelets and regulation by calcium. Biochem. J. 288 (1992) 891-896
    • (1992) Biochem. J. , vol.288 , pp. 891-896
    • Crabos, M.1    Fabbro, D.2    Stabel, S.3    Erne, P.4
  • 37
    • 0027393046 scopus 로고
    • Accumulation of 1,2-sn-diradylglycerol with increased membrane-associated protein kinase C may be the mechanism for spontaneous hepatocarcinogenesis in choline deficient rats
    • daCosta K.A., Cochary E.F., Blusztajn J.K., Garner S.F., and Zeisel S.H. Accumulation of 1,2-sn-diradylglycerol with increased membrane-associated protein kinase C may be the mechanism for spontaneous hepatocarcinogenesis in choline deficient rats. J. Biol. Chem. 268 (1993) 2100-2105
    • (1993) J. Biol. Chem. , vol.268 , pp. 2100-2105
    • daCosta, K.A.1    Cochary, E.F.2    Blusztajn, J.K.3    Garner, S.F.4    Zeisel, S.H.5
  • 38
    • 0028798679 scopus 로고
    • Effects of prolonged (1 year) choline deficiency and subsequent refeeding of choline on 1,2-sn-diradylglycerol, fatty acids and protein kinase C in rat liver
    • daCosta K.-A., Garmer S.C., Chang J., and Zeisel S.H. Effects of prolonged (1 year) choline deficiency and subsequent refeeding of choline on 1,2-sn-diradylglycerol, fatty acids and protein kinase C in rat liver. Carcinogenesis 16 (1995) 327-334
    • (1995) Carcinogenesis , vol.16 , pp. 327-334
    • daCosta, K.-A.1    Garmer, S.C.2    Chang, J.3    Zeisel, S.H.4
  • 40
    • 0023267841 scopus 로고
    • Parallel changes in amino acid transport and protein kinase C localization in LLL-PK1 cells treated with TPA or diradylglycerols
    • Dawson W.D., and Cook J.S. Parallel changes in amino acid transport and protein kinase C localization in LLL-PK1 cells treated with TPA or diradylglycerols. J. Cell. Physiol. 132 (1987) 104-110
    • (1987) J. Cell. Physiol. , vol.132 , pp. 104-110
    • Dawson, W.D.1    Cook, J.S.2
  • 41
    • 0026642318 scopus 로고
    • Physical evidence for the presence of two forms of phosphatidate phosphohydrolase in rat liver
    • Day C.P., and Yeaman S.J. Physical evidence for the presence of two forms of phosphatidate phosphohydrolase in rat liver. Biochim. Biophys. Acta 1127 (1992) 87-94
    • (1992) Biochim. Biophys. Acta , vol.1127 , pp. 87-94
    • Day, C.P.1    Yeaman, S.J.2
  • 42
    • 0025119208 scopus 로고
    • Evidence for a role of phosphatidylcholine-hydrolysing phospholipase C in the regulation of protein kinase C by ras and src oncogenes
    • Diaz-Laviada I., Larrodera P., Diaz-Meco M., Cornet M.E., Guddal P.H., Johansen T., and Moscat J. Evidence for a role of phosphatidylcholine-hydrolysing phospholipase C in the regulation of protein kinase C by ras and src oncogenes. Embo J. 9 (1990) 3907-3912
    • (1990) Embo J. , vol.9 , pp. 3907-3912
    • Diaz-Laviada, I.1    Larrodera, P.2    Diaz-Meco, M.3    Cornet, M.E.4    Guddal, P.H.5    Johansen, T.6    Moscat, J.7
  • 43
    • 0026040577 scopus 로고
    • The polyphosphoinositide cycle exists in the nuclei of Swiss 3T3 cells under the control of a receptor (for IGF-I) in the plasma membrane, and stimulation of the cycle increases nuclear diacylglycerol and apparently induces translocation of protein kinase C to the nucleus
    • Divecha N., Banfic H., and Irvine R.F. The polyphosphoinositide cycle exists in the nuclei of Swiss 3T3 cells under the control of a receptor (for IGF-I) in the plasma membrane, and stimulation of the cycle increases nuclear diacylglycerol and apparently induces translocation of protein kinase C to the nucleus. Embo J. 10 (1991) 3207-3214
    • (1991) Embo J. , vol.10 , pp. 3207-3214
    • Divecha, N.1    Banfic, H.2    Irvine, R.F.3
  • 44
    • 0025779217 scopus 로고
    • Incorporation of xenobiotic carboxylic acids into lipids
    • Dodds P.F. Incorporation of xenobiotic carboxylic acids into lipids. Life Sci. 49 (1991) 629-649
    • (1991) Life Sci. , vol.49 , pp. 629-649
    • Dodds, P.F.1
  • 45
    • 0025281376 scopus 로고
    • Effect of various triglycerides on plasma cholecystekinin levels in rats
    • Douglas B.R., Jansen J.B.M.J., deJong A.J.L., and Lamers C.B.H.W. Effect of various triglycerides on plasma cholecystekinin levels in rats. J. Nutr. 120 (1990) 686-690
    • (1990) J. Nutr. , vol.120 , pp. 686-690
    • Douglas, B.R.1    Jansen, J.B.M.J.2    deJong, A.J.L.3    Lamers, C.B.H.W.4
  • 47
    • 0025162155 scopus 로고
    • Signaling through phosphatidylcholine breakdown
    • Exton J.H. Signaling through phosphatidylcholine breakdown. J. Biol. Chem. 265 (1990) 1-4
    • (1990) J. Biol. Chem. , vol.265 , pp. 1-4
    • Exton, J.H.1
  • 48
    • 0026451709 scopus 로고
    • Regulation of phosphoinositide and phosphatidylcholine phospholipases by G proteins
    • Exton J.H., Taylor S.J., Blank J.S., and Bocckino S.B. Regulation of phosphoinositide and phosphatidylcholine phospholipases by G proteins. Ciba Found. Symp. 164 (1992) 36-42
    • (1992) Ciba Found. Symp. , vol.164 , pp. 36-42
    • Exton, J.H.1    Taylor, S.J.2    Blank, J.S.3    Bocckino, S.B.4
  • 49
    • 0024239820 scopus 로고
    • Phospholipid signaling systems in insulin action
    • Farese R.V. Phospholipid signaling systems in insulin action. Amer. J. Med. 85 (1988) 36-53
    • (1988) Amer. J. Med. , vol.85 , pp. 36-53
    • Farese, R.V.1
  • 51
    • 0023865191 scopus 로고
    • Identification of endogenous 1-O-alk-1′-enyl-2-acyl-sn-glycerol in myocardium and its effective utilization by choline phosphotransferase
    • Ford D.A., and Gross R.W. Identification of endogenous 1-O-alk-1′-enyl-2-acyl-sn-glycerol in myocardium and its effective utilization by choline phosphotransferase. J. Biol. Chem. 263 (1988) 2644-2650
    • (1988) J. Biol. Chem. , vol.263 , pp. 2644-2650
    • Ford, D.A.1    Gross, R.W.2
  • 52
    • 0024313358 scopus 로고
    • Activation of protein kinase C by naturally occurring ether-linked diglycerides
    • Ford D.A., Miyake R., Glaser P.E., and Gross R.W. Activation of protein kinase C by naturally occurring ether-linked diglycerides. J. Biol. Chem. 264 (1989) 13818-13824
    • (1989) J. Biol. Chem. , vol.264 , pp. 13818-13824
    • Ford, D.A.1    Miyake, R.2    Glaser, P.E.3    Gross, R.W.4
  • 53
    • 0026643973 scopus 로고
    • The primary determinant of rabbit myocardial ethanolamine phosphotransferase substrate selectivity is the covalent nature of the sn-1 aliphatic group of diradyl glycerol acceptors
    • Ford D.A., Rosenbloom K.B., and Gross R.W. The primary determinant of rabbit myocardial ethanolamine phosphotransferase substrate selectivity is the covalent nature of the sn-1 aliphatic group of diradyl glycerol acceptors. J. Biol. Chem. 267 (1992) 11222-11228
    • (1992) J. Biol. Chem. , vol.267 , pp. 11222-11228
    • Ford, D.A.1    Rosenbloom, K.B.2    Gross, R.W.3
  • 54
    • 0026700612 scopus 로고
    • Sphingolipid metabolism and signal transduction: Inhibition of in vitro phospholipase activity by sphingosine
    • Franson R.C., Harris L.K., Ghosh S.S., and Rosenthal M.D. Sphingolipid metabolism and signal transduction: Inhibition of in vitro phospholipase activity by sphingosine. Biochim. Biophys. Acta 1136 (1992) 169-174
    • (1992) Biochim. Biophys. Acta , vol.1136 , pp. 169-174
    • Franson, R.C.1    Harris, L.K.2    Ghosh, S.S.3    Rosenthal, M.D.4
  • 56
    • 0027454923 scopus 로고
    • Characterization of a triacylglycerol lipase that liberates arachidonic acid from bovine chromaffin cells during secretion
    • Galatioto L.E., and Zahler P. Characterization of a triacylglycerol lipase that liberates arachidonic acid from bovine chromaffin cells during secretion. J. Neurochem. 60 (1993) 32-39
    • (1993) J. Neurochem. , vol.60 , pp. 32-39
    • Galatioto, L.E.1    Zahler, P.2
  • 57
    • 0344114246 scopus 로고
    • Specificity and mechanism of protein kinase C activation by sn-1,2-diacylglycerols
    • Ganong B.R., Loomis C.R., Hannun Y.A., and Bell R.M. Specificity and mechanism of protein kinase C activation by sn-1,2-diacylglycerols. Proc. Natl. Acad. Sci. USA 83 (1986) 1184-1188
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 1184-1188
    • Ganong, B.R.1    Loomis, C.R.2    Hannun, Y.A.3    Bell, R.M.4
  • 58
    • 77957039256 scopus 로고
    • New pathways of phagocyte activation: The coupling of receptor-linked phospholipase D and the role of tyrosine kinase in primed neutrophils
    • Garland L.G. New pathways of phagocyte activation: The coupling of receptor-linked phospholipase D and the role of tyrosine kinase in primed neutrophils. Fems Microbiol. Immunol. 5 (1992) 229-237
    • (1992) Fems Microbiol. Immunol. , vol.5 , pp. 229-237
    • Garland, L.G.1
  • 60
    • 0023261504 scopus 로고
    • Further studies on the specificity of diacylglycerol for protein kinase C activation
    • Go M., Sekiguchi K., Nomura H., Kikkawa U., and Nishizuka Y. Further studies on the specificity of diacylglycerol for protein kinase C activation. Biochem. Biophys. Res. Comm. 144 (1987) 598-605
    • (1987) Biochem. Biophys. Res. Comm. , vol.144 , pp. 598-605
    • Go, M.1    Sekiguchi, K.2    Nomura, H.3    Kikkawa, U.4    Nishizuka, Y.5
  • 61
    • 0026572274 scopus 로고
    • Effects of okadaic acid on the activities of two distinct phosphatidate phosphohydrolases in rat hepatocytes
    • Gomez-Munoz A., Hatch G.M., Martin A., Jamal Z., Vance D.E., and Brindley D.N. Effects of okadaic acid on the activities of two distinct phosphatidate phosphohydrolases in rat hepatocytes. FEBS Lett. 301 (1992) 103-106
    • (1992) FEBS Lett. , vol.301 , pp. 103-106
    • Gomez-Munoz, A.1    Hatch, G.M.2    Martin, A.3    Jamal, Z.4    Vance, D.E.5    Brindley, D.N.6
  • 62
    • 0020356864 scopus 로고
    • Regulation of triacylglycerol synthesis in liver: Modulation of diacylglycerol acyltransferase in vitro
    • Haagsman H.P., de Haas G.M., Geelen M.J.H., and van Golde L.M.G. Regulation of triacylglycerol synthesis in liver: Modulation of diacylglycerol acyltransferase in vitro. J. Biol. Chem. 257 (1982) 10593-10598
    • (1982) J. Biol. Chem. , vol.257 , pp. 10593-10598
    • Haagsman, H.P.1    de Haas, G.M.2    Geelen, M.J.H.3    van Golde, L.M.G.4
  • 63
    • 0026077940 scopus 로고
    • The interfacial conformation and transbilayer movement of diacylglycerols in phospholipid bilayers
    • Hamilton J.A., Bhamidipati S.P., Kodali D.R., and Small D.M. The interfacial conformation and transbilayer movement of diacylglycerols in phospholipid bilayers. J. Biol. Chem. 266 (1991) 1177-1186
    • (1991) J. Biol. Chem. , vol.266 , pp. 1177-1186
    • Hamilton, J.A.1    Bhamidipati, S.P.2    Kodali, D.R.3    Small, D.M.4
  • 64
    • 0024552849 scopus 로고
    • Gastric lipolysis and fat absorption in preterm infants: Effect of medium-chain triglyceride or long-chain triglyceride-containing formulas
    • Hamosh M., Bitman J., and Liao T. Gastric lipolysis and fat absorption in preterm infants: Effect of medium-chain triglyceride or long-chain triglyceride-containing formulas. Pediatrics 83 (1989) 86-92
    • (1989) Pediatrics , vol.83 , pp. 86-92
    • Hamosh, M.1    Bitman, J.2    Liao, T.3
  • 65
    • 0022974603 scopus 로고
    • Sphingosine inhibition of protein kinase C activity and of phorbol dibutyrate binding in vitro and in human platelets
    • Hannun Y.A., Loomis C.R., Merrill A.H.J., and Bell R.M. Sphingosine inhibition of protein kinase C activity and of phorbol dibutyrate binding in vitro and in human platelets. J. Biol. Chem. 261 (1986) 12604-12609
    • (1986) J. Biol. Chem. , vol.261 , pp. 12604-12609
    • Hannun, Y.A.1    Loomis, C.R.2    Merrill, A.H.J.3    Bell, R.M.4
  • 66
    • 0026009188 scopus 로고
    • Use of sphingosine as an inhibitor of protein kinase C
    • Hannun Y.A., Merrill A.H.J., and Bell R.M. Use of sphingosine as an inhibitor of protein kinase C. Meth. Enzymol. 201 (1991) 316-328
    • (1991) Meth. Enzymol. , vol.201 , pp. 316-328
    • Hannun, Y.A.1    Merrill, A.H.J.2    Bell, R.M.3
  • 67
    • 0027994349 scopus 로고
    • The sphingomyelin cycle and the second messenger function of ceramide
    • Hannun Y.A. The sphingomyelin cycle and the second messenger function of ceramide. J. Biol. Chem. 269 (1994) 3125-3128
    • (1994) J. Biol. Chem. , vol.269 , pp. 3125-3128
    • Hannun, Y.A.1
  • 68
    • 0024374061 scopus 로고
    • Platelet-derived growth factor stimulates synthesis of 1,2-diacylglycerol from monoacylglycerol in Balb/c 3T3 cells
    • Hata Y., Ogata E., and Kojima I. Platelet-derived growth factor stimulates synthesis of 1,2-diacylglycerol from monoacylglycerol in Balb/c 3T3 cells. Biochem. J. 262 (1989) 947-952
    • (1989) Biochem. J. , vol.262 , pp. 947-952
    • Hata, Y.1    Ogata, E.2    Kojima, I.3
  • 69
    • 0023662384 scopus 로고
    • Alkyl analogs of diacylglycerol as activators of protein kinase C
    • Heymans F., Da S.C., Marrec N., Godfroid J.J., and Castagna M. Alkyl analogs of diacylglycerol as activators of protein kinase C. FEBS Lett. 218 (1987) 35-40
    • (1987) FEBS Lett. , vol.218 , pp. 35-40
    • Heymans, F.1    Da, S.C.2    Marrec, N.3    Godfroid, J.J.4    Castagna, M.5
  • 70
    • 0025829047 scopus 로고
    • Molecular insights into enzymes of membrane bilayer assembly
    • Hjelmstad R.H., and Bell R.M. Molecular insights into enzymes of membrane bilayer assembly. Biochemistry 30 (1991) 1731-1739
    • (1991) Biochemistry , vol.30 , pp. 1731-1739
    • Hjelmstad, R.H.1    Bell, R.M.2
  • 71
    • 0025806498 scopus 로고
    • sn-1,2-diacylglycerol choline- and ethanolaminephosphotransferases in Saccharomyces cerevisiae. Mixed micellar analysis of the CPT1 and EPT1 gene products
    • Hjelmstad R.H., and Bell R.M. sn-1,2-diacylglycerol choline- and ethanolaminephosphotransferases in Saccharomyces cerevisiae. Mixed micellar analysis of the CPT1 and EPT1 gene products. J. Biol. Chem. 266 (1991) 4357-4365
    • (1991) J. Biol. Chem. , vol.266 , pp. 4357-4365
    • Hjelmstad, R.H.1    Bell, R.M.2
  • 72
    • 0026067787 scopus 로고
    • Selective translocation of beta II-protein kinase C to the nucleus of human promyelocytic (HL60) leukemia cells
    • Hocevar B.A., and Fields A.P. Selective translocation of beta II-protein kinase C to the nucleus of human promyelocytic (HL60) leukemia cells. J. Biol. Chem. 266 (1991) 28-33
    • (1991) J. Biol. Chem. , vol.266 , pp. 28-33
    • Hocevar, B.A.1    Fields, A.P.2
  • 73
    • 0026648932 scopus 로고
    • Glycerophospholipid metabolism: Back to the future
    • Holmsen H., Hindenes J.O., and Fukami M. Glycerophospholipid metabolism: Back to the future. Thromb. Res. 67 (1992) 313-323
    • (1992) Thromb. Res. , vol.67 , pp. 313-323
    • Holmsen, H.1    Hindenes, J.O.2    Fukami, M.3
  • 74
    • 0026545179 scopus 로고
    • Phosphatidylethanolamine metabolism in rat liver after partial hepatectomy. Control of biosynthesis of phosphatidylethanolamine by the availability of ethanolamine
    • Houweling M., Tijburg L.B., Vaartjes W.J., and van-Golde L.M. Phosphatidylethanolamine metabolism in rat liver after partial hepatectomy. Control of biosynthesis of phosphatidylethanolamine by the availability of ethanolamine. Biochem. J. 283 (1992) 55-61
    • (1992) Biochem. J. , vol.283 , pp. 55-61
    • Houweling, M.1    Tijburg, L.B.2    Vaartjes, W.J.3    van-Golde, L.M.4
  • 75
    • 0026514657 scopus 로고
    • Protein kinase C activity in neonatal cultured rat cardiomyocytes supplemented with docosahexaenoic acid
    • Hrelia S., Biagi P.L., Turchetto E., Rossi C.A., and Bordoni A. Protein kinase C activity in neonatal cultured rat cardiomyocytes supplemented with docosahexaenoic acid. Biochem. Biophys. Res. Commun. 183 (1992) 893-898
    • (1992) Biochem. Biophys. Res. Commun. , vol.183 , pp. 893-898
    • Hrelia, S.1    Biagi, P.L.2    Turchetto, E.3    Rossi, C.A.4    Bordoni, A.5
  • 76
    • 0026787123 scopus 로고
    • Identification of phosphatidylcholine-selective and phosphatidylinositol-selective phospholipase D in Madin-Darby canine kidney cells
    • Huang C., Wykle R.L., Daniel L.W., and Cabot M.C. Identification of phosphatidylcholine-selective and phosphatidylinositol-selective phospholipase D in Madin-Darby canine kidney cells. J. Biol. Chem. 267 (1992) 16859-16865
    • (1992) J. Biol. Chem. , vol.267 , pp. 16859-16865
    • Huang, C.1    Wykle, R.L.2    Daniel, L.W.3    Cabot, M.C.4
  • 77
    • 0025999406 scopus 로고
    • Stimulation and inhibition of the activity of rat liver cytosolic phosphatidate phosphohydrolase by various phospholipids
    • Humble E., and Berglund L. Stimulation and inhibition of the activity of rat liver cytosolic phosphatidate phosphohydrolase by various phospholipids. J. Lipid Res. 32 (1991) 1869-1872
    • (1991) J. Lipid Res. , vol.32 , pp. 1869-1872
    • Humble, E.1    Berglund, L.2
  • 78
    • 0026720002 scopus 로고
    • Carbachol stimulation of triacylglycerol lipase activity in pancreatic acinar cells
    • Hundley T.R., and Rubin R.P. Carbachol stimulation of triacylglycerol lipase activity in pancreatic acinar cells. Biochem. Biophys. Res. Commun. 184 (1992) 626-633
    • (1992) Biochem. Biophys. Res. Commun. , vol.184 , pp. 626-633
    • Hundley, T.R.1    Rubin, R.P.2
  • 79
    • 0026519969 scopus 로고
    • Soybean phospholipid dependent reductions in triacylglycerol concentration and synthesis in the liver of fasted-refed rats
    • Ide T., Hirabayashi S., Kano S., and Sugano M. Soybean phospholipid dependent reductions in triacylglycerol concentration and synthesis in the liver of fasted-refed rats. Biochim. Biophys. Acta 1124 (1992) 163-170
    • (1992) Biochim. Biophys. Acta , vol.1124 , pp. 163-170
    • Ide, T.1    Hirabayashi, S.2    Kano, S.3    Sugano, M.4
  • 80
    • 0026764442 scopus 로고
    • Soybean protein-dependent changes in triacylglycerol synthesis and concentration of diacylglycerol in the liver microsomes of fasted-refed rats
    • Ide T., Murata M., and Sunada Y. Soybean protein-dependent changes in triacylglycerol synthesis and concentration of diacylglycerol in the liver microsomes of fasted-refed rats. Ann. Nutr. Metab. 36 (1992) 87-96
    • (1992) Ann. Nutr. Metab. , vol.36 , pp. 87-96
    • Ide, T.1    Murata, M.2    Sunada, Y.3
  • 81
    • 0026643557 scopus 로고
    • Phosphatidic acid and polyphosphoinositide metabolism in rod outer segments. Differential role of soluble and peripheral proteins
    • Ilincheta d.B.M.G., and Giusto N.M. Phosphatidic acid and polyphosphoinositide metabolism in rod outer segments. Differential role of soluble and peripheral proteins. Biochim. Biophys. Acta 1127 (1992) 105-115
    • (1992) Biochim. Biophys. Acta , vol.1127 , pp. 105-115
    • Ilincheta, d.B.M.G.1    Giusto, N.M.2
  • 82
    • 0025774977 scopus 로고
    • Plasma membrane fractions from rat liver contain a phosphatidate phosphohydrolase distinct from that in the endoplasmic reticulum and cytosol
    • Jamal Z., Martin A., Gomez-Munoz A., and Brindley D.N. Plasma membrane fractions from rat liver contain a phosphatidate phosphohydrolase distinct from that in the endoplasmic reticulum and cytosol. J. Biol. Chem. 266 (1991) 2988-2996
    • (1991) J. Biol. Chem. , vol.266 , pp. 2988-2996
    • Jamal, Z.1    Martin, A.2    Gomez-Munoz, A.3    Brindley, D.N.4
  • 84
    • 0024516088 scopus 로고
    • Membrane-permeable diacylglycerol, its application to platelet secretion, and regulation of platelet protein kinase C
    • Kajikawa N., Kikkawa U., Itoh K., and Nishizuka Y. Membrane-permeable diacylglycerol, its application to platelet secretion, and regulation of platelet protein kinase C. Meth. Enzymol. 169 (1989) 430-442
    • (1989) Meth. Enzymol. , vol.169 , pp. 430-442
    • Kajikawa, N.1    Kikkawa, U.2    Itoh, K.3    Nishizuka, Y.4
  • 85
    • 0025015227 scopus 로고
    • Diacylglycerol kinase: A key modulator of signal transduction?
    • Kanoh H., Yamada K., and Sakane F. Diacylglycerol kinase: A key modulator of signal transduction?. Trends Biochem. Sci. 15 (1990) 47-50
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 47-50
    • Kanoh, H.1    Yamada, K.2    Sakane, F.3
  • 86
    • 0023484050 scopus 로고
    • Phorbol ester- and light-induced endogenous phosphorylation of rat rod outer-segment proteins
    • Kapoor C.L., O'Brien P.J., and Chader G.J. Phorbol ester- and light-induced endogenous phosphorylation of rat rod outer-segment proteins. Exper. Eye Res. 45 (1987) 545-556
    • (1987) Exper. Eye Res. , vol.45 , pp. 545-556
    • Kapoor, C.L.1    O'Brien, P.J.2    Chader, G.J.3
  • 87
    • 0024583036 scopus 로고
    • Defect in phorbol acetate-induced translocation of diacylglycerol kinase in erbB-transformed fibroblast cells
    • Kato M., Kawai S., and Takenawa T. Defect in phorbol acetate-induced translocation of diacylglycerol kinase in erbB-transformed fibroblast cells. FEBS Lett. 247 (1989) 247-250
    • (1989) FEBS Lett. , vol.247 , pp. 247-250
    • Kato, M.1    Kawai, S.2    Takenawa, T.3
  • 89
    • 0019332349 scopus 로고
    • Activation of calcium and phospholipid dependent protein kinase by diacylglycerol, its possible relation to phosphatidylinositol turnover
    • Kishimoto A., Yoshimi T., Mori T., Kikkawa U., and Nishizuka Y. Activation of calcium and phospholipid dependent protein kinase by diacylglycerol, its possible relation to phosphatidylinositol turnover. J. Biol. Chem. 255 (1980) 2273-2276
    • (1980) J. Biol. Chem. , vol.255 , pp. 2273-2276
    • Kishimoto, A.1    Yoshimi, T.2    Mori, T.3    Kikkawa, U.4    Nishizuka, Y.5
  • 90
    • 0024273138 scopus 로고
    • Electron microscopic localization of type I protein kinase C in rat Purkinje cells
    • Kose A., Saito N., Ito H., Kikkawa U., Nishizuka Y., and Tanaka C. Electron microscopic localization of type I protein kinase C in rat Purkinje cells. J. Neurosci. 8 (1988) 4262-4268
    • (1988) J. Neurosci. , vol.8 , pp. 4262-4268
    • Kose, A.1    Saito, N.2    Ito, H.3    Kikkawa, U.4    Nishizuka, Y.5    Tanaka, C.6
  • 91
    • 0026016879 scopus 로고
    • Intracellular transport and metabolism of sphinomyelin
    • Koval M., and Pagano R.E. Intracellular transport and metabolism of sphinomyelin. Biochim. Biophys. Acta 1082 (1991) 113-125
    • (1991) Biochim. Biophys. Acta , vol.1082 , pp. 113-125
    • Koval, M.1    Pagano, R.E.2
  • 92
    • 0023513561 scopus 로고
    • Novel source of 1,2-diacylglycerol elevated in cells transformed by Ha-ras oncogene
    • Lacal J.C., Moscat J., and Aaronson S.A. Novel source of 1,2-diacylglycerol elevated in cells transformed by Ha-ras oncogene. Nature 330 (1987) 269-272
    • (1987) Nature , vol.330 , pp. 269-272
    • Lacal, J.C.1    Moscat, J.2    Aaronson, S.A.3
  • 93
    • 0025852233 scopus 로고
    • Dissociation of protein kinase C activation and sn-1,2-diacylglycerol formation. Comparison of phosphatidylinositol- and phosphatidylcholine-derived diglycerides in alpha-thrombin-stimulated fibroblasts
    • Leach K.L., Ruff V.A., Wright T.M., Pessin M.S., and Raben D.M. Dissociation of protein kinase C activation and sn-1,2-diacylglycerol formation. Comparison of phosphatidylinositol- and phosphatidylcholine-derived diglycerides in alpha-thrombin-stimulated fibroblasts. J. Biol. Chem. 266 (1991) 3215-3221
    • (1991) J. Biol. Chem. , vol.266 , pp. 3215-3221
    • Leach, K.L.1    Ruff, V.A.2    Wright, T.M.3    Pessin, M.S.4    Raben, D.M.5
  • 94
    • 0026098922 scopus 로고
    • Molecular species of diacylglycerols and phosphoglycerides and the postmortem changes in the molecular species of diacylglycerols in rat brains
    • Lee C.H., and Hajra A.K. Molecular species of diacylglycerols and phosphoglycerides and the postmortem changes in the molecular species of diacylglycerols in rat brains. J. Neurochem. 56 (1991) 370-379
    • (1991) J. Neurochem. , vol.56 , pp. 370-379
    • Lee, C.H.1    Hajra, A.K.2
  • 95
    • 0023875593 scopus 로고
    • Formation of 1-alkyl-2-acetyl-sn-glycerols via the de novo biosynthetic pathway for platelet-activating factor. Characterization of 1-alkyl-2-acetyl-sn-glycero-3-phosphate phosphohydrolase in rat spleens
    • Lee T.C., Malone B., and Snyder F. Formation of 1-alkyl-2-acetyl-sn-glycerols via the de novo biosynthetic pathway for platelet-activating factor. Characterization of 1-alkyl-2-acetyl-sn-glycero-3-phosphate phosphohydrolase in rat spleens. J. Biol. Chem. 263 (1988) 1755-1760
    • (1988) J. Biol. Chem. , vol.263 , pp. 1755-1760
    • Lee, T.C.1    Malone, B.2    Snyder, F.3
  • 96
    • 0025896824 scopus 로고
    • The protein kinase C content is increased in the nuclear fraction of rat adrenal zona glomerulosa following long-term ACTH administration
    • Lehoux J.G., Grondin F., Pacuraru J.P., and Yachaoui Y. The protein kinase C content is increased in the nuclear fraction of rat adrenal zona glomerulosa following long-term ACTH administration. Mol. Cell. Endocrinol. 78 (1991) 97-106
    • (1991) Mol. Cell. Endocrinol. , vol.78 , pp. 97-106
    • Lehoux, J.G.1    Grondin, F.2    Pacuraru, J.P.3    Yachaoui, Y.4
  • 97
    • 0025138343 scopus 로고
    • Distribution of distinct arachidonoyl-specific and non-specific isoenzymes of diacylglycerol kinase in baboon (Papio cynocephalus) tissues
    • Lemaitre R.N., King W.C., MacDonald M.L., and Glomset J.A. Distribution of distinct arachidonoyl-specific and non-specific isoenzymes of diacylglycerol kinase in baboon (Papio cynocephalus) tissues. Biochem. J. 266 (1990) 291-299
    • (1990) Biochem. J. , vol.266 , pp. 291-299
    • Lemaitre, R.N.1    King, W.C.2    MacDonald, M.L.3    Glomset, J.A.4
  • 98
    • 0023874013 scopus 로고
    • A membrane-bound diacylglycerol kinase that selectively phosphorylates arachidonoyl-diacylglycerol. Distinction from cytosolic diacylglycerol kinase and comparison with the membrane-bound enzyme from Escherichia coli
    • MacDonald M.L., Mack K.F., Williams B.W., King W.C., and Glomset J.A. A membrane-bound diacylglycerol kinase that selectively phosphorylates arachidonoyl-diacylglycerol. Distinction from cytosolic diacylglycerol kinase and comparison with the membrane-bound enzyme from Escherichia coli. J. Biol. Chem. 263 (1988) 1584-1592
    • (1988) J. Biol. Chem. , vol.263 , pp. 1584-1592
    • MacDonald, M.L.1    Mack, K.F.2    Williams, B.W.3    King, W.C.4    Glomset, J.A.5
  • 100
    • 0021760351 scopus 로고
    • The phosphorylcholine acceptor in the phosphatidylcholine: Ceramide cholinephosphotransferase reaction. Is the enzyme a transferase or a hydrolase?
    • Marggraf W.-D., and Kanfer J.N. The phosphorylcholine acceptor in the phosphatidylcholine: Ceramide cholinephosphotransferase reaction. Is the enzyme a transferase or a hydrolase?. Biochim. Biophys. Acta 793 (1984) 346-353
    • (1984) Biochim. Biophys. Acta , vol.793 , pp. 346-353
    • Marggraf, W.-D.1    Kanfer, J.N.2
  • 101
    • 0026693238 scopus 로고
    • Nuclear localization and signalling activity of phosphoinositidase C beta in Swiss 3T3 cells
    • Martelli A.M., Gilmour R.S., Bertagnolo V., Neri L.M., Manzoli L., and Cocco L. Nuclear localization and signalling activity of phosphoinositidase C beta in Swiss 3T3 cells. Nature 358 (1992) 242-245
    • (1992) Nature , vol.358 , pp. 242-245
    • Martelli, A.M.1    Gilmour, R.S.2    Bertagnolo, V.3    Neri, L.M.4    Manzoli, L.5    Cocco, L.6
  • 102
    • 0022861220 scopus 로고
    • Selective incorporation of various C-22 polyunsaturated fatty acids in Ehrlich ascites tumor cells
    • Masuzawa Y., Okano S., Waku K., Sprecher H., and Lands W.E. Selective incorporation of various C-22 polyunsaturated fatty acids in Ehrlich ascites tumor cells. J. Lipid Res. 27 (1986) 1145-1153
    • (1986) J. Lipid Res. , vol.27 , pp. 1145-1153
    • Masuzawa, Y.1    Okano, S.2    Waku, K.3    Sprecher, H.4    Lands, W.E.5
  • 103
    • 0027530629 scopus 로고
    • Stimulation of nuclear protein kinase C leads to phosphorylation of nuclear inositol 1,4,5-trisphosphate receptor and accelerated calcium release by inositol 1,4,5-trisphosphate from isolated rat liver nuclei
    • Matter N., Ritz M.F., Freyermuth S., Rogue P., and Malviya A.N. Stimulation of nuclear protein kinase C leads to phosphorylation of nuclear inositol 1,4,5-trisphosphate receptor and accelerated calcium release by inositol 1,4,5-trisphosphate from isolated rat liver nuclei. J. Biol. Chem. 268 (1993) 732-736
    • (1993) J. Biol. Chem. , vol.268 , pp. 732-736
    • Matter, N.1    Ritz, M.F.2    Freyermuth, S.3    Rogue, P.4    Malviya, A.N.5
  • 104
    • 0021853150 scopus 로고
    • Inhibition of diacylglycerol acyltransferase by 2-bromooctanoate in cultured rat hepatocytes
    • Mayorek N., and Bar-Tana J. Inhibition of diacylglycerol acyltransferase by 2-bromooctanoate in cultured rat hepatocytes. J. Biol. Chem. 260 (1985) 6528-6532
    • (1985) J. Biol. Chem. , vol.260 , pp. 6528-6532
    • Mayorek, N.1    Bar-Tana, J.2
  • 105
    • 0024351939 scopus 로고
    • Triacylglycerol synthesis in cultured rat hepatocytes. The rate-limiting role of diacylglycerol acyltransferase
    • Mayorek N., Grinstein I., and Bar-Tana J. Triacylglycerol synthesis in cultured rat hepatocytes. The rate-limiting role of diacylglycerol acyltransferase. Eur. J. Biochem. 182 (1989) 395-400
    • (1989) Eur. J. Biochem. , vol.182 , pp. 395-400
    • Mayorek, N.1    Grinstein, I.2    Bar-Tana, J.3
  • 106
    • 0022761915 scopus 로고
    • Cyclic AMP increases incorporation of exogenous fatty acids into triacylglycerols in hamster fibroblasts
    • Maziere C., Maziere J.C., Mora L., Auclair M., and Polonovski J. Cyclic AMP increases incorporation of exogenous fatty acids into triacylglycerols in hamster fibroblasts. Lipids 21 8 (1986) 525-528
    • (1986) Lipids , vol.21 , Issue.8 , pp. 525-528
    • Maziere, C.1    Maziere, J.C.2    Mora, L.3    Auclair, M.4    Polonovski, J.5
  • 107
    • 0026015925 scopus 로고
    • The Ptd-Ins-PLC superfamily and signal transduction
    • Meldrum E., Parker P.J., and Carozzi A. The Ptd-Ins-PLC superfamily and signal transduction. Biochim. Biophys. Acta 1092 (1991) 49-71
    • (1991) Biochim. Biophys. Acta , vol.1092 , pp. 49-71
    • Meldrum, E.1    Parker, P.J.2    Carozzi, A.3
  • 108
    • 0023001006 scopus 로고
    • The tumor promoter 12-O-tetradecanoyl phorbol 13-acetate and regulatory diacylglycerols are substrates for the same carboxylesterase
    • Mentlein R. The tumor promoter 12-O-tetradecanoyl phorbol 13-acetate and regulatory diacylglycerols are substrates for the same carboxylesterase. J. Biol. Chem. 261 (1986) 7816-7818
    • (1986) J. Biol. Chem. , vol.261 , pp. 7816-7818
    • Mentlein, R.1
  • 109
    • 0023277671 scopus 로고
    • Genetic identification of rat liver carboxylesterases isolated in different laboratories
    • Mentlein R., Ronai A., Robbi M., Heymann E., and von Deimling O. Genetic identification of rat liver carboxylesterases isolated in different laboratories. Biochim. Biophys. Acta 913 (1987) 27-38
    • (1987) Biochim. Biophys. Acta , vol.913 , pp. 27-38
    • Mentlein, R.1    Ronai, A.2    Robbi, M.3    Heymann, E.4    von Deimling, O.5
  • 110
    • 0026675439 scopus 로고
    • Ceramide: A new lipid "second messenger"?
    • Merrill A.H. Ceramide: A new lipid "second messenger"?. Nutr. Rev. 50 (1992) 78-80
    • (1992) Nutr. Rev. , vol.50 , pp. 78-80
    • Merrill, A.H.1
  • 111
    • 0025283928 scopus 로고
    • An update of the enzymology and regulation of sphingomyelin metabolism
    • Merrill A.H., and Jones D.D. An update of the enzymology and regulation of sphingomyelin metabolism. Biochim. Biophys. Acta 1044 (1990) 1-12
    • (1990) Biochim. Biophys. Acta , vol.1044 , pp. 1-12
    • Merrill, A.H.1    Jones, D.D.2
  • 112
    • 0024496181 scopus 로고
    • Modulation of protein kinase C and diverse cell functions by sphingosine- a pharmacologically interesting compound linking sphingolipids and signal transduction
    • Merrill A.H., and Stevens V.L. Modulation of protein kinase C and diverse cell functions by sphingosine- a pharmacologically interesting compound linking sphingolipids and signal transduction. Biochim. Biophys. Acta 1010 (1989) 131-139
    • (1989) Biochim. Biophys. Acta , vol.1010 , pp. 131-139
    • Merrill, A.H.1    Stevens, V.L.2
  • 113
    • 0026060118 scopus 로고
    • Phospholipase D in the pancreatic islet: Evidence suggesting the involvement of phosphatidic acid in signal transduction
    • Metz S., and Dunlop M. Phospholipase D in the pancreatic islet: Evidence suggesting the involvement of phosphatidic acid in signal transduction. Adv. Prostaglandin Thromboxane Leukotriene Res. 21A (1991) 287-290
    • (1991) Adv. Prostaglandin Thromboxane Leukotriene Res. , vol.21 A , pp. 287-290
    • Metz, S.1    Dunlop, M.2
  • 114
    • 0023672096 scopus 로고
    • Perspectives in diabetes. Is protein kinase C required for physiologic insulin release?
    • Metz S.A. Perspectives in diabetes. Is protein kinase C required for physiologic insulin release?. Diabetes 37 1 (1988) 3-7
    • (1988) Diabetes , vol.37 , Issue.1 , pp. 3-7
    • Metz, S.A.1
  • 115
    • 0027023825 scopus 로고
    • Protein kinase C isoforms in human glioblastoma cells
    • Misra-Press A., Fields A.P., Samols D., and Goldthwait D.A. Protein kinase C isoforms in human glioblastoma cells. Glia 6 (1992) 188-197
    • (1992) Glia , vol.6 , pp. 188-197
    • Misra-Press, A.1    Fields, A.P.2    Samols, D.3    Goldthwait, D.A.4
  • 116
    • 0023687477 scopus 로고
    • Structural studies on the diglyceride-mediated activation of protein kinase C
    • Molleyres L.P., and Rando R.R. Structural studies on the diglyceride-mediated activation of protein kinase C. J. Biol. Chem. 263 (1988) 14832-14838
    • (1988) J. Biol. Chem. , vol.263 , pp. 14832-14838
    • Molleyres, L.P.1    Rando, R.R.2
  • 117
    • 0025877224 scopus 로고
    • Cell-free transfer of membrane lipids. Evidence for lipid processing
    • Moreau P., and Morre D.J. Cell-free transfer of membrane lipids. Evidence for lipid processing. J. Biol. Chem. 266 (1991) 4329-4333
    • (1991) J. Biol. Chem. , vol.266 , pp. 4329-4333
    • Moreau, P.1    Morre, D.J.2
  • 118
    • 0026326485 scopus 로고
    • Fecal excretion, uptake and metabolism by colon mucosa of diacylglycerol in rats
    • Morotomi M., and Weinstein I.B. Fecal excretion, uptake and metabolism by colon mucosa of diacylglycerol in rats. Biochem. Biophys. Res. Commun. 181 (1991) 1028-1034
    • (1991) Biochem. Biophys. Res. Commun. , vol.181 , pp. 1028-1034
    • Morotomi, M.1    Weinstein, I.B.2
  • 119
    • 0025173924 scopus 로고
    • Phosphoinositide metabolism in cultured glioma and neuroblastoma cells: Subcellular distribution of enzymes indicate incomplete turnover at the plasma membrane
    • Morris S.J., Cook H.W., Byers D.M., Spence M.W., and Palmer F.B. Phosphoinositide metabolism in cultured glioma and neuroblastoma cells: Subcellular distribution of enzymes indicate incomplete turnover at the plasma membrane. Biochim. Biophys. Acta 1022 (1990) 339-347
    • (1990) Biochim. Biophys. Acta , vol.1022 , pp. 339-347
    • Morris, S.J.1    Cook, H.W.2    Byers, D.M.3    Spence, M.W.4    Palmer, F.B.5
  • 120
    • 0027162121 scopus 로고
    • Increased hepatic monoacylglycerol acyltransferase activity in streptozotocin-induce diabetes: Characterization and comparison with activities from adult and neonatal rat liver
    • in press
    • in press. Mostafa N., Bhat B.G., and Coleman R.A. Increased hepatic monoacylglycerol acyltransferase activity in streptozotocin-induce diabetes: Characterization and comparison with activities from adult and neonatal rat liver. Biochim. Biophys. Acta (1993)
    • (1993) Biochim. Biophys. Acta
    • Mostafa, N.1    Bhat, B.G.2    Coleman, R.A.3
  • 121
    • 0024829871 scopus 로고
    • 2(+)-dependent phosphorylation of the cAMP-binding protein and a phospholipid-activated mitochondrial phospholipase
    • 2(+)-dependent phosphorylation of the cAMP-binding protein and a phospholipid-activated mitochondrial phospholipase. Biochemistry 28 (1989) 9974-9981
    • (1989) Biochemistry , vol.28 , pp. 9974-9981
    • Muller, G.1    Bandlow, W.2
  • 122
    • 0025866050 scopus 로고
    • Sphingosine inhibits phosphatidate phosphohydrolase in human neutrophils by a protein kinase C-independent mechanism
    • Mullmann T.J., Siegel M.I., Egan R.W., and Billah M.M. Sphingosine inhibits phosphatidate phosphohydrolase in human neutrophils by a protein kinase C-independent mechanism. J. Biol. Chem. 266 (1991) 2013-2016
    • (1991) J. Biol. Chem. , vol.266 , pp. 2013-2016
    • Mullmann, T.J.1    Siegel, M.I.2    Egan, R.W.3    Billah, M.M.4
  • 123
    • 0026658539 scopus 로고
    • Purification and characterization of the zeta isoform of protein kinase C from bovine kidney
    • Nakanishi H., and Exton J.H. Purification and characterization of the zeta isoform of protein kinase C from bovine kidney. J. Biol. Chem. 267 (1992) 16347-16354
    • (1992) J. Biol. Chem. , vol.267 , pp. 16347-16354
    • Nakanishi, H.1    Exton, J.H.2
  • 124
    • 0026451081 scopus 로고
    • Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C
    • Nishizuka Y. Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C. Science 258 (1992) 607-614
    • (1992) Science , vol.258 , pp. 607-614
    • Nishizuka, Y.1
  • 126
    • 0024020409 scopus 로고
    • What is the fate of diacylglycerol produced at the Golgi apparatus?
    • Pagano R.E. What is the fate of diacylglycerol produced at the Golgi apparatus?. Trends Biochem. Sci. 13 (1988) 202-205
    • (1988) Trends Biochem. Sci. , vol.13 , pp. 202-205
    • Pagano, R.E.1
  • 127
    • 0021918091 scopus 로고
    • Phosphorylation, transbilayer movement and facilitated intracellular transport of diacylglycerols are involved in the uptake of a fluorescent analog of phosphatidic acid by culture fibroblasts
    • Pagano R.E., and Longmuir K.J. Phosphorylation, transbilayer movement and facilitated intracellular transport of diacylglycerols are involved in the uptake of a fluorescent analog of phosphatidic acid by culture fibroblasts. J. Biol. Chem. 260 (1985) 1909-1916
    • (1985) J. Biol. Chem. , vol.260 , pp. 1909-1916
    • Pagano, R.E.1    Longmuir, K.J.2
  • 128
    • 0021099118 scopus 로고
    • Intracellular translocation and metabolism of a fluorescent phosphatidic acid analogue in cultured fibroblasts
    • Pagano R.E., Longmuir K.J., and Martin O.C. Intracellular translocation and metabolism of a fluorescent phosphatidic acid analogue in cultured fibroblasts. J. Biol. Chem. 258 (1983) 2034-2040
    • (1983) J. Biol. Chem. , vol.258 , pp. 2034-2040
    • Pagano, R.E.1    Longmuir, K.J.2    Martin, O.C.3
  • 129
    • 0026011097 scopus 로고
    • Overexpression of protein kinase C beta 1 enhances phospholipase D activity and diacylglycerol formation in phorbol ester-stimulated rat fibroblasts
    • Pai J.K., Pachter J.A., Weinstein I.B., and Bishop W.R. Overexpression of protein kinase C beta 1 enhances phospholipase D activity and diacylglycerol formation in phorbol ester-stimulated rat fibroblasts. Proc. Natl. Acad. Sci. USA 88 (1991) 598-602
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 598-602
    • Pai, J.K.1    Pachter, J.A.2    Weinstein, I.B.3    Bishop, W.R.4
  • 130
    • 0016157763 scopus 로고
    • Liver ultrastructure in abetalipoproteinemia: Evaluation of micronodular cirrhosis
    • Partin J.S., Partin J.C., Schubert W.K., and McAdams A.J. Liver ultrastructure in abetalipoproteinemia: Evaluation of micronodular cirrhosis. Gastroenterology 67 (1974) 107-118
    • (1974) Gastroenterology , vol.67 , pp. 107-118
    • Partin, J.S.1    Partin, J.C.2    Schubert, W.K.3    McAdams, A.J.4
  • 131
    • 0026730882 scopus 로고
    • A differential location of phosphoinositide kinases, diacylglycerol kinase, and phospholipase C in the nuclear matrix
    • Payrastre B., Nievers M., Boonstra J., Breton M., Verkleij A.J., and Van B.e.H.P.M. A differential location of phosphoinositide kinases, diacylglycerol kinase, and phospholipase C in the nuclear matrix. J. Biol. Chem. 267 (1992) 5078-5084
    • (1992) J. Biol. Chem. , vol.267 , pp. 5078-5084
    • Payrastre, B.1    Nievers, M.2    Boonstra, J.3    Breton, M.4    Verkleij, A.J.5    Van, B.e.H.P.M.6
  • 133
    • 0022970190 scopus 로고
    • Quantitative measurement of sn-1,2-diacylglycerols present in platelets, hepatocytes, and ras- and sis-transformed normal rat kidney cells
    • Preiss J., Loomis C.R., Bishop W.R., Stein R., Niedel J.E., and Bell R.M. Quantitative measurement of sn-1,2-diacylglycerols present in platelets, hepatocytes, and ras- and sis-transformed normal rat kidney cells. J. Biol. Chem. 261 (1986) 8597-8600
    • (1986) J. Biol. Chem. , vol.261 , pp. 8597-8600
    • Preiss, J.1    Loomis, C.R.2    Bishop, W.R.3    Stein, R.4    Niedel, J.E.5    Bell, R.M.6
  • 134
    • 0024458707 scopus 로고
    • Stimulation of phosphatidylcholine hydrolysis, diacylglycerol release, and arachidonic acid production by oncogenic ras is a consequence of protein kinase C activation
    • Price B.D., Morris J.D., Marshall C.J., and Hall A. Stimulation of phosphatidylcholine hydrolysis, diacylglycerol release, and arachidonic acid production by oncogenic ras is a consequence of protein kinase C activation. J. Biol. Chem. 264 (1989) 16638-16643
    • (1989) J. Biol. Chem. , vol.264 , pp. 16638-16643
    • Price, B.D.1    Morris, J.D.2    Marshall, C.J.3    Hall, A.4
  • 135
    • 0026787944 scopus 로고
    • Stimulation of phosphatidate synthesis in endothelial cells in response to P2-receptor activation. Evidence for phospholipase C and phospholipase D involvement, phosphatidate and diacylglycerol interconversion and the role of protein kinase C
    • Purkiss J.R., and Boarder M.R. Stimulation of phosphatidate synthesis in endothelial cells in response to P2-receptor activation. Evidence for phospholipase C and phospholipase D involvement, phosphatidate and diacylglycerol interconversion and the role of protein kinase C. Biochem J. 287 (1992) 31-36
    • (1992) Biochem J. , vol.287 , pp. 31-36
    • Purkiss, J.R.1    Boarder, M.R.2
  • 136
    • 0025228692 scopus 로고
    • A novel mechanism for acetylcholine to generate diacylglycerol in brain
    • Qian Z., and Drewes L.R. A novel mechanism for acetylcholine to generate diacylglycerol in brain. J. Biol. Chem. 265 (1990) 3607-3610
    • (1990) J. Biol. Chem. , vol.265 , pp. 3607-3610
    • Qian, Z.1    Drewes, L.R.2
  • 137
    • 0023913608 scopus 로고
    • Regulation of protein kinase C activity by lipids
    • Rando R.R. Regulation of protein kinase C activity by lipids. FASEB J. 2 (1988) 2348-2355
    • (1988) FASEB J. , vol.2 , pp. 2348-2355
    • Rando, R.R.1
  • 138
    • 0026513625 scopus 로고
    • Structural basis of protein kinase C activation by diacylglycerols and tumor promoters
    • Rando R.R., and Kishi Y. Structural basis of protein kinase C activation by diacylglycerols and tumor promoters. Biochemistry 31 (1992) 2211-2218
    • (1992) Biochemistry , vol.31 , pp. 2211-2218
    • Rando, R.R.1    Kishi, Y.2
  • 139
    • 0023905177 scopus 로고
    • Phorbol diesters and dioctanoylglycerol stimulate accumulation of both diacylglycerols and alkylacylglycerols in human neutrophils
    • Rider L.G., Dougherty R.W., and Niedel J.E. Phorbol diesters and dioctanoylglycerol stimulate accumulation of both diacylglycerols and alkylacylglycerols in human neutrophils. J. Immunol. 140 (1988) 200-207
    • (1988) J. Immunol. , vol.140 , pp. 200-207
    • Rider, L.G.1    Dougherty, R.W.2    Niedel, J.E.3
  • 140
    • 0026712941 scopus 로고
    • Reversible ATP-dependent inactivation of adipose diacylglycerol acyltransferase
    • Rodriguez M.A., Dias C., and Lau T.E. Reversible ATP-dependent inactivation of adipose diacylglycerol acyltransferase. Lipids 27 (1992) 577-581
    • (1992) Lipids , vol.27 , pp. 577-581
    • Rodriguez, M.A.1    Dias, C.2    Lau, T.E.3
  • 141
    • 0023658504 scopus 로고
    • Further evidence for the existence of different diacylglycerol pools of the phosphatidylcholine synthesis in microsomes
    • Rustow B., and Kunze D. Further evidence for the existence of different diacylglycerol pools of the phosphatidylcholine synthesis in microsomes. Biochim. Biophys. Acta 921 (1987) 552-558
    • (1987) Biochim. Biophys. Acta , vol.921 , pp. 552-558
    • Rustow, B.1    Kunze, D.2
  • 142
    • 0025873916 scopus 로고
    • Porcine 80-kDa diacylglycerol kinase is a calcium-binding and calcium/phospholipid-dependent enzyme and undergoes calcium-dependent translocation
    • Sakane F., Yamada K., Imai S., and Kanoh H. Porcine 80-kDa diacylglycerol kinase is a calcium-binding and calcium/phospholipid-dependent enzyme and undergoes calcium-dependent translocation. J. Biol. Chem. 266 (1991) 7096-7100
    • (1991) J. Biol. Chem. , vol.266 , pp. 7096-7100
    • Sakane, F.1    Yamada, K.2    Imai, S.3    Kanoh, H.4
  • 143
    • 0027537612 scopus 로고
    • Potentiation of diacylglycerol-induced activation of protein kinase C by lysophospholipids: Subspecies difference
    • Sasaki Y., Asoaka Y., and Nishizuka Y. Potentiation of diacylglycerol-induced activation of protein kinase C by lysophospholipids: Subspecies difference. Febs Lett. 320 (1993) 47-51
    • (1993) Febs Lett. , vol.320 , pp. 47-51
    • Sasaki, Y.1    Asoaka, Y.2    Nishizuka, Y.3
  • 145
    • 0025294841 scopus 로고
    • Properties of phosphatidate phosphohydrolase and diacylglycerol acyltransferase activities in the isolated rat heart. Effect of glucagon, ischemia and diabetes
    • Schoonderwoerd K., Broekhoven-Schokker S., Hulsmann W.C., and Stam H. Properties of phosphatidate phosphohydrolase and diacylglycerol acyltransferase activities in the isolated rat heart. Effect of glucagon, ischemia and diabetes. Biochem. J. 268 (1990) 487-492
    • (1990) Biochem. J. , vol.268 , pp. 487-492
    • Schoonderwoerd, K.1    Broekhoven-Schokker, S.2    Hulsmann, W.C.3    Stam, H.4
  • 146
    • 0023786091 scopus 로고
    • Activation of protein kinase C by cis- and trans-fatty acids and its potentiation by diacylglycerol
    • Seifert R., Schachtele C., Rosenthal W., and Schultz G. Activation of protein kinase C by cis- and trans-fatty acids and its potentiation by diacylglycerol. Biochem. Biophys. Res. Comm. 154 (1988) 20-26
    • (1988) Biochem. Biophys. Res. Comm. , vol.154 , pp. 20-26
    • Seifert, R.1    Schachtele, C.2    Rosenthal, W.3    Schultz, G.4
  • 147
    • 0026579804 scopus 로고
    • Diacylglycerol-stimulated formation of actin nucleation sites at plasma membranes
    • Shariff A., and Luna E.J. Diacylglycerol-stimulated formation of actin nucleation sites at plasma membranes. Science 256 (1992) 245-247
    • (1992) Science , vol.256 , pp. 245-247
    • Shariff, A.1    Luna, E.J.2
  • 148
    • 0026023348 scopus 로고
    • Protein kinase C subspecies in adult rat hippocampal synaptosomes. Activation by diacylglycerol and arachidonic acid
    • Shearman M.S., Shinomura T., Oda T., and Nishizuka Y. Protein kinase C subspecies in adult rat hippocampal synaptosomes. Activation by diacylglycerol and arachidonic acid. FEBS Lett. 279 (1991) 261-264
    • (1991) FEBS Lett. , vol.279 , pp. 261-264
    • Shearman, M.S.1    Shinomura, T.2    Oda, T.3    Nishizuka, Y.4
  • 149
    • 0026352592 scopus 로고
    • Transcriptional regulation of p90 with sequence homology to E. Coli glycerol-3-phosphate acyltransferase
    • Shin D.H., Paulauskis J.D., Moustaid N., and Sul H.S. Transcriptional regulation of p90 with sequence homology to E. Coli glycerol-3-phosphate acyltransferase. J. Biol. Chem. 266 (1991) 23834-23839
    • (1991) J. Biol. Chem. , vol.266 , pp. 23834-23839
    • Shin, D.H.1    Paulauskis, J.D.2    Moustaid, N.3    Sul, H.S.4
  • 150
    • 0026050726 scopus 로고
    • Synergistic action of diacylglycerol and unsaturated fatty acid for protein kinase C activation: Its possible implications
    • Shinomura T., Asaoka Y., Oka M., Yoshida K., and Nishizuka Y. Synergistic action of diacylglycerol and unsaturated fatty acid for protein kinase C activation: Its possible implications. Proc. Natl. Acad. Sci. USA 88 (1991) 5149-5153
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 5149-5153
    • Shinomura, T.1    Asaoka, Y.2    Oka, M.3    Yoshida, K.4    Nishizuka, Y.5
  • 151
    • 0026446851 scopus 로고
    • Oleate stimulation of diacylglycerol formation from phosphatidylcholine through effects on phospholipase D and phosphatidate phosphohydrolase
    • Siddiqui R.A., and Exton J.H. Oleate stimulation of diacylglycerol formation from phosphatidylcholine through effects on phospholipase D and phosphatidate phosphohydrolase. Eur. J. Biochem. 210 (1992) 601-607
    • (1992) Eur. J. Biochem. , vol.210 , pp. 601-607
    • Siddiqui, R.A.1    Exton, J.H.2
  • 152
    • 0024582146 scopus 로고
    • Physiological levels of diacylglycerols in phospholipid membranes induce membrane fusion and stabilize inverted phases
    • Siegel D.P., Banschbach J., Alford D., Ellens H., Lis L.J., Quinn P.J., Yeagle P.L., and Bentz J. Physiological levels of diacylglycerols in phospholipid membranes induce membrane fusion and stabilize inverted phases. Biochemistry 28 (1989) 3703-3709
    • (1989) Biochemistry , vol.28 , pp. 3703-3709
    • Siegel, D.P.1    Banschbach, J.2    Alford, D.3    Ellens, H.4    Lis, L.J.5    Quinn, P.J.6    Yeagle, P.L.7    Bentz, J.8
  • 153
    • 0026091210 scopus 로고
    • Swiss 3T3 cells preferentially incorporate sn-2-arachidonoyl monoacylglycerol into sn-1-stearoyl-2-arachidonoyl phosphatidylinositol
    • Simpson C.M., Itabe H., Reynolds C.N., King W.C., and Glomset J.A. Swiss 3T3 cells preferentially incorporate sn-2-arachidonoyl monoacylglycerol into sn-1-stearoyl-2-arachidonoyl phosphatidylinositol. J. Biol. Chem. 266 (1991) 15902-15909
    • (1991) J. Biol. Chem. , vol.266 , pp. 15902-15909
    • Simpson, C.M.1    Itabe, H.2    Reynolds, C.N.3    King, W.C.4    Glomset, J.A.5
  • 154
    • 0024356723 scopus 로고
    • Free sphingosine formation from endogenous substrates by a liver plasma membrane system with a divalent cation dependence and a neutral pH optimum
    • Slife C.W., Wang E., Hunter R., Wang S., Burgess C., Liotta D.C., and Merrill Jr. A.H. Free sphingosine formation from endogenous substrates by a liver plasma membrane system with a divalent cation dependence and a neutral pH optimum. J. Biol. Chem. 264 (1989) 10371-10377
    • (1989) J. Biol. Chem. , vol.264 , pp. 10371-10377
    • Slife, C.W.1    Wang, E.2    Hunter, R.3    Wang, S.4    Burgess, C.5    Liotta, D.C.6    Merrill Jr., A.H.7
  • 155
    • 0024839795 scopus 로고
    • Mechanisms of short-term (second range) regulation of the activities of enzymes of lipid and phospholipid metabolism in secretory cells
    • Soling H.D., Fest W., Machoczek K., Schmidt T., Esselmann H., and Fischer M. Mechanisms of short-term (second range) regulation of the activities of enzymes of lipid and phospholipid metabolism in secretory cells. Adv. Enzyme Regul. 28 (1989) 35-50
    • (1989) Adv. Enzyme Regul. , vol.28 , pp. 35-50
    • Soling, H.D.1    Fest, W.2    Machoczek, K.3    Schmidt, T.4    Esselmann, H.5    Fischer, M.6
  • 156
    • 0024390999 scopus 로고
    • Signal transmission in exocrine cells is associated with rapid activity changes of acyltransferases and diacylglycerol kinase due to reversible protein phosphorylation
    • Soling H.D., Fest W., Schmidt T., Esselmann H., and Bachmann V. Signal transmission in exocrine cells is associated with rapid activity changes of acyltransferases and diacylglycerol kinase due to reversible protein phosphorylation. J. Biol. Chem. 264 (1989) 10643-10648
    • (1989) J. Biol. Chem. , vol.264 , pp. 10643-10648
    • Soling, H.D.1    Fest, W.2    Schmidt, T.3    Esselmann, H.4    Bachmann, V.5
  • 158
    • 0026561011 scopus 로고
    • Factors influencing triacylglycerol synthesis in permeabilized rat hepatocytes
    • Stals H.K., Mannaerts G.P., and Declercq P.E. Factors influencing triacylglycerol synthesis in permeabilized rat hepatocytes. Biochem. J. 283 (1992) 719-725
    • (1992) Biochem. J. , vol.283 , pp. 719-725
    • Stals, H.K.1    Mannaerts, G.P.2    Declercq, P.E.3
  • 159
    • 0022637252 scopus 로고
    • Characterization of mono-, di- and triacylglycerol lipase activities in the isolated rat heart
    • Stam H., Broekhoven-Schokker S., and Hulsmann W.C. Characterization of mono-, di- and triacylglycerol lipase activities in the isolated rat heart. Biochim. Biophys. Acta 875 (1986) 76-86
    • (1986) Biochim. Biophys. Acta , vol.875 , pp. 76-86
    • Stam, H.1    Broekhoven-Schokker, S.2    Hulsmann, W.C.3
  • 160
    • 0025694802 scopus 로고
    • Identification of two cytosolic diacylglycerol kinase isoforms in rat brain, and in NIH-3T3 and ras-transformed fibroblasts
    • Stathopoulos V.M., Coco M.A., Wei C.W., Goth M., Zaricznyj C., and Macara I.G. Identification of two cytosolic diacylglycerol kinase isoforms in rat brain, and in NIH-3T3 and ras-transformed fibroblasts. Biochem. J. 272 (1990) 569-575
    • (1990) Biochem. J. , vol.272 , pp. 569-575
    • Stathopoulos, V.M.1    Coco, M.A.2    Wei, C.W.3    Goth, M.4    Zaricznyj, C.5    Macara, I.G.6
  • 161
    • 0026030499 scopus 로고
    • Calcium-calmodulin and calcium-phospholipid dependent phosphorylation of membranous fraction proteins related to the tropic regulation by estradiol in the corpus luteum
    • Steinschneider A., Rao M.C., Khan I., McLean M.P., and Gibori G. Calcium-calmodulin and calcium-phospholipid dependent phosphorylation of membranous fraction proteins related to the tropic regulation by estradiol in the corpus luteum. Endocrinology 128 (1991) 263-272
    • (1991) Endocrinology , vol.128 , pp. 263-272
    • Steinschneider, A.1    Rao, M.C.2    Khan, I.3    McLean, M.P.4    Gibori, G.5
  • 162
    • 0026497385 scopus 로고
    • Regulation of phospholipase C by G proteins
    • Sternweis P.C., and Smrcka A.V. Regulation of phospholipase C by G proteins. Trends Biochem. Sci. 17 (1992) 502-506
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 502-506
    • Sternweis, P.C.1    Smrcka, A.V.2
  • 163
    • 0026086943 scopus 로고
    • Fatty acid and molecular species compositions of phospholipids and diacylglycerols from rat retinal membranes
    • Stinson A.M., Wiegand R.D., and Anderson R.E. Fatty acid and molecular species compositions of phospholipids and diacylglycerols from rat retinal membranes. Exper. Eye Res. 52 (1991) 213-218
    • (1991) Exper. Eye Res. , vol.52 , pp. 213-218
    • Stinson, A.M.1    Wiegand, R.D.2    Anderson, R.E.3
  • 164
    • 0025094053 scopus 로고
    • Medium-chain fatty acids: Evidence for incorporation into chylomicron triglycerides in humans
    • Swift L.L., Hill J.O., Peters J.C., and Greene H.L. Medium-chain fatty acids: Evidence for incorporation into chylomicron triglycerides in humans. Am. J. Clin. Nutr. 52 (1990) 834-836
    • (1990) Am. J. Clin. Nutr. , vol.52 , pp. 834-836
    • Swift, L.L.1    Hill, J.O.2    Peters, J.C.3    Greene, H.L.4
  • 165
    • 0024987362 scopus 로고
    • Effects of medium-chain triglycerides on brush border membrane-bound enzyme activity in rat small intestine
    • Takase S., and Goda T. Effects of medium-chain triglycerides on brush border membrane-bound enzyme activity in rat small intestine. J. Nutr. 120 (1990) 969-976
    • (1990) J. Nutr. , vol.120 , pp. 969-976
    • Takase, S.1    Goda, T.2
  • 166
    • 0024994161 scopus 로고
    • The temporal relationship between phospholipase activation, diradylglycerol formation and superoxide production in the human neutrophil
    • Thompson N.T., Tateson J.E., Randall R.W., Spacey G.D., Bonser R.W., and Garland L.G. The temporal relationship between phospholipase activation, diradylglycerol formation and superoxide production in the human neutrophil. Biochem. J. 271 (1990) 209-213
    • (1990) Biochem. J. , vol.271 , pp. 209-213
    • Thompson, N.T.1    Tateson, J.E.2    Randall, R.W.3    Spacey, G.D.4    Bonser, R.W.5    Garland, L.G.6
  • 167
    • 0025820155 scopus 로고
    • Biosynthesis and secretion of triacylglycerol in rat liver after partial hepatectomy
    • Tijburg L.B., Nyathi C.B., Meijer G.W., and Geelen M.J. Biosynthesis and secretion of triacylglycerol in rat liver after partial hepatectomy. Biochem. J. 277 (1991) 723-728
    • (1991) Biochem. J. , vol.277 , pp. 723-728
    • Tijburg, L.B.1    Nyathi, C.B.2    Meijer, G.W.3    Geelen, M.J.4
  • 168
    • 0024996687 scopus 로고
    • Regulation of platelet protein kinase C by oleic acid. Kinetic analysis of allosteric regulation and effects on autophosphorylation, phorbol ester binding, and susceptibility to inhibition
    • Touny S., Khan W., and Hannun Y. Regulation of platelet protein kinase C by oleic acid. Kinetic analysis of allosteric regulation and effects on autophosphorylation, phorbol ester binding, and susceptibility to inhibition. J. Biol. Chem. 265 27 (1990) 16437-16943
    • (1990) J. Biol. Chem. , vol.265 , Issue.27 , pp. 16437-16943
    • Touny, S.1    Khan, W.2    Hannun, Y.3
  • 169
    • 0024344148 scopus 로고
    • On the biological occurrence and regulation of 1-acyl and 1-O-alkyl-diradylglycerols in human neutrophils. Selective destruction of diacyl species using Rhizopus lipase
    • Tyagi S.R., Burnham D.N., and Lambeth J.D. On the biological occurrence and regulation of 1-acyl and 1-O-alkyl-diradylglycerols in human neutrophils. Selective destruction of diacyl species using Rhizopus lipase. J. Biol. Chem. 264 22 (1989) 12977-12982
    • (1989) J. Biol. Chem. , vol.264 , Issue.22 , pp. 12977-12982
    • Tyagi, S.R.1    Burnham, D.N.2    Lambeth, J.D.3
  • 170
    • 0026346995 scopus 로고
    • Diacylglycerol Signals the Translocation of CTP: Choline-phosphate Cytidylyltransferase in HeLa Cells treated with 12-0-Tetradecanoylphorbol-13-acetate*
    • Utal A.K., Jamil H., and Vance D.E. Diacylglycerol Signals the Translocation of CTP: Choline-phosphate Cytidylyltransferase in HeLa Cells treated with 12-0-Tetradecanoylphorbol-13-acetate*. J. Biol. Chem. 266 (1991) 24084-24091
    • (1991) J. Biol. Chem. , vol.266 , pp. 24084-24091
    • Utal, A.K.1    Jamil, H.2    Vance, D.E.3
  • 171
    • 0024296459 scopus 로고
    • Effect of harvesting methods, growth conditions and growth phase on diacylglycerol levels in cultured human adherent cells
    • Van Veldhoven P.P., and Bell R.M. Effect of harvesting methods, growth conditions and growth phase on diacylglycerol levels in cultured human adherent cells. Biochim. Biophys. Acta 959 2 (1988) 185-196
    • (1988) Biochim. Biophys. Acta , vol.959 , Issue.2 , pp. 185-196
    • Van Veldhoven, P.P.1    Bell, R.M.2
  • 172
    • 0025134479 scopus 로고
    • Boehringer Mannheim Award lecture. Phosphatidylcholine metabolism: Masochistic enzymology, metabolic regulation, and lipoprotein assembly
    • Vance D.E. Boehringer Mannheim Award lecture. Phosphatidylcholine metabolism: Masochistic enzymology, metabolic regulation, and lipoprotein assembly. Biochem. Cell. Biol. 68 10 (1990) 1151-1165
    • (1990) Biochem. Cell. Biol. , vol.68 , Issue.10 , pp. 1151-1165
    • Vance, D.E.1
  • 173
    • 0023903699 scopus 로고
    • Does rat liver Golgi have the capacity to synthesize phospholipids for lipoprotein secretion?
    • Vance J.E., and Vance D.E. Does rat liver Golgi have the capacity to synthesize phospholipids for lipoprotein secretion?. J. Biol. Chem. 263 12 (1988) 5898-5909
    • (1988) J. Biol. Chem. , vol.263 , Issue.12 , pp. 5898-5909
    • Vance, J.E.1    Vance, D.E.2
  • 174
    • 0025746264 scopus 로고
    • Organelle biogenesis and intracellular lipid transport in eukaryotes
    • Voelker D.R. Organelle biogenesis and intracellular lipid transport in eukaryotes. Microbiol. Rev. 55 4 (1991) 543-560
    • (1991) Microbiol. Rev. , vol.55 , Issue.4 , pp. 543-560
    • Voelker, D.R.1
  • 175
    • 0022924167 scopus 로고
    • 2+-dependent phosphatidate phosphohydrolase between cytosol and endoplasmic reticulum in a permanent cell line from human lung
    • 2+-dependent phosphatidate phosphohydrolase between cytosol and endoplasmic reticulum in a permanent cell line from human lung. Biochem. Cell Biol. 64 11 (1986) 1135-1140
    • (1986) Biochem. Cell Biol. , vol.64 , Issue.11 , pp. 1135-1140
    • Walton, P.A.1    Possmayer, F.2
  • 176
    • 0028816963 scopus 로고
    • Identification of the nuclear localization signal of rat liver CTP: Phosphocholine cytidyltransferase
    • Wang Y., MacDonald J.I., and Kent C. Identification of the nuclear localization signal of rat liver CTP: Phosphocholine cytidyltransferase. J. Biol. Chem. 270 (1995) 354-360
    • (1995) J. Biol. Chem. , vol.270 , pp. 354-360
    • Wang, Y.1    MacDonald, J.I.2    Kent, C.3
  • 177
    • 0027415175 scopus 로고
    • Nuclear localization of soluble CTP: Phosphocholine cytidyltransferase
    • Wang Y., Sweitzer T.D., Weinhold P.A., and Kent C. Nuclear localization of soluble CTP: Phosphocholine cytidyltransferase. J. Biol. Chem. 268 (1993) 5899-5904
    • (1993) J. Biol. Chem. , vol.268 , pp. 5899-5904
    • Wang, Y.1    Sweitzer, T.D.2    Weinhold, P.A.3    Kent, C.4
  • 178
    • 0026627736 scopus 로고
    • The lipolysis/esterification cycle of hepatic triacylglycerol. Its role in the secretion of very-low-density lipoprotein and its response to hormones and sulphoylureas
    • Wiggins D., and Gibbons G.F. The lipolysis/esterification cycle of hepatic triacylglycerol. Its role in the secretion of very-low-density lipoprotein and its response to hormones and sulphoylureas. Biochem. J. 284 (1992) 457-462
    • (1992) Biochem. J. , vol.284 , pp. 457-462
    • Wiggins, D.1    Gibbons, G.F.2
  • 179
    • 0024383917 scopus 로고
    • Elevation of 1,2-diacylglycerol in ras-transformed neonatal liver and pancreas of transgenic mice
    • Wilkison W.O., Sandgren E.P., Palmiter R.D., Brinster R.L., and Bell R.M. Elevation of 1,2-diacylglycerol in ras-transformed neonatal liver and pancreas of transgenic mice. Oncogene 4 (1989) 625-628
    • (1989) Oncogene , vol.4 , pp. 625-628
    • Wilkison, W.O.1    Sandgren, E.P.2    Palmiter, R.D.3    Brinster, R.L.4    Bell, R.M.5
  • 180
    • 0023646010 scopus 로고
    • Down-regulation of protein kinase C and of an endogenous 80-kDa substrate in transformed fibroblasts
    • Wolfman A., Wingrove T.G., Blackshear P.J., and Macara I.G. Down-regulation of protein kinase C and of an endogenous 80-kDa substrate in transformed fibroblasts. J. Biol. Chem. 262 34 (1987) 16546-16552
    • (1987) J. Biol. Chem. , vol.262 , Issue.34 , pp. 16546-16552
    • Wolfman, A.1    Wingrove, T.G.2    Blackshear, P.J.3    Macara, I.G.4
  • 181
    • 0022884849 scopus 로고
    • Immunocytochemical localization of protein kinase C in identified neuronal compartments of rat brain
    • Wood J.G., Girard P.R., Mazzei G.J., and Kuo J.F. Immunocytochemical localization of protein kinase C in identified neuronal compartments of rat brain. J. Neurosci. 6 9 (1986) 2571-2577
    • (1986) J. Neurosci. , vol.6 , Issue.9 , pp. 2571-2577
    • Wood, J.G.1    Girard, P.R.2    Mazzei, G.J.3    Kuo, J.F.4
  • 182
    • 0023927798 scopus 로고
    • Kinetic analysis of 1,2-diacylglycerol mass levels in cultured fibroblasts. Comparison of stimulation by alpha-thrombin and epidermal growth factor
    • Wright T.M., Rangan L.A., Shin H.S., and Raben D.M. Kinetic analysis of 1,2-diacylglycerol mass levels in cultured fibroblasts. Comparison of stimulation by alpha-thrombin and epidermal growth factor. J. Biol. Chem. 263 19 (1988) 9374-9380
    • (1988) J. Biol. Chem. , vol.263 , Issue.19 , pp. 9374-9380
    • Wright, T.M.1    Rangan, L.A.2    Shin, H.S.3    Raben, D.M.4
  • 183
    • 0026766698 scopus 로고
    • Diacylglycerol metabolism in neonatal rat liver: Characterization of cytosolic diacylglycerol lipase activity and its activation by monoalkylglycerols
    • Xia T., and Coleman R.A. Diacylglycerol metabolism in neonatal rat liver: Characterization of cytosolic diacylglycerol lipase activity and its activation by monoalkylglycerols. Biochim. Biophys. Acta 1126 3 (1992) 327-336
    • (1992) Biochim. Biophys. Acta , vol.1126 , Issue.3 , pp. 327-336
    • Xia, T.1    Coleman, R.A.2
  • 184
    • 0345254527 scopus 로고
    • Ontogeny of hepatic 1,2-sn-diacylglycerol content and protein kinase C activity in the neonatal rat: Lack of concordance
    • in press
    • in press. Xia T., Garner S.A., Zeisel S.H., and Coleman R.A. Ontogeny of hepatic 1,2-sn-diacylglycerol content and protein kinase C activity in the neonatal rat: Lack of concordance. J. Nutr. Biochem. (1993)
    • (1993) J. Nutr. Biochem.
    • Xia, T.1    Garner, S.A.2    Zeisel, S.H.3    Coleman, R.A.4
  • 185
    • 0025104648 scopus 로고
    • Purification and characterization of cytosolic diacylglycerol kinases of human platelets
    • Yada Y., Ozeki T., Kanoh H., and Nozawa Y. Purification and characterization of cytosolic diacylglycerol kinases of human platelets. J. Biol. Chem. 265 31 (1990) 19237-19243
    • (1990) J. Biol. Chem. , vol.265 , Issue.31 , pp. 19237-19243
    • Yada, Y.1    Ozeki, T.2    Kanoh, H.3    Nozawa, Y.4
  • 186
    • 0026654652 scopus 로고
    • Platelet activiation by simultaneous actions of diacylglycerol and unsaturated fatty acids
    • 14
    • Yoshida K., Asaoka Y., and Nishizuka Y. Platelet activiation by simultaneous actions of diacylglycerol and unsaturated fatty acids. Proc. Natl. Acad. Sci. USA 89 (1992) 6443-6446 14
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 6443-6446
    • Yoshida, K.1    Asaoka, Y.2    Nishizuka, Y.3
  • 187
    • 0026565677 scopus 로고
    • Ceramide is a competitive inhibitor of diacylglycerol kinase in vitro and in intact human leukemia (HL-60) cells
    • Younes A., Kahn D.W., Besterman J.M., Bittman R., Byun H.S., and Kolesnick R.N. Ceramide is a competitive inhibitor of diacylglycerol kinase in vitro and in intact human leukemia (HL-60) cells. J. Biol. Chem. 267 2 (1992) 842-847
    • (1992) J. Biol. Chem. , vol.267 , Issue.2 , pp. 842-847
    • Younes, A.1    Kahn, D.W.2    Besterman, J.M.3    Bittman, R.4    Byun, H.S.5    Kolesnick, R.N.6
  • 188
    • 0024994545 scopus 로고
    • 1,2-diacylglycerol content and its arachidonyl-containing molecular species are reduced in sciatic nerve from streptozotocin-induced diabetic rats
    • Zhu X., and Eichberg J. 1,2-diacylglycerol content and its arachidonyl-containing molecular species are reduced in sciatic nerve from streptozotocin-induced diabetic rats. J. Neurochem. 55 3 (1990) 1087-1090
    • (1990) J. Neurochem. , vol.55 , Issue.3 , pp. 1087-1090
    • Zhu, X.1    Eichberg, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.