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Volumn 41, Issue 1, 2000, Pages 48-57

The open lid mediates pancreatic lipase function

Author keywords

Bile salts; Colipase; Pancreatic lipase related protein; Site directed mutagenesis

Indexed keywords

BILE SALT; COLIPASE; PHOSPHOLIPASE; TRIACYLGLYCEROL LIPASE; TRIACYLGLYCEROL LIPASE RELATED PROTEIN 2; UNCLASSIFIED DRUG;

EID: 0033971766     PISSN: 00222275     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (42)

References (30)
  • 1
    • 0026572737 scopus 로고
    • Structure and evolution of the lipase superfamily
    • Hide, W. A., L. Cham and W-H. Li. 1992. Structure and evolution of the lipase superfamily. J. Lipid Res. 33: 167-178.
    • (1992) J. Lipid Res. , vol.33 , pp. 167-178
    • Hide, W.A.1    Cham, L.2    Li, W.-H.3
  • 2
    • 0002175277 scopus 로고
    • Pancreatic lipase
    • B. Borgstrom, and H. L. Brockman, editors. Elsevier, Amsterdam.
    • Verger, R. 1984. Pancreatic lipase. In Lipases. B. Borgstrom, and H. L. Brockman, editors. Elsevier, Amsterdam. 84-150.
    • (1984) Lipases , pp. 84-150
    • Verger, R.1
  • 3
    • 0026671201 scopus 로고
    • Two novel human pancreatic lipase related proteins, hPLRP1 and hPLRP2: Differences in colipase dependency and in lipase activity
    • Giller, T., P. Buchwald, D. Blum-Kaelin, and W. Hunziker. 1992. Two novel human pancreatic lipase related proteins, hPLRP1 and hPLRP2: differences in colipase dependency and in lipase activity. J. Biol. Chem. 267: 16509-16516.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16509-16516
    • Giller, T.1    Buchwald, P.2    Blum-Kaelin, D.3    Hunziker, W.4
  • 5
    • 0028806511 scopus 로고
    • Rat GP-3 is a pancreatic lipase with kinetic properties that differ from colipase-dependent pancreatic lipase
    • Jennens, M. L., and M. E. Lowe. 1995. Rat GP-3 is a pancreatic lipase with kinetic properties that differ from colipase-dependent pancreatic lipase. J. Lipid Res. 36: 2374-2381.
    • (1995) J. Lipid Res. , vol.36 , pp. 2374-2381
    • Jennens, M.L.1    Lowe, M.E.2
  • 6
    • 0028279834 scopus 로고
    • Evidence for a pancreatic lipase subfamily with new kinetic properties
    • Thirstrup, K., R. Verger, and F. Carriere. 1994. Evidence for a pancreatic lipase subfamily with new kinetic properties. Biochemistry. 33: 2748-2756.
    • (1994) Biochemistry , vol.33 , pp. 2748-2756
    • Thirstrup, K.1    Verger, R.2    Carriere, F.3
  • 7
    • 0000392201 scopus 로고    scopus 로고
    • Pancreatic lipase-related protein 2 but not classical pancreatic lipase hydrolyzes galactolipids
    • Andersson, L., F. Carriere, M. E. Lowe, A. Nilsson, and R. Verger. 1996. Pancreatic lipase-related protein 2 but not classical pancreatic lipase hydrolyzes galactolipids. Biochim. Biophys. Acta. 1302: 236-240.
    • (1996) Biochim. Biophys. Acta. , vol.1302 , pp. 236-240
    • Andersson, L.1    Carriere, F.2    Lowe, M.E.3    Nilsson, A.4    Verger, R.5
  • 9
    • 0025062291 scopus 로고
    • Structure of human pancreatic lipase
    • Winkler, F. K., A. D'Arcy, and W. Hunziker. 1990. Structure of human pancreatic lipase. Nature. 343: 771-774.
    • (1990) Nature , vol.343 , pp. 771-774
    • Winkler, F.K.1    D'Arcy, A.2    Hunziker, W.3
  • 11
    • 0026687923 scopus 로고
    • Structure of the pancreatic lipase-procolipase complex
    • van Tilbeurgh, H., L. Sarda, R. Verger, and C. Cambillau. 1992. Structure of the pancreatic lipase-procolipase complex. Nature. 359: 159-162.
    • (1992) Nature , vol.359 , pp. 159-162
    • Van Tilbeurgh, H.1    Sarda, L.2    Verger, R.3    Cambillau, C.4
  • 12
    • 0027200087 scopus 로고
    • Interfacial activation of the lipase-procolipase complex by mixed micelles revealed by X-ray crystallography
    • van Tilbeurgh, H., M. P. Egloff, C. Martinez, N. Rugani, R. Verger, and C. Cambillau. 1993. Interfacial activation of the lipase-procolipase complex by mixed micelles revealed by X-ray crystallography. Nature. 362: 814-820.
    • (1993) Nature , vol.362 , pp. 814-820
    • Van Tilbeurgh, H.1    Egloff, M.P.2    Martinez, C.3    Rugani, N.4    Verger, R.5    Cambillau, C.6
  • 13
    • 0026487341 scopus 로고
    • Human lipoprotein lipase: The loop covering the catalytic site is essential for interaction with lipid substrates
    • Dugi, K. A., H. L. Dichek, G. D. Talley, H. B. Brewer, and S. Santamarina-Fojo. 1992. Human lipoprotein lipase: the loop covering the catalytic site is essential for interaction with lipid substrates. J. Biol. Chem. 267: 25086-25091.
    • (1992) J. Biol. Chem. , vol.267 , pp. 25086-25091
    • Dugi, K.A.1    Dichek, H.L.2    Talley, G.D.3    Brewer, H.B.4    Santamarina-Fojo, S.5
  • 14
    • 0028875755 scopus 로고
    • Human hepatic and lipoprotein lipase: The loop covering the catalytic site mediates lipase substrate specificity
    • Dugi, K. A., H. L. Dichek, and S. Santamarina-Fojo. 1995. Human hepatic and lipoprotein lipase: The loop covering the catalytic site mediates lipase substrate specificity. J. Biol. Chem. 270: 25396-25401.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25396-25401
    • Dugi, K.A.1    Dichek, H.L.2    Santamarina-Fojo, S.3
  • 15
    • 0026761311 scopus 로고
    • Functional topology of a surface loop shielding the catalytic center in lipoprotein lipase
    • Faustinella, F., L. C. Smith, and L. Chan. 1992. Functional topology of a surface loop shielding the catalytic center in lipoprotein lipase. Biochemistry. 31: 7219-7223.
    • (1992) Biochemistry. , vol.31 , pp. 7219-7223
    • Faustinella, F.1    Smith, L.C.2    Chan, L.3
  • 17
    • 0028152436 scopus 로고
    • A surface loop covering the active site of human pancreatic lipase influences interfacial activation and lipid binding
    • Jennens, M. L., and M. E. Lowe. 1994. A surface loop covering the active site of human pancreatic lipase influences interfacial activation and lipid binding. J. Biol. Chem. 269: 25470-25474.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25470-25474
    • Jennens, M.L.1    Lowe, M.E.2
  • 18
    • 0031027027 scopus 로고    scopus 로고
    • Colipase stabilizes the lid domain of pancreatic triglyceride lipase
    • Lowe, M. 1997. Colipase stabilizes the lid domain of pancreatic triglyceride lipase. J. Biol. Chem. 272: 9-12.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9-12
    • Lowe, M.1
  • 20
    • 0023684064 scopus 로고
    • A general method of in vitro preparation and specific mutations of DNA fragments: Study of protein and DNA interactions
    • Higuchi, R., B. Krummel, and R. K. Saiki. 1988. A general method of in vitro preparation and specific mutations of DNA fragments: study of protein and DNA interactions. Nucleic Acids Res. 16: 7351-7367.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 7351-7367
    • Higuchi, R.1    Krummel, B.2    Saiki, R.K.3
  • 21
    • 0028307251 scopus 로고
    • Rat pancreatic lipase and two related proteins: Enzymatic properties and mRNA expression during development
    • Payne, R. M., H. F. Sims, M. L. Jennens, and M. E. Lowe. 1994. Rat pancreatic lipase and two related proteins: enzymatic properties and mRNA expression during development. Am. J. Physiol. 266: G914-G921.
    • (1994) Am. J. Physiol. , vol.266
    • Payne, R.M.1    Sims, H.F.2    Jennens, M.L.3    Lowe, M.E.4
  • 22
    • 0032103761 scopus 로고    scopus 로고
    • Human pancreatic triglyceride lipase expressed in yeast cells: Purification and characterization
    • Yang, Y., and M. Lowe. 1998. Human pancreatic triglyceride lipase expressed in yeast cells: Purification and characterization. Protein Expr. Purif. 13: 36-40.
    • (1998) Protein Expr. Purif. , vol.13 , pp. 36-40
    • Yang, Y.1    Lowe, M.2
  • 23
    • 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
  • 24
    • 0032102712 scopus 로고    scopus 로고
    • Purification and characterization of human procolipase expressed in yeast cells
    • Cordle, R. A., and M. E. Lowe. 1998. Purification and characterization of human procolipase expressed in yeast cells. Protein Expr. Purif. 13: 30-35.
    • (1998) Protein Expr. Purif. , vol.13 , pp. 30-35
    • Cordle, R.A.1    Lowe, M.E.2
  • 25
    • 0032614763 scopus 로고    scopus 로고
    • Assays for pancreatic triglyceride lipase and colipase
    • M. H. Doolittle, and K. Reue, editors. Humana Press Inc., Totowa, NJ
    • Lowe, M. E. 1998. Assays for pancreatic triglyceride lipase and colipase. In Methods in Molecular Biology: Lipase and Phopholipase Protocols. Vol. 109. M. H. Doolittle, and K. Reue, editors. Humana Press Inc., Totowa, NJ. 59-70.
    • (1998) Methods in Molecular Biology: Lipase and Phopholipase Protocols , vol.109 , pp. 59-70
    • Lowe, M.E.1
  • 26
    • 0024278678 scopus 로고
    • Kinetic analysis of the Ca-dependent, membrane-bound, macrophage phospholipase A2 and the effects of arachidonic acid
    • Lister, M. D., R. A. Deems, Y. Watanabe, R. J. Ulevitch, and E. A. Dennis. 1988. Kinetic analysis of the Ca-dependent, membrane-bound, macrophage phospholipase A2 and the effects of arachidonic acid. J. Biol. Chem. 263: 7506-7513.
    • (1988) J. Biol. Chem. , vol.263 , pp. 7506-7513
    • Lister, M.D.1    Deems, R.A.2    Watanabe, Y.3    Ulevitch, R.J.4    Dennis, E.A.5
  • 27
    • 0029148636 scopus 로고
    • On the interfacial activation of Candida antartica lipase A and B as compared with Humicola lanuginosa lipase
    • Martinelle, M., M. Holmquist, and K. Hult. 1995. On the interfacial activation of Candida antartica lipase A and B as compared with Humicola lanuginosa lipase. Biochim. Biophys. Acta. 1258: 272-276.
    • (1995) Biochim. Biophys. Acta. , vol.1258 , pp. 272-276
    • Martinelle, M.1    Holmquist, M.2    Hult, K.3
  • 28
    • 0026550733 scopus 로고
    • Catalysis at the interface: The anatomy of a conformational change in a triglyceride lipase
    • Derewenda, U., A. M. Brzozowski, D. M. Lawson, and Z. S. Derewenda. 1992. Catalysis at the interface: the anatomy of a conformational change in a triglyceride lipase. Biochemistry. 31: 1532-1541.
    • (1992) Biochemistry. , vol.31 , pp. 1532-1541
    • Derewenda, U.1    Brzozowski, A.M.2    Lawson, D.M.3    Derewenda, Z.S.4
  • 29
    • 0029161231 scopus 로고
    • The 2.46 a resolution of the pancreatic lipase-colipase complex inhibited by a C11 alkyl phosphonate
    • Egloff, M. P., F. Marguet, G. Buono, R. Verger, C. Cambillau, and H. van Tilbeurgh. 1995. The 2.46 A resolution of the pancreatic lipase-colipase complex inhibited by a C11 alkyl phosphonate. Biochemistry. 24: 2751-2762.
    • (1995) Biochemistry. , vol.24 , pp. 2751-2762
    • Egloff, M.P.1    Marguet, F.2    Buono, G.3    Verger, R.4    Cambillau, C.5    Van Tilbeurgh, H.6
  • 30
    • 0030881003 scopus 로고    scopus 로고
    • New pancreatic lipases: Gene expression, protein secretion, and the newborn
    • Lowe, M. E. 1997. New pancreatic lipases: gene expression, protein secretion, and the newborn. Methods Enzymol. 284: 285-297.
    • (1997) Methods Enzymol. , vol.284 , pp. 285-297
    • Lowe, M.E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.