메뉴 건너뛰기




Volumn 4, Issue 11, 2005, Pages 1710-1717

The lipolytic proteome of mouse adipose tissue

Author keywords

[No Author keywords available]

Indexed keywords

TRIACYLGLYCEROL LIPASE;

EID: 28644432203     PISSN: 15359476     EISSN: None     Source Type: Journal    
DOI: 10.1074/mcp.M500062-MCP200     Document Type: Article
Times cited : (52)

References (50)
  • 2
    • 0036254607 scopus 로고    scopus 로고
    • Insulin resistance in type 2 diabetes: Role of fatty acids
    • Arner, P. (2002) Insulin resistance in type 2 diabetes: role of fatty acids. Diabetes Metab. Res. Rev. 18, Suppl. 2, S5-S9
    • (2002) Diabetes Metab. Res. Rev. , vol.18 , Issue.SUPPL. 2
    • Arner, P.1
  • 3
    • 8844255630 scopus 로고    scopus 로고
    • Free fatty acids in obesity and type 2 diabetes: Defining their role in the development of insulin resistance and beta-cell dysfunction
    • Boden, G., and Shulman, G. I. (2002) Free fatty acids in obesity and type 2 diabetes: defining their role in the development of insulin resistance and beta-cell dysfunction. Eur. J. Clin. Investig. 32, Suppl. 3, 14-23
    • (2002) Eur. J. Clin. Investig. , vol.32 , Issue.SUPPL. 3 , pp. 14-23
    • Boden, G.1    Shulman, G.I.2
  • 4
    • 0141857891 scopus 로고    scopus 로고
    • Fatty acid metabolism in obesity and type 2 diabetes mellitus
    • Blaak, E. E. (2003) Fatty acid metabolism in obesity and type 2 diabetes mellitus. Proc. Nutr. Soc. 62, 753-760
    • (2003) Proc. Nutr. Soc. , vol.62 , pp. 753-760
    • Blaak, E.E.1
  • 5
    • 0018324166 scopus 로고
    • Pancreatic lipase and colipase. An example of heterogeneous biocatalysis
    • Semeriva, M., and Desnuelle, P. (1979) Pancreatic lipase and colipase. An example of heterogeneous biocatalysis. Adv. Enzymol. Relat. Areas Mol. Biol. 48, 319-370
    • (1979) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.48 , pp. 319-370
    • Semeriva, M.1    Desnuelle, P.2
  • 6
    • 0036775676 scopus 로고    scopus 로고
    • Lipoprotein lipase: The regulation of tissue specific expression and its role in lipid and energy metabolism
    • Preiss-Landl, K., Zimmermann, R., Hammerle, G., and Zechner, R. (2002) Lipoprotein lipase: the regulation of tissue specific expression and its role in lipid and energy metabolism. Curr. Opin. Lipidol. 13, 471-481
    • (2002) Curr. Opin. Lipidol. , vol.13 , pp. 471-481
    • Preiss-Landl, K.1    Zimmermann, R.2    Hammerle, G.3    Zechner, R.4
  • 7
    • 0034128132 scopus 로고    scopus 로고
    • Hepatic lipase and HDL metabolism
    • Thuren, T. (2000) Hepatic lipase and HDL metabolism. Curr. Opin. Lipidol. 11, 277-283
    • (2000) Curr. Opin. Lipidol. , vol.11 , pp. 277-283
    • Thuren, T.1
  • 9
    • 0036794551 scopus 로고    scopus 로고
    • Hormone-sensitive lipase: Control of intracellular tri-(di-)acylglycerol and cholesteryl ester hydrolysis
    • Kraemer, F. B., and Shen, W. J. (2002) Hormone-sensitive lipase: control of intracellular tri-(di-)acylglycerol and cholesteryl ester hydrolysis. J. Lipid Res. 43, 1585-1594
    • (2002) J. Lipid Res. , vol.43 , pp. 1585-1594
    • Kraemer, F.B.1    Shen, W.J.2
  • 10
    • 0030767295 scopus 로고    scopus 로고
    • cDNA cloning, tissue distribution, and identification of the catalytic triad of monoglyceride lipase. Evolutionary relationship to esterases, lysophospholipases, and haloperoxidases
    • Karlsson, M., Contreras, J. A., Hellman, U., Tornqvist, H., and Holm, C. (1997) cDNA cloning, tissue distribution, and identification of the catalytic triad of monoglyceride lipase. Evolutionary relationship to esterases, lysophospholipases, and haloperoxidases. J. Biol. Chem. 272, 27218-27223
    • (1997) J. Biol. Chem. , vol.272 , pp. 27218-27223
    • Karlsson, M.1    Contreras, J.A.2    Hellman, U.3    Tornqvist, H.4    Holm, C.5
  • 11
    • 0035967790 scopus 로고    scopus 로고
    • The cloning and expression of a murine triacylglycerol hydrolase cDNA and the structure of its corresponding gene
    • Dolinsky, V. W., Sipione, S., Lehner, R., and Vance, D. E. (2001) The cloning and expression of a murine triacylglycerol hydrolase cDNA and the structure of its corresponding gene. Biochim. Biophys. Acta 1532, 162-172
    • (2001) Biochim. Biophys. Acta , vol.1532 , pp. 162-172
    • Dolinsky, V.W.1    Sipione, S.2    Lehner, R.3    Vance, D.E.4
  • 12
    • 12844286809 scopus 로고    scopus 로고
    • Triacylglycerol hydrolase is localized to the endoplasmic reticulum by an unusual retrieval sequence where it participates in VLDL assembly without utilizing VLDL lipids as substrates
    • Gilham, D., Alam, M., Gao, W., Vance, D. E., and Lehner, R. (2005) Triacylglycerol hydrolase is localized to the endoplasmic reticulum by an unusual retrieval sequence where it participates in VLDL assembly without utilizing VLDL lipids as substrates. Mol. Biol. Cell 16, 984-996
    • (2005) Mol. Biol. Cell , vol.16 , pp. 984-996
    • Gilham, D.1    Alam, M.2    Gao, W.3    Vance, D.E.4    Lehner, R.5
  • 13
    • 0033636862 scopus 로고    scopus 로고
    • Chemical strategies for the global analysis of protein function
    • Cravatt, B. F., and Sorensen, E. J. (2000) Chemical strategies for the global analysis of protein function. Curr. Opin. Chem. Biol. 4, 663-668
    • (2000) Curr. Opin. Chem. Biol. , vol.4 , pp. 663-668
    • Cravatt, B.F.1    Sorensen, E.J.2
  • 15
    • 0037397491 scopus 로고    scopus 로고
    • Functional profiling of the proteome with affinity labels
    • Campbell, D. A., and Szardenings, A. K. (2003) Functional profiling of the proteome with affinity labels. Curr. Opin. Chem. Biol. 7, 296-303
    • (2003) Curr. Opin. Chem. Biol. , vol.7 , pp. 296-303
    • Campbell, D.A.1    Szardenings, A.K.2
  • 16
    • 0347087452 scopus 로고    scopus 로고
    • Chemical strategies for activity-based proteomics
    • Speers, A. E., and Cravatt, B. F. (2004) Chemical strategies for activity-based proteomics. ChemBioChem 5, 41-47
    • (2004) ChemBioChem , vol.5 , pp. 41-47
    • Speers, A.E.1    Cravatt, B.F.2
  • 19
    • 0030874881 scopus 로고    scopus 로고
    • Lipases and α/β hydrolase fold
    • Schrag, J. D., and Cygler, M. (1997) Lipases and α/β hydrolase fold. Methods Enzymol. 284, 85-107
    • (1997) Methods Enzymol. , vol.284 , pp. 85-107
    • Schrag, J.D.1    Cygler, M.2
  • 20
    • 0035469599 scopus 로고    scopus 로고
    • Direct visualization of serine hydrolase activities in complex proteomes using fluorescent active site-directed probes
    • Patricelli, M. P., Giang, D. K., Stamp, L. M., and Burbaum, J. J. (2001) Direct visualization of serine hydrolase activities in complex proteomes using fluorescent active site-directed probes. Proteomics 1, 1067-1071
    • (2001) Proteomics , vol.1 , pp. 1067-1071
    • Patricelli, M.P.1    Giang, D.K.2    Stamp, L.M.3    Burbaum, J.J.4
  • 21
    • 0036678119 scopus 로고    scopus 로고
    • Enzyme activity profiles of the secreted and membrane proteome that depict cancer cell invasiveness
    • Jessani, N., Liu, Y., Humphrey, M., and Cravatt, B. F. (2002) Enzyme activity profiles of the secreted and membrane proteome that depict cancer cell invasiveness. Proc. Natl. Acad. Sci. U. S. A. 99, 10335-10340
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 10335-10340
    • Jessani, N.1    Liu, Y.2    Humphrey, M.3    Cravatt, B.F.4
  • 23
    • 0141518525 scopus 로고    scopus 로고
    • Fluorescent organophosphonates as inhibitors of microbial lipases
    • Oskolkova, O. V., Saf, R., Zenzmaier, E., and Hermetter, A. (2003) Fluorescent organophosphonates as inhibitors of microbial lipases. Chem. Phys. Lipids 125, 103-114
    • (2003) Chem. Phys. Lipids , vol.125 , pp. 103-114
    • Oskolkova, O.V.1    Saf, R.2    Zenzmaier, E.3    Hermetter, A.4
  • 24
    • 0344577852 scopus 로고    scopus 로고
    • Fluorescent inhibitors for the qualitative and quantitative analysis of lipolytic enzymes
    • Scholze, H., Stutz, H., Paltauf, F., and Hermetter, A. (1999) Fluorescent inhibitors for the qualitative and quantitative analysis of lipolytic enzymes. Anal. Biochem. 276, 72-80
    • (1999) Anal. Biochem. , vol.276 , pp. 72-80
    • Scholze, H.1    Stutz, H.2    Paltauf, F.3    Hermetter, A.4
  • 25
    • 18844466768 scopus 로고    scopus 로고
    • Identification of various lipolytic enzymes in crude porcine pancreatic lipase preparations using covalent fluorescent inhibitors
    • Birner-Grunberger, R., Scholze, H., Faber, K., and Hermetter, A. (2004) Identification of various lipolytic enzymes in crude porcine pancreatic lipase preparations using covalent fluorescent inhibitors. Biotechnol. Bioeng. 85, 147-154
    • (2004) Biotechnol. Bioeng. , vol.85 , pp. 147-154
    • Birner-Grunberger, R.1    Scholze, H.2    Faber, K.3    Hermetter, A.4
  • 27
    • 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
  • 28
    • 0022539027 scopus 로고
    • Peptide and protein molecular weight determination by electrophoresis using a high-molarity tris buffer system without urea
    • Fling, S. P., and Gregerson, D. S. (1986) Peptide and protein molecular weight determination by electrophoresis using a high-molarity tris buffer system without urea. Anal. Biochem. 155, 83-88
    • (1986) Anal. Biochem. , vol.155 , pp. 83-88
    • Fling, S.P.1    Gregerson, D.S.2
  • 29
    • 84988129091 scopus 로고
    • Improved horizontal two-dimensional electrophoresis with hybrid isoelectric-focusing in immobilized pH gradients in the 1st-dimension and laying-on transfer to the 2nd-dimension
    • Gorg, A., Postel, W., Gunther, S., and Weser J. (1985) Improved horizontal two-dimensional electrophoresis with hybrid isoelectric-focusing in immobilized pH gradients in the 1st-dimension and laying-on transfer to the 2nd-dimension. Electrophoresis 6, 599-604
    • (1985) Electrophoresis , vol.6 , pp. 599-604
    • Gorg, A.1    Postel, W.2    Gunther, S.3    Weser, J.4
  • 30
    • 0023768475 scopus 로고
    • The current state of two-dimensional electrophoresis with immobilized pH gradients
    • Gorg, A., Postel, W., and Gunther, S. (1988) The current state of two-dimensional electrophoresis with immobilized pH gradients. Electrophoresis 9, 531-546
    • (1988) Electrophoresis , vol.9 , pp. 531-546
    • Gorg, A.1    Postel, W.2    Gunther, S.3
  • 31
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins from silver stained polyacrylamide gels
    • Shevchenko, A., Wilm, M., Vorm, O., and Mann, M. (1996) Mass spectrometric sequencing of proteins from silver stained polyacrylamide gels. Anal. Chem. 68, 850-858
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 32
    • 3042735127 scopus 로고    scopus 로고
    • The need for guidelines in publication of peptide and protein identification data
    • Working Group on Publication Guidelines for Peptide and Protein Identification Data
    • Carr, S., Aebersold, R., Baldwin, M., Burlingame, A., Clauser, K., and Nesvizhskii, A. (2004) The need for guidelines in publication of peptide and protein identification data. Working Group on Publication Guidelines for Peptide and Protein Identification Data. Mol. Cell. Proteomics 3, 531-533
    • (2004) Mol. Cell. Proteomics , vol.3 , pp. 531-533
    • Carr, S.1    Aebersold, R.2    Baldwin, M.3    Burlingame, A.4    Clauser, K.5    Nesvizhskii, A.6
  • 34
    • 0031019790 scopus 로고    scopus 로고
    • Purification and characterization of a porcine liver microsomal triacylglycerol hydrolase
    • Lehner, R., and Verger, R. (1997) Purification and characterization of a porcine liver microsomal triacylglycerol hydrolase. Biochemistry (Mosc.) 36, 1861-1868
    • (1997) Biochemistry (Mosc.) , vol.36 , pp. 1861-1868
    • Lehner, R.1    Verger, R.2
  • 35
    • 0020478566 scopus 로고
    • Lipoprotein lipase-catalyzed hydrolysis of p-nitrophenyl butyrate. Interfacial activation by phospholipid vesicles
    • Shirai, K., and Jackson, R. L. (1982) Lipoprotein lipase-catalyzed hydrolysis of p-nitrophenyl butyrate. Interfacial activation by phospholipid vesicles. J. Biol. Chem. 257, 1253-1258
    • (1982) J. Biol. Chem. , vol.257 , pp. 1253-1258
    • Shirai, K.1    Jackson, R.L.2
  • 37
    • 0030973125 scopus 로고    scopus 로고
    • Cloning, expression, and catalytic mechanism of murine lysophospholipase I
    • Wang, A., Deems, R. A., and Dennis, E. A. (1997) Cloning, expression, and catalytic mechanism of murine lysophospholipase I. J. Biol. Chem. 272, 12723-12729
    • (1997) J. Biol. Chem. , vol.272 , pp. 12723-12729
    • Wang, A.1    Deems, R.A.2    Dennis, E.A.3
  • 38
    • 0023812814 scopus 로고
    • Purification and characterization of a lysophospholipase from a macrophage-like cell line P388D1
    • Zhang, Y. Y., and Dennis, E. A. (1988) Purification and characterization of a lysophospholipase from a macrophage-like cell line P388D1. J. Biol. Chem. 263, 9965-9972
    • (1988) J. Biol. Chem. , vol.263 , pp. 9965-9972
    • Zhang, Y.Y.1    Dennis, E.A.2
  • 39
    • 0038361307 scopus 로고    scopus 로고
    • Discovering potent and selective reversible inhibitors of enzymes in complex proteomes
    • Leung, D., Hardouin, C., Boger, D. L., and Cravatt, B. F. (2003) Discovering potent and selective reversible inhibitors of enzymes in complex proteomes. Nat. Biotechnol. 21, 687-691
    • (2003) Nat. Biotechnol. , vol.21 , pp. 687-691
    • Leung, D.1    Hardouin, C.2    Boger, D.L.3    Cravatt, B.F.4
  • 40
    • 0030583302 scopus 로고    scopus 로고
    • Isolation of cDNA for a novel human protein KNP-I that is homologous to the E. coli SCRP-27A protein from the autoimmune polyglandular disease type I (APECED) region of chromosome 21q22.3
    • Nagamine, K., Kudoh, J., Minoshima, S., Kawasaki, K., Asakawa, S., Ito, F., and Shimizu, N. (1996) Isolation of cDNA for a novel human protein KNP-I that is homologous to the E. coli SCRP-27A protein from the autoimmune polyglandular disease type I (APECED) region of chromosome 21q22.3. Biochem. Biophys. Res. Commun. 225, 608-616
    • (1996) Biochem. Biophys. Res. Commun. , vol.225 , pp. 608-616
    • Nagamine, K.1    Kudoh, J.2    Minoshima, S.3    Kawasaki, K.4    Asakawa, S.5    Ito, F.6    Shimizu, N.7
  • 41
    • 0022466965 scopus 로고
    • Purification, biochemical characterization, and biological function of human esterase D
    • Lee, W. H., Wheatley, W., Benedict, W. F., Huang, C. M., and Lee, E. Y. (1986) Purification, biochemical characterization, and biological function of human esterase D. Proc. Natl. Acad. Sci. U. S. A. 83, 6790-6794
    • (1986) Proc. Natl. Acad. Sci. U. S. A. , vol.83 , pp. 6790-6794
    • Lee, W.H.1    Wheatley, W.2    Benedict, W.F.3    Huang, C.M.4    Lee, E.Y.5
  • 42
    • 0023001208 scopus 로고
    • Molecular cloning of the human esterase D gene, a genetic marker of retinoblastoma
    • Lee, E. Y., and Lee, W. H. (1986) Molecular cloning of the human esterase D gene, a genetic marker of retinoblastoma. Proc. Natl. Acad. Sci. U. S. A. 83, 6337-6341
    • (1986) Proc. Natl. Acad. Sci. U. S. A. , vol.83 , pp. 6337-6341
    • Lee, E.Y.1    Lee, W.H.2
  • 43
    • 0036590136 scopus 로고    scopus 로고
    • Identification of additional transcripts in the Williams-Beuren syndrome critical region
    • Merla, G., Ucla, C., Guipponi, M., and Reymond, A. (2002) Identification of additional transcripts in the Williams-Beuren syndrome critical region. Hum. Genet. 110, 429-438
    • (2002) Hum. Genet. , vol.110 , pp. 429-438
    • Merla, G.1    Ucla, C.2    Guipponi, M.3    Reymond, A.4
  • 45
    • 0033553570 scopus 로고    scopus 로고
    • A protein phosphatase methylesterase (PME-1) is one of several novel proteins stably associating with two inactive mutants of protein phosphatase 2A
    • Ogris, E., Du, X., Nelson, K. C., Mak, E. K., Yu, X. X., Lane, W. S., and Pallas, D. C. (1999) A protein phosphatase methylesterase (PME-1) is one of several novel proteins stably associating with two inactive mutants of protein phosphatase 2A. J. Biol. Chem. 274, 14382-14391
    • (1999) J. Biol. Chem. , vol.274 , pp. 14382-14391
    • Ogris, E.1    Du, X.2    Nelson, K.C.3    Mak, E.K.4    Yu, X.X.5    Lane, W.S.6    Pallas, D.C.7
  • 46
    • 0026022786 scopus 로고
    • Genetic relationship between acylpeptide hydrolase and acylase, two hydrolytic enzymes with similar binding but different catalytic specificities
    • Jones, W. M., Scaloni, A., Bossa, F., Popowicz, A. M., Schneewind, O., and Manning, J. M. (1991) Genetic relationship between acylpeptide hydrolase and acylase, two hydrolytic enzymes with similar binding but different catalytic specificities. Proc. Natl. Acad. Sci. U. S. A. 88, 2194-2198
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 2194-2198
    • Jones, W.M.1    Scaloni, A.2    Bossa, F.3    Popowicz, A.M.4    Schneewind, O.5    Manning, J.M.6
  • 47
    • 0024380716 scopus 로고
    • Cloning and sequence analysis of a rat liver cDNA encoding acyl-peptide hydrolase
    • Kobayashi, K., Lin, L. W., Yeadon, J. E., Klickstein, L. B., and Smith, J. A. (1989) Cloning and sequence analysis of a rat liver cDNA encoding acyl-peptide hydrolase. J. Biol. Chem. 264, 8892-8899
    • (1989) J. Biol. Chem. , vol.264 , pp. 8892-8899
    • Kobayashi, K.1    Lin, L.W.2    Yeadon, J.E.3    Klickstein, L.B.4    Smith, J.A.5
  • 48
    • 1242337279 scopus 로고    scopus 로고
    • Esterase-like activity of serum albumin: Characterization of its structural chemistry using p-nitrophenyl esters as substrates
    • Sakurai, Y., Ma, S. F., Watanabe, H., Yamaotsu, N., Hirono, S., Kurono, Y., Kragh-Hansen, U., and Otagiri, M. (2004) Esterase-like activity of serum albumin: characterization of its structural chemistry using p-nitrophenyl esters as substrates. Pharm. Res. 21, 285-292
    • (2004) Pharm. Res. , vol.21 , pp. 285-292
    • Sakurai, Y.1    Ma, S.F.2    Watanabe, H.3    Yamaotsu, N.4    Hirono, S.5    Kurono, Y.6    Kragh-Hansen, U.7    Otagiri, M.8
  • 49
    • 0033773201 scopus 로고    scopus 로고
    • The hormone-sensitive lipase gene is transcribed from at least five alternative first exons in mouse adipose tissue
    • Laurin, N. N., Wang, S. P., and Mitchell, G. A. (2000) The hormone-sensitive lipase gene is transcribed from at least five alternative first exons in mouse adipose tissue. Mamm. Genome 11, 972-978
    • (2000) Mamm. Genome , vol.11 , pp. 972-978
    • Laurin, N.N.1    Wang, S.P.2    Mitchell, G.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.