메뉴 건너뛰기




Volumn 102, Issue 4, 1998, Pages 828-836

A mesangium-predominant gene, megsin, is a new serpin upregulated in IgA nephropathy

Author keywords

3' directed cDNA library; Cell specific protein; Glomerulonephritis; Mesangial proliferation; Serpin

Indexed keywords

CELL PROTEIN; SERINE PROTEINASE INHIBITOR;

EID: 0032528967     PISSN: 00219738     EISSN: None     Source Type: Journal    
DOI: 10.1172/JCI2450     Document Type: Article
Times cited : (79)

References (38)
  • 1
    • 0031887859 scopus 로고    scopus 로고
    • Functional quantitative analysis of the genome in cultured human mesangial cells
    • Yasuda, Y., T. Miyata, M. Nangaku, Y. Iida, K. Maeda, K. Kurokawa, and K. Okuho. 1998. Functional quantitative analysis of the genome in cultured human mesangial cells. Kidney Int. 53:154-158.
    • (1998) Kidney Int. , vol.53 , pp. 154-158
    • Yasuda, Y.1    Miyata, T.2    Nangaku, M.3    Iida, Y.4    Maeda, K.5    Kurokawa, K.6    Okuho, K.7
  • 2
  • 3
    • 0026553672 scopus 로고
    • PROSITE: A dictionary of sites and patterns in proteins
    • Bairoch, A. 1992. PROSITE: a dictionary of sites and patterns in proteins. Nucleic Acids Res. 20:2013-2018.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 2013-2018
    • Bairoch, A.1
  • 4
    • 0029916915 scopus 로고    scopus 로고
    • The PROSITE database: Its status in 1995
    • Bairoch, A., P. Bucher, and K. Hofmann. 1996. The PROSITE database: its status in 1995. Nucleic Acids Res. 24:189-196.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 189-196
    • Bairoch, A.1    Bucher, P.2    Hofmann, K.3
  • 5
    • 0026728019 scopus 로고
    • Construction of a dictionary of sequence motifs that characterize groups of related proteins
    • Ogiwara, A., I. Uchiyama, Y. Seto, and M. Kanehisa. 1992. Construction of a dictionary of sequence motifs that characterize groups of related proteins. Protein Eng. 5:479-488.
    • (1992) Protein Eng. , vol.5 , pp. 479-488
    • Ogiwara, A.1    Uchiyama, I.2    Seto, Y.3    Kanehisa, M.4
  • 6
    • 0023989064 scopus 로고
    • Improved tools for biological sequence comparison
    • Pearson, W.R., and D.J. Lipman. 1988. Improved tools for biological sequence comparison. Proc. Natl. Acad. Sci. USA. 85:2444-2448.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 2444-2448
    • Pearson, W.R.1    Lipman, D.J.2
  • 7
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J., and R.F. Doolittle. 1982. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157:105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 8
    • 0027291015 scopus 로고
    • Prediction of protein structure at better than 70% accuracy
    • Rost, B., and C. Sander. 1993. Prediction of protein structure at better than 70% accuracy. J. Mol. Biol. 232:584-599.
    • (1993) J. Mol. Biol. , vol.232 , pp. 584-599
    • Rost, B.1    Sander, C.2
  • 9
    • 0030818120 scopus 로고    scopus 로고
    • In situ hybridization studies of matrix metalloproteinase-3, tissue inhibitor of metalloproteinase-1 and type IV collagen in diabetic nephropathy
    • Suzuki, D., M. Miyazaki, K. Jinde, T. Koji, M. Yagame, M. Endoh, Y. Nomoto, and H. Sakai. 1997. In situ hybridization studies of matrix metalloproteinase-3, tissue inhibitor of metalloproteinase-1 and type IV collagen in diabetic nephropathy. Kidney Int. 52:111-119.
    • (1997) Kidney Int. , vol.52 , pp. 111-119
    • Suzuki, D.1    Miyazaki, M.2    Jinde, K.3    Koji, T.4    Yagame, M.5    Endoh, M.6    Nomoto, Y.7    Sakai, H.8
  • 10
    • 0027756748 scopus 로고
    • cDNA analyses in the human genome project
    • Matsubara, K., and K. Okubo. 1993. cDNA analyses in the human genome project. Gene. 135:265-274.
    • (1993) Gene. , vol.135 , pp. 265-274
    • Matsubara, K.1    Okubo, K.2
  • 11
    • 0026947554 scopus 로고
    • Large scale cDNA sequencing for analysis of quantitative and qualitative aspects of gene expression
    • Okubo, K., N. Hori, R. Matoba, T. Niiyama, A. Fukushima, Y. Kojima, and K. Matsubara. 1992. Large scale cDNA sequencing for analysis of quantitative and qualitative aspects of gene expression. Nat. Genet. 2:173-179.
    • (1992) Nat. Genet. , vol.2 , pp. 173-179
    • Okubo, K.1    Hori, N.2    Matoba, R.3    Niiyama, T.4    Fukushima, A.5    Kojima, Y.6    Matsubara, K.7
  • 12
    • 0021985069 scopus 로고
    • α1-Antitrypsin and the serpins: Variation and countervariation
    • Carrell, R., and J. Travis. 1985. α1-Antitrypsin and the serpins: variation and countervariation. Trends Biochem. Sci. 10:20-24.
    • (1985) Trends Biochem. Sci. , vol.10 , pp. 20-24
    • Carrell, R.1    Travis, J.2
  • 14
    • 0028787122 scopus 로고
    • Biological and clinical aspects of plasminogen activator inhibitor type 2
    • Kruithof, E.K.O., M.S. Baker, and C.L. Bunn. 1995. Biological and clinical aspects of plasminogen activator inhibitor type 2. Blood. 86:4007-4024.
    • (1995) Blood , vol.86 , pp. 4007-4024
    • Kruithof, E.K.O.1    Baker, M.S.2    Bunn, C.L.3
  • 15
    • 0028206262 scopus 로고
    • The serpin superfamily of proteinase inhibitors: Structure, function, and regulation
    • Potempa, J., E. Korzus, and J. Travis. 1994. The serpin superfamily of proteinase inhibitors: structure, function, and regulation. J. Biol. Chem. 269: 15957-15960.
    • (1994) J. Biol. Chem. , vol.269 , pp. 15957-15960
    • Potempa, J.1    Korzus, E.2    Travis, J.3
  • 16
    • 0027393310 scopus 로고
    • The ovalbumin family of serpin proteins
    • Remold-O'Donnell, E. 1993. The ovalbumin family of serpin proteins. FEBS Lett. 315:105-108.
    • (1993) FEBS Lett. , vol.315 , pp. 105-108
    • Remold-O'Donnell, E.1
  • 17
    • 0029157233 scopus 로고
    • Mechanisms contributing to the conformational and functional flexibility of plasminogen activator inhibitor-1
    • Aertgeerts, K., H.L. De Bondt, C.J. De Ranter, and P.J. Declerck. 1995. Mechanisms contributing to the conformational and functional flexibility of plasminogen activator inhibitor-1. Nat. Struct. Biol. 2:891-897.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 891-897
    • Aertgeerts, K.1    De Bondt, H.L.2    De Ranter, C.J.3    Declerck, P.J.4
  • 18
    • 0028090118 scopus 로고
    • Function of mapsin
    • Hopkins, P.C., and J. Whisstock. 1994. Function of mapsin. Science. 265: 1893-1894.
    • (1994) Science , vol.265 , pp. 1893-1894
    • Hopkins, P.C.1    Whisstock, J.2
  • 19
    • 0029925433 scopus 로고    scopus 로고
    • Significance of secondary structure predictions on the reactive center loop region of serpins: A model for the folding of serpins into a metastable state
    • Patston, P.A., and P.G.W. Gettins. 1996. Significance of secondary structure predictions on the reactive center loop region of serpins: a model for the folding of serpins into a metastable state. FEBS Lett. 383:87-92.
    • (1996) FEBS Lett. , vol.383 , pp. 87-92
    • Patston, P.A.1    Gettins, P.G.W.2
  • 20
    • 0030159797 scopus 로고    scopus 로고
    • The structural puzzle of how serpin serine protease inhibitors work
    • Wright, H.T. 1996. The structural puzzle of how serpin serine protease inhibitors work. Bioessays. 18:453-464.
    • (1996) Bioessays , vol.18 , pp. 453-464
    • Wright, H.T.1
  • 21
    • 0029589824 scopus 로고
    • What do dysfunctional serpins tell us about molecular mobility and disease?
    • Stein, P.E., and R.W. Carrell. 1995. What do dysfunctional serpins tell us about molecular mobility and disease? Struct. Biol. 2:96-113.
    • (1995) Struct. Biol. , vol.2 , pp. 96-113
    • Stein, P.E.1    Carrell, R.W.2
  • 22
    • 0027633477 scopus 로고
    • The role of conformational change in serpin structure and function
    • Gettins, P., P.A. Patston, and M. Schapira. 1993. The role of conformational change in serpin structure and function. Bioessays. 15:461-467.
    • (1993) Bioessays , vol.15 , pp. 461-467
    • Gettins, P.1    Patston, P.A.2    Schapira, M.3
  • 23
    • 0023255581 scopus 로고
    • Sequences of the genes and polypeptide precursors for two bovine protease inhibitors
    • Creighton, T.E., and I.G. Charles. 1987. Sequences of the genes and polypeptide precursors for two bovine protease inhibitors. J. Mol. Biol. 194:11-22.
    • (1987) J. Mol. Biol. , vol.194 , pp. 11-22
    • Creighton, T.E.1    Charles, I.G.2
  • 24
    • 0023932373 scopus 로고
    • Mammalian protein secretion without signal peptide removal: Biosynthesis of plasminogen activator inhibitor-2 in U-937 cells
    • Ye, R.D., T.-C. Wun, and J.E. Sadler. 1988. Mammalian protein secretion without signal peptide removal: biosynthesis of plasminogen activator inhibitor-2 in U-937 cells. J. Biol. Chem. 263:4869-4875.
    • (1988) J. Biol. Chem. , vol.263 , pp. 4869-4875
    • Ye, R.D.1    Wun, T.-C.2    Sadler, J.E.3
  • 25
    • 0023267551 scopus 로고
    • Plasminogen activator-specific inhibitors in mouse macrophages: In vivo and in vitro modulation of their synthesis and secretion
    • Wohlwend, A., D. Belin, and J.D. Vassalli. 1987. Plasminogen activator-specific inhibitors in mouse macrophages: in vivo and in vitro modulation of their synthesis and secretion. J. Immunol. 139:1278-1284.
    • (1987) J. Immunol. , vol.139 , pp. 1278-1284
    • Wohlwend, A.1    Belin, D.2    Vassalli, J.D.3
  • 26
    • 0023124557 scopus 로고
    • Plasminogen activator-specific inhibitors produced by human monocytes/macrophages
    • Wohlwend, A., D. Belin, and J.D. Vassalli. 1987. Plasminogen activator-specific inhibitors produced by human monocytes/macrophages. J. Exp. Med. 165:320-339.
    • (1987) J. Exp. Med. , vol.165 , pp. 320-339
    • Wohlwend, A.1    Belin, D.2    Vassalli, J.D.3
  • 27
    • 0027136633 scopus 로고
    • Plasminogen-activator inhibitor type 2 (PAI-2) is a spontaneously polymerising SERPIN: Biochemical characterization of the recombinant intracellular and extracellular forms
    • Mikus, P., T. Urano, P. Liljestroem, and T. Ny. 1993. Plasminogen-activator inhibitor type 2 (PAI-2) is a spontaneously polymerising SERPIN: biochemical characterization of the recombinant intracellular and extracellular forms. Eur. J. Biochem. 218:1071-1082.
    • (1993) Eur. J. Biochem. , vol.218 , pp. 1071-1082
    • Mikus, P.1    Urano, T.2    Liljestroem, P.3    Ny, T.4
  • 28
    • 0023148141 scopus 로고
    • Phorbol ester induces the biosynthesis of glycosylated and non-glycosylated plasminogen activator inhibitor 2 in high excess over urokinase-type plasminogen activator in human U-937 lymphoma cells
    • Genton, C., E.K.O. Kruithof, and W.D. Schleuning. 1987. Phorbol ester induces the biosynthesis of glycosylated and non-glycosylated plasminogen activator inhibitor 2 in high excess over urokinase-type plasminogen activator in human U-937 lymphoma cells. J. Cell Biol. 104:705-712.
    • (1987) J. Cell Biol. , vol.104 , pp. 705-712
    • Genton, C.1    Kruithof, E.K.O.2    Schleuning, W.D.3
  • 31
    • 0028069635 scopus 로고
    • Glomerular cells in vitro versus the glomerulus in vivo
    • Floege, J., H.R. Radeke, and R.J. Johnson. 1994. Glomerular cells in vitro versus the glomerulus in vivo. Kidney Int. 45:360-368.
    • (1994) Kidney Int. , vol.45 , pp. 360-368
    • Floege, J.1    Radeke, H.R.2    Johnson, R.J.3
  • 33
    • 0029119073 scopus 로고
    • The enigma PAI-2: Gene expression, evolutionary and functional aspects
    • Bachmann, F. 1995. The enigma PAI-2: Gene expression, evolutionary and functional aspects. Thromb. Haemostasis. 74:172-179.
    • (1995) Thromb. Haemostasis , vol.74 , pp. 172-179
    • Bachmann, F.1
  • 34
    • 0030054203 scopus 로고    scopus 로고
    • Bleomycin-induced pulmonary fibrosis in transgenic mice that either lack or overexpress the murine plasminogen activator inhihitor-1 gene
    • Eitzman, D.T., R.D. McCoy, X. Zheng, W.P. Fay, T. Shen, D. Ginsburg, and R.H. Simon. 1996. Bleomycin-induced pulmonary fibrosis in transgenic mice that either lack or overexpress the murine plasminogen activator inhihitor-1 gene. J. Clin. Invest. 97:232-237.
    • (1996) J. Clin. Invest. , vol.97 , pp. 232-237
    • Eitzman, D.T.1    McCoy, R.D.2    Zheng, X.3    Fay, W.P.4    Shen, T.5    Ginsburg, D.6    Simon, R.H.7
  • 35
    • 0028874970 scopus 로고
    • Plasminogen activator inhibitor type 2 inhibits tumor necrosis factor alpha-induced apoptosis
    • Dickinson, J.L., E.J. Bates, A. Ferrante, and T.M. Antalis. 1995. Plasminogen activator inhibitor type 2 inhibits tumor necrosis factor alpha-induced apoptosis. J. Biol. Chem. 270:27894-27904.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27894-27904
    • Dickinson, J.L.1    Bates, E.J.2    Ferrante, A.3    Antalis, T.M.4
  • 36
    • 0025746246 scopus 로고
    • Protection from tumor necrosis factor-mediated cytolysis by overexpression of plasminogen activator inhibitor type-2
    • Kumar, S., and C. Baglioni. 1991. Protection from tumor necrosis factor-mediated cytolysis by overexpression of plasminogen activator inhibitor type-2. J. Biol. Chem. 266:20960-20964.
    • (1991) J. Biol. Chem. , vol.266 , pp. 20960-20964
    • Kumar, S.1    Baglioni, C.2
  • 37
    • 0014211618 scopus 로고
    • On the size of the active site in proteases. I. Papain
    • Schechter, I., and A. Berger. 1967. On the size of the active site in proteases. I. Papain. Biochem. Biophys. Res. Commun. 27:157-162.
    • (1967) Biochem. Biophys. Res. Commun. , vol.27 , pp. 157-162
    • Schechter, I.1    Berger, A.2
  • 38
    • 0031032401 scopus 로고    scopus 로고
    • Squamous cell carcinoma antigen 2 is a novel serpin that inhibits the chyotrypsin-like proteases cathepsin G and mast cell chymase
    • Schick, C., Y. Kamachi, A.J. Bartuski, S. Cataltepe, N.M. Schechter, P.A. Pemberton, and G.A. Silverman. 1997. Squamous cell carcinoma antigen 2 is a novel serpin that inhibits the chyotrypsin-like proteases cathepsin G and mast cell chymase. J. Biol. Chem. 272:1849-1855.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1849-1855
    • Schick, C.1    Kamachi, Y.2    Bartuski, A.J.3    Cataltepe, S.4    Schechter, N.M.5    Pemberton, P.A.6    Silverman, G.A.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.