메뉴 건너뛰기




Volumn 32, Issue 2, 2008, Pages 117-127

Enzymological characteristics of plasma membrane phosphatidate phosphohydrolase (PAP2) from rat liver

Author keywords

Phosphatidate phosphohydrolase; Phosphatidic acid

Indexed keywords


EID: 70350325648     PISSN: 10286276     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (7)

References (29)
  • 1
    • 0030610803 scopus 로고    scopus 로고
    • Mammalian Mg2+ independent phosphatidate phosphatase (PAP2) displays diacylglycerol pyrophosphatase activity
    • Dillon, A. D., Chen, X., Zeimetz, G. M., Wu, W. I., Waggoner, D. W., Dewald, J., Brindley, D. N. & Carman, G. M. (1997). Mammalian Mg2+ independent phosphatidate phosphatase (PAP2) displays diacylglycerol pyrophosphatase activity. J. Biol. Chem., 272, 10361-10366.
    • (1997) J. Biol. Chem. , vol.272 , pp. 10361-10366
    • Dillon, A.D.1    Chen, X.2    Zeimetz, G.M.3    Wu, W.I.4    Waggoner, D.W.5    Dewald, J.6    Brindley, D.N.7    Carman, G.M.8
  • 2
    • 0029744530 scopus 로고    scopus 로고
    • Identification and cDNA cloning of 35kDa phosphatidic acid phosphatase (type 2) bound to plasma membranes
    • Kai, M.,Wada, I., Imai, S. I., Sankane, F. & Kanoh, H. (1996). Identification and cDNA cloning of 35kDa phosphatidic acid phosphatase (type 2) bound to plasma membranes. J. Biol. Chem., 271, 18931-18938.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18931-18938
    • Kai, M.1
  • 3
    • 0029024743 scopus 로고
    • Purification and characterization of N_ ethylmaleimide-sensitive and insensitive phosphatidic acid phosphohydrolase (PAP2) from rat liver
    • Fleming, I. N. & Yeaman, J. (1995). Purification and characterization of N_ ethylmaleimide-sensitive and insensitive phosphatidic acid phosphohydrolase (PAP2) from rat liver. Biochem. J., 308, 983-989.
    • (1995) Biochem. J. , vol.308 , pp. 983-989
    • Fleming, I.N.1    Yeaman, J.2
  • 4
    • 0029127249 scopus 로고
    • Purification and characterization of a novel plasma membrane phosphatidate phosphohydrolase from rat liver
    • Waggoner, D. W., Martin, A., Dewald, J., Munoz, A. G. & Brindley, D. N. (1995). Purification and characterization of a novel plasma membrane phosphatidate phosphohydrolase from rat liver. J. Biol. Chem., 270, 19422-19429.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19422-19429
    • Waggoner, D.W.1    Martin, A.2    Dewald, J.3    Munoz, A.G.4    Brindley, D.N.5
  • 5
    • 52849122495 scopus 로고    scopus 로고
    • The relationship between cation-induced substrate configuration and enzymatic activity of phosphatidate phosphohydrolase from human liver
    • Haghighi, B., Yari, M. & Tori, S. (2000). The relationship between cation-induced substrate configuration and enzymatic activity of phosphatidate phosphohydrolase from human liver. Iranian Biomed. J., 4, 13-19.
    • (2000) Iranian Biomed. J. , vol.4 , pp. 13-19
    • Haghighi, B.1    Yari, M.2    Tori, S.3
  • 6
    • 20144365964 scopus 로고
    • The effects of hydrazine on the phosphatidate phosphohydrolase activity in rat liver
    • Haghighi, B. & Honarjou, S. (1987). The effects of hydrazine on the phosphatidate phosphohydrolase activity in rat liver. Biochem. Pharmaco., 3, 113-115.
    • (1987) Biochem. Pharmaco. , vol.3 , pp. 113-115
    • Haghighi, B.1    Honarjou, S.2
  • 7
    • 0026483490 scopus 로고
    • Purification and properties of phosphatidic acid phosphatase from porcine thymus membrane
    • Kanoh, H., Imai, S. I., Yamada, K. & Sakane, F. (1992). Purification and properties of phosphatidic acid phosphatase from porcine thymus membrane. J. Biol. Chem., 267, 25309-25314.
    • (1992) J. Biol. Chem. , vol.267 , pp. 25309-25314
    • Kanoh, H.1    Imai, S.I.2    Yamada, K.3    Sakane, F.4
  • 8
    • 0029130345 scopus 로고
    • Lipid signaling enzymes and surface dilution kinetics
    • Carman, G. M., Deems, R. A. & Dennis, E. A. (1995). Lipid signaling enzymes and surface dilution kinetics. J. Biol. Chem., 270, 18711-18714.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18711-18714
    • Carman, G.M.1    Deems, R.A.2    Dennis, E.A.3
  • 9
    • 0025134135 scopus 로고
    • Structure of the inverted hexagonal (HII) phase, and nonlamellar phase transition of lipids
    • Seddon, J. M. (1990). Structure of the inverted hexagonal (HII) phase, and nonlamellar phase transition of lipids. Biochim. Biophys. Acta, 1031, 1-69.
    • (1990) Biochim. Biophys. Acta , vol.1031 , pp. 1-69
    • Seddon, J.M.1
  • 10
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem., 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 11
    • 0001809974 scopus 로고
    • Gel electrophoresis of erythrocyte membrane proteins
    • (ed. J. C. Ellory and J. D. Young), London: Academic Press
    • Thompson, S. & Maddy, A. H. (1982). Gel electrophoresis of erythrocyte membrane proteins. In red cell membranes. A methodological approach (ed. J. C. Ellory and J. D. Young), London: Academic Press.
    • (1982) Red cell membranes. A methodological approach
    • Thompson, S.1    Maddy, A.H.2
  • 12
    • 0021043301 scopus 로고
    • Rapid protein phosphorylation induced by phorbol ester in HL- 60 cells
    • Feuerstein, N. & Cooper, L. (1983). Rapid protein phosphorylation induced by phorbol ester in HL- 60 cells. J. Biol. Chem., 258, 10786-10793.
    • (1983) J. Biol. Chem. , vol.258 , pp. 10786-10793
    • Feuerstein, N.1    Cooper, L.2
  • 13
    • 0021988172 scopus 로고
    • Simplified method for silver staining of proteins in polyacrylamide gels and the mechanism of the silver staining
    • Heukeshoven, J. & Dernick, R. (1985). Simplified method for silver staining of proteins in polyacrylamide gels and the mechanism of the silver staining. Electrophoresis, 6(3), 103-112.
    • (1985) Electrophoresis , vol.6 , Issue.3 , pp. 103-112
    • Heukeshoven, J.1    Dernick, R.2
  • 14
    • 0030012094 scopus 로고    scopus 로고
    • Identification of phosphatidate phosphohydrolase purified from rat liver membrane on SDS-polyacrylamide gel electrophoresis
    • Siess, E. A. & Hofstetter, M. (1996). Identification of phosphatidate phosphohydrolase purified from rat liver membrane on SDS-polyacrylamide gel electrophoresis. FEBS Lett., 381, 169-173.
    • (1996) FEBS Lett. , vol.381 , pp. 169-173
    • Siess, E.A.1    Hofstetter, M.2
  • 15
    • 0021105815 scopus 로고
    • Polymorphic phase preference of phosphatidic: A 31P and 2H NMR study
    • Farren, S. B., Hope, M. J. & Cullis, P. R. (1983). Polymorphic phase preference of phosphatidic: A 31P and 2H NMR study. Biochem. Biophys. Res. Commun., 111, 675-682.
    • (1983) Biochem. Biophys. Res. Commun. , vol.111 , pp. 675-682
    • Farren, S.B.1    Hope, M.J.2    Cullis, P.R.3
  • 16
    • 0021304591 scopus 로고
    • Solubilization of functional membrane proteins
    • Hjelmeland, L. M. & Chambach, A. (1984). Solubilization of functional membrane proteins. Methods Enzymol., 104, 305-318.
    • (1984) Methods Enzymol. , vol.104 , pp. 305-318
    • Hjelmeland, L.M.1    Chambach, A.2
  • 17
    • 0017194357 scopus 로고
    • Studies on membrane fusion. II) Induction of fusion in pure phospholipid membranes by calcium ions and other divalent metals
    • Papahadjopoulos, D., Vail, W. J., Pangborn, W. A. & Poste, G. (1976). Studies on membrane fusion. II) Induction of fusion in pure phospholipid membranes by calcium ions and other divalent metals. Biochim. Biophys. Acta, 448, 265-283.
    • (1976) Biochim. Biophys. Acta , vol.448 , pp. 265-283
    • Papahadjopoulos, D.1    Vail, W.J.2    Pangborn, W.A.3    Poste, G.4
  • 18
    • 0016743560 scopus 로고
    • Kinetic analysis of phospholipase A2 activity toward mixed and its implication for the study of lipolytic enzyme
    • Deems, R. A., Eaton, B. R. & Dennis, E. A. (1975). Kinetic analysis of phospholipase A2 activity toward mixed and its implication for the study of lipolytic enzyme. J. Biol. Chem., 250, 9013-9020.
    • (1975) J. Biol. Chem. , vol.250 , pp. 9013-9020
    • Deems, R.A.1    Eaton, B.R.2    Dennis, E.A.3
  • 19
    • 0030586215 scopus 로고    scopus 로고
    • Modulation of the activities of enzymes of membrane lipid metabolism by non-bilayer-forming lipids
    • Cornell, R. B. & Arnold, R. S. (1996). Modulation of the activities of enzymes of membrane lipid metabolism by non-bilayer-forming lipids. Chem. Phys. Lipids, 81, 215-227.
    • (1996) Chem. Phys. Lipids , vol.81 , pp. 215-227
    • Cornell, R.B.1    Arnold, R.S.2
  • 20
    • 0031552937 scopus 로고    scopus 로고
    • Phosphatidatic acid phosphatase from mammalian tissues: Discovery of channel-like proteins with unexpected functions
    • Kanoh, H., Kai, M. & Wada, I. (1997). Phosphatidatic acid phosphatase from mammalian tissues: discovery of channel-like proteins with unexpected functions. Biochim. Biophys. Acta, 1384, 56-62.
    • (1997) Biochim. Biophys. Acta , vol.1384 , pp. 56-62
    • Kanoh, H.1    Kai, M.2    Wada, I.3
  • 21
    • 70350271921 scopus 로고
    • Phosphatidate metabolism and its relation to triacylglycerol biosythesis
    • Brindley, D. N. & Sturton, R. G. (1982). Phosphatidate metabolism and its relation to triacylglycerol biosythesis. New Compr. Biochem., 4, 179-213.
    • (1982) New Compr. Biochem. , vol.4 , pp. 179-213
    • Brindley, D.N.1    Sturton, R.G.2
  • 22
    • 0018846846 scopus 로고
    • Enzymes of glycerolipid synthesis in eukaryotes
    • Bell, R. M. & Coleman, R. A. (1980). Enzymes of glycerolipid synthesis in eukaryotes. Annu. Rev. Biochem., 49, 459-487.
    • (1980) Annu. Rev. Biochem. , vol.49 , pp. 459-487
    • Bell, R.M.1    Coleman, R.A.2
  • 23
    • 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., Munoz, A. G. & Brindley, D. N. (1991). Plasma membrane fractions from rat liver contain a phosphatidate phosphohydrolase distinct from that in the endoplasmic reticulum and cytosol. J. Biol. Chem., 266, 2988-2996.
    • (1991) J. Biol. Chem. , vol.266 , pp. 2988-2996
    • Jamal, Z.1    Martin, A.2    Munoz, A.G.3    Brindley, D.N.4
  • 24
    • 0020724194 scopus 로고
    • Calorimetric studies of gel- fluid (Lβ -Lα) and lamellar-inverted hexagonal (Lα-HII) phase transitions in dialkyl and diacylphosphatidylethanolamine
    • Seddon, J. M., Ceve, G. & Marxh, D. (1983). Calorimetric studies of gel -fluid (Lβ -Lα) and lamellar-inverted hexagonal (Lα-HII) phase transitions in dialkyl and diacylphosphatidylethanolamine. Biochemistry, 22, 1280-1289.
    • (1983) Biochemistry , vol.22 , pp. 1280-1289
    • Seddon, J.M.1    Ceve, G.2    Marxh, D.3
  • 25
    • 0023646686 scopus 로고
    • Kinetics and mechanism of transitions involving the lamellar cubic, inverted hexagonal and fluid isotropic phases of hydrated monoacylglycerides monitored by time-resolved X-ray diffraction
    • Caffrey, M. (1987). Kinetics and mechanism of transitions involving the lamellar cubic, inverted hexagonal and fluid isotropic phases of hydrated monoacylglycerides monitored by time-resolved X-ray diffraction. Biochemistry, 26, 6349-6363.
    • (1987) Biochemistry , vol.26 , pp. 6349-6363
    • Caffrey, M.1
  • 26
    • 73849156710 scopus 로고
    • Effect of ethylene glycol on the conformation of γ- globulin and β-lactoglobin
    • Tanford, C., Buckley, C. E., De, P. K. & Lively, E. P. (1962). Effect of ethylene glycol on the conformation of γ- globulin and β-lactoglobin. J. Biol. Chem., 237, 1168-1171.
    • (1962) J. Biol. Chem. , vol.237 , pp. 1168-1171
    • Tanford, C.1    Buckley, C.E.2    De, P.K.3    Lively, E.P.4
  • 27
    • 0018789680 scopus 로고
    • Increased thermal stability of protein in the presence of sugars
    • Joan, F. B., David, O. & Malcom, B. S. (1979). Increased thermal stability of protein in the presence of sugars. Biochemistry, 18, 5191-5196.
    • (1979) Biochemistry , vol.18 , pp. 5191-5196
    • Joan, F.B.1    David, O.2    Malcom, B.S.3
  • 28
    • 0024460832 scopus 로고
    • Direct transition of dioleoylphosphatidylethanolamine from lamellar gel to inverted hexagonal phase caused by trehalose
    • Aurell, W. C., Rand, R. P., Growe, L. M., Spargo, B. J. & Crowe, J. H. (1989). Direct transition of dioleoylphosphatidylethanolamine from lamellar gel to inverted hexagonal phase caused by trehalose. Biochim. Biophys. Acta, 984, 238-242.
    • (1989) Biochim. Biophys. Acta , vol.984 , pp. 238-242
    • Aurell, W.C.1    Rand, R.P.2    Growe, L.M.3    Spargo, B.J.4    Crowe, J.H.5
  • 29
    • 0032441482 scopus 로고    scopus 로고
    • Stabilization against thermal inactivation promoted by sugar on enzyme structure and function: Why is trehalose more effective than other sugars?
    • Mauro, S. P. & Roberto, M. F. (1998). Stabilization against thermal inactivation promoted by sugar on enzyme structure and function: Why is trehalose more effective than other sugars? Arch. Biochim. Biophys., 360, 10-14.
    • (1998) Arch. Biochim. Biophys. , vol.360 , pp. 10-14
    • Mauro, S.P.1    Roberto, M.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.