메뉴 건너뛰기




Volumn 128, Issue 1, 2000, Pages 83-92

Four types of calpastatin isoforms with distinct amino-terminal sequences are specified by alternative first exons and differentially expressed in mouse tissues

Author keywords

Calpastatin; Exon; Isoform; Multiple promoters; Protease inhibitor

Indexed keywords

CALPASTATIN;

EID: 0033931805     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a022733     Document Type: Article
Times cited : (57)

References (54)
  • 1
    • 0001253821 scopus 로고
    • Calpain and calpastatin
    • Murachi, T. (1983) Calpain and calpastatin. Trends Biochem. Sci. 8, 167-169
    • (1983) Trends Biochem. Sci. , vol.8 , pp. 167-169
    • Murachi, T.1
  • 3
    • 0033573897 scopus 로고    scopus 로고
    • Role of calpain in adipocyte differentiation
    • Patel, Y.M. and Lane, M.D. (1999) Role of calpain in adipocyte differentiation. Proc. Natl. Acad. Sci. USA 96, 1279-1284
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 1279-1284
    • Patel, Y.M.1    Lane, M.D.2
  • 6
    • 0031570757 scopus 로고    scopus 로고
    • Calpain contributes to silica-induced IκB-α degradation and nuclear factor-κB activation
    • Chen, F., Lu, Y., Kuhn, D.C., Maki, M., Shi, X., Sun, S.C., and Demers, L.M. (1997) Calpain contributes to silica-induced IκB-α degradation and nuclear factor-κB activation. Arch. Biochem. Biophys. 342, 383-388
    • (1997) Arch. Biochem. Biophys. , vol.342 , pp. 383-388
    • Chen, F.1    Lu, Y.2    Kuhn, D.C.3    Maki, M.4    Shi, X.5    Sun, S.C.6    Demers, L.M.7
  • 8
    • 0032834418 scopus 로고    scopus 로고
    • Suppression of okadaic acid-induced apoptosis by overexpression of calpastatin in human UVr-1 cells
    • Chi, X.J., Hiwasa, T., Maki, M., Sugaya, S., Nomura, J., Kita, K., and Suzuki, N. (1999) Suppression of okadaic acid-induced apoptosis by overexpression of calpastatin in human UVr-1 cells. FEBS Lett. 459, 391-394
    • (1999) FEBS Lett. , vol.459 , pp. 391-394
    • Chi, X.J.1    Hiwasa, T.2    Maki, M.3    Sugaya, S.4    Nomura, J.5    Kita, K.6    Suzuki, N.7
  • 9
    • 0002398530 scopus 로고
    • Calpains in lens and cataract
    • Mellgren, R.L. and Murachi, T., eds. CRC Press, Boca Raton, FL
    • Shearer, T.R. and David, L.L. (1990) Calpains in lens and cataract. in Intracellular Calcium-Dependent Proteolysis (Mellgren, R.L. and Murachi, T., eds.) pp. 265-274, CRC Press, Boca Raton, FL
    • (1990) Intracellular Calcium-dependent Proteolysis , pp. 265-274
    • Shearer, T.R.1    David, L.L.2
  • 10
    • 0030445196 scopus 로고    scopus 로고
    • The calpain-calpastatin system in rheumatoid arthritis
    • Ménard, H. and El-amine, M. (1996) The calpain-calpastatin system in rheumatoid arthritis. Trends Immunol. Today 17, 545-547
    • (1996) Trends Immunol. Today , vol.17 , pp. 545-547
    • Ménard, H.1    El-Amine, M.2
  • 11
    • 0025831476 scopus 로고
    • Calcium-activated neutral protease (calpain) system: Structure, function, and regulation
    • Croall, D.E. and DeMartino, G.N. (1991) Calcium-activated neutral protease (calpain) system: Structure, function, and regulation. Physiol. Rev. 71, 813-847
    • (1991) Physiol. Rev. , vol.71 , pp. 813-847
    • Croall, D.E.1    Demartino, G.N.2
  • 12
    • 0031452173 scopus 로고    scopus 로고
    • Structure and physiological function of calpains
    • Sorimachi, H., Ishiura, S., and Suzuki, K. (1997) Structure and physiological function of calpains. Biochem. J. 328, 721-732
    • (1997) Biochem. J. , vol.328 , pp. 721-732
    • Sorimachi, H.1    Ishiura, S.2    Suzuki, K.3
  • 13
    • 0001854880 scopus 로고    scopus 로고
    • Structure of calpastatin and its inhibitory control of calpain
    • Wang, K.K.W. and Yuen, P.-W., eds. Taylor & Francis, Philadelphia, PA
    • Takano, E. and Maki, M. (1999) Structure of calpastatin and its inhibitory control of calpain. in Calpain: Pharmacology and Toxicology of Calcium-Dependent Protease (Wang, K.K.W. and Yuen, P.-W., eds.) pp. 25-49, Taylor & Francis, Philadelphia, PA
    • (1999) Calpain: Pharmacology and Toxicology of Calcium-dependent Protease , pp. 25-49
    • Takano, E.1    Maki, M.2
  • 14
    • 0028148057 scopus 로고
    • Amino-terminal conserved region in proteinase inhibitor domain of calpastatin potentiates its calpain inhibitory activity by interacting with calmodulin-like domain of the proteinase
    • Ma, H., Yang, H.Q., Takano, E., Hatanaka, M., and Maki, M. (1994) Amino-terminal conserved region in proteinase inhibitor domain of calpastatin potentiates its calpain inhibitory activity by interacting with calmodulin-like domain of the proteinase. J. Biol. Chem. 269, 24430-24436
    • (1994) J. Biol. Chem. , vol.269 , pp. 24430-24436
    • Ma, H.1    Yang, H.Q.2    Takano, E.3    Hatanaka, M.4    Maki, M.5
  • 15
    • 0028263631 scopus 로고
    • Analysis of calcium-dependent interaction between amino-terminal conserved region of calpastatin functional domain and calmodulin-like domain of μ-calpain large subunit
    • Yang, H.Q., Ma, H., Takano, E., Hatanaka, M., and Maki, M. (1994) Analysis of calcium-dependent interaction between amino-terminal conserved region of calpastatin functional domain and calmodulin-like domain of μ-calpain large subunit. J. Biol. Chem. 269, 18977-18984
    • (1994) J. Biol. Chem. , vol.269 , pp. 18977-18984
    • Yang, H.Q.1    Ma, H.2    Takano, E.3    Hatanaka, M.4    Maki, M.5
  • 16
    • 0028965234 scopus 로고
    • Preference of calcium-dependent interactions between calmodulin-like domains of calpain and calpastatin subdomains
    • Takano, E., Ma, H., Yang, H.Q., Maki, M., and Hatanaka, M. (1995) Preference of calcium-dependent interactions between calmodulin-like domains of calpain and calpastatin subdomains. FEBS Lett. 362, 93-97
    • (1995) FEBS Lett. , vol.362 , pp. 93-97
    • Takano, E.1    Ma, H.2    Yang, H.Q.3    Maki, M.4    Hatanaka, M.5
  • 17
    • 0038057187 scopus 로고
    • Endogenous inhibitor for calcium-dependent cysteine protease contains four internal repeats that could be responsible for its multiple reactive sites
    • Emori, Y., Kawasaki, H., Imajoh, S., Minami, Y., and Suzuki, K. (1987) Endogenous inhibitor for calcium-dependent cysteine protease contains four internal repeats that could be responsible for its multiple reactive sites. Proc. Natl Acad. Sci. USA 84, 3590-3594
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 3590-3594
    • Emori, Y.1    Kawasaki, H.2    Imajoh, S.3    Minami, Y.4    Suzuki, K.5
  • 18
    • 0023920362 scopus 로고
    • Pig heart calpastatin: Identification of repetitive domain structures and anomalous behavior in polyacrylamide gel electrophoresis
    • Takano, E., Maki, M., Mori, H., Hatanaka, M., Marti, T., Titani, K., Kannagi, R., Ooi, T., and Murachi, T. (1988) Pig heart calpastatin: identification of repetitive domain structures and anomalous behavior in polyacrylamide gel electrophoresis. Biochemistry 27, 1964-1972
    • (1988) Biochemistry , vol.27 , pp. 1964-1972
    • Takano, E.1    Maki, M.2    Mori, H.3    Hatanaka, M.4    Marti, T.5    Titani, K.6    Kannagi, R.7    Ooi, T.8    Murachi, T.9
  • 20
    • 0025975755 scopus 로고
    • Rat calpastatin has diverged primary sequence from other mammalian calpastatins but retains functionally important sequences
    • Ishida, S., Emori, Y., and Suzuki, K. (1991) Rat calpastatin has diverged primary sequence from other mammalian calpastatins but retains functionally important sequences. Biochim. Biophys. Acta 1088, 436-438
    • (1991) Biochim. Biophys. Acta , vol.1088 , pp. 436-438
    • Ishida, S.1    Emori, Y.2    Suzuki, K.3
  • 21
    • 0028398180 scopus 로고
    • Bovine skeletal muscle calpastatin: Cloning, sequence analysis, and steady-state mRNA expression
    • Killefer, J. and Koohmaraie, M. (1994) Bovine skeletal muscle calpastatin: cloning, sequence analysis, and steady-state mRNA expression. J. Anim. Sci. 72, 606-614
    • (1994) J. Anim. Sci. , vol.72 , pp. 606-614
    • Killefer, J.1    Koohmaraie, M.2
  • 23
    • 0031962266 scopus 로고    scopus 로고
    • The bovine calpastatin gene promoter and a new N-terminal region of the protein are targets for cAMP-dependent protein kinase activity
    • Cong, M., Thompson, V.F., Goll, D.E., and Antin, PB. (1998) The bovine calpastatin gene promoter and a new N-terminal region of the protein are targets for cAMP-dependent protein kinase activity. J. Biol. Chem. 273, 660-666
    • (1998) J. Biol. Chem. , vol.273 , pp. 660-666
    • Cong, M.1    Thompson, V.F.2    Goll, D.E.3    Antin, P.B.4
  • 24
    • 0033526847 scopus 로고    scopus 로고
    • Structure of mouse calpastatin isoforms: Implications of species-common and species-specific alternative splicing
    • Takano, J., Kawamura, T., Murase, M., Hitomi, K., and Maki, M. (1999) Structure of mouse calpastatin isoforms: implications of species-common and species-specific alternative splicing. Biochem. Biophys. Res. Commun. 260, 339-345
    • (1999) Biochem. Biophys. Res. Commun. , vol.260 , pp. 339-345
    • Takano, J.1    Kawamura, T.2    Murase, M.3    Hitomi, K.4    Maki, M.5
  • 25
    • 0026644784 scopus 로고
    • Molecular diversity in amino-terminal domains of human calpastatin by exon skipping
    • Lee, W.J., Ma, H., Takano, E., Yang, H.Q., Hatanaka, M., and Maki, M. (1992) Molecular diversity in amino-terminal domains of human calpastatin by exon skipping. J. Biol. Chem. 267, 8437-8442
    • (1992) J. Biol. Chem. , vol.267 , pp. 8437-8442
    • Lee, W.J.1    Ma, H.2    Takano, E.3    Yang, H.Q.4    Hatanaka, M.5    Maki, M.6
  • 26
    • 0026703169 scopus 로고
    • Cloning and stable maintenance of 300-kilobase-pair fragments of human DNA in Escherichia coli using an F-factor-based vector
    • Shizuya, H., Birren, B., Kim, U.J., Mancino, V., Slepak, T., Tachiiri, Y., and Simon, M. (1992) Cloning and stable maintenance of 300-kilobase-pair fragments of human DNA in Escherichia coli using an F-factor-based vector. Proc. Natl. Acad. Sci. USA 89, 8794-8797
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 8794-8797
    • Shizuya, H.1    Birren, B.2    Kim, U.J.3    Mancino, V.4    Slepak, T.5    Tachiiri, Y.6    Simon, M.7
  • 27
    • 0018800089 scopus 로고
    • A rapid alkaline extraction procedure for screening recombinant plasmid DNA
    • Birnboim, H.C. and Doly, J. (1979) A rapid alkaline extraction procedure for screening recombinant plasmid DNA. Nucleic Acids Res. 7, 1513-1523
    • (1979) Nucleic Acids Res. , vol.7 , pp. 1513-1523
    • Birnboim, H.C.1    Doly, J.2
  • 28
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski, P. and Sacchi, N. (1986) Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162, 156-159
    • (1986) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 29
    • 0026515545 scopus 로고
    • Multiple forms of rat calpastatin cDNA in the coding region of functionally unknown amino-terminal domain
    • Lee, W.J., Hatanaka, M., and Maki, M., (1992) Multiple forms of rat calpastatin cDNA in the coding region of functionally unknown amino-terminal domain. Biochim. Biophys. Acta 1129, 251-253
    • (1992) Biochim. Biophys. Acta , vol.1129 , pp. 251-253
    • Lee, W.J.1    Hatanaka, M.2    Maki, M.3
  • 30
    • 0023651307 scopus 로고
    • RNA splice junctions of different classes of eukaryotes: Sequence statistics and functional implications in gene expression
    • Shapiro, M.B. and Senapathy, P. (1987) RNA splice junctions of different classes of eukaryotes: sequence statistics and functional implications in gene expression. Nucleic Acids Res. 15, 7155-7174
    • (1987) Nucleic Acids Res. , vol.15 , pp. 7155-7174
    • Shapiro, M.B.1    Senapathy, P.2
  • 31
    • 0032569973 scopus 로고    scopus 로고
    • cAMP responsiveness of the bovine calpastatin gene promoter
    • Cong, M., Goll, D.E., and Antin, P.B. (1998) cAMP responsiveness of the bovine calpastatin gene promoter. Biochim. Biophys. Acta 1443, 186-192
    • (1998) Biochim. Biophys. Acta , vol.1443 , pp. 186-192
    • Cong, M.1    Goll, D.E.2    Antin, P.B.3
  • 32
  • 34
    • 0025767317 scopus 로고
    • Transcription inhibition of the somatic-type phosphoglycerate kinase 1 gene in vitro by a testis-specific factor that recognizes a sequence similar to the binding site for Ets oncoproteins
    • Goto, M., Tamura, T., Mikoshiba, K., Masamune, Y., and Nakanishi, Y. (1991) Transcription inhibition of the somatic-type phosphoglycerate kinase 1 gene in vitro by a testis-specific factor that recognizes a sequence similar to the binding site for Ets oncoproteins. Nucleic Acids Res. 19, 3959-3963
    • (1991) Nucleic Acids Res. , vol.19 , pp. 3959-3963
    • Goto, M.1    Tamura, T.2    Mikoshiba, K.3    Masamune, Y.4    Nakanishi, Y.5
  • 35
    • 0028230351 scopus 로고
    • The silencer of mouse Pgk-2 consists of two discrete DNA elements that individually have no effect
    • Nishiyama, S., Masamune, Y., and Nakanishi, Y. (1994) The silencer of mouse Pgk-2 consists of two discrete DNA elements that individually have no effect. Gene 141, 261-266
    • (1994) Gene , vol.141 , pp. 261-266
    • Nishiyama, S.1    Masamune, Y.2    Nakanishi, Y.3
  • 36
    • 0022476812 scopus 로고
    • Two different molecular species of pig calpastatin. Structural and functional relationship between 107 kDa and 68 kDa molecules
    • Takano, E., Kitahara, A., Sasaki, T., Kannagi, R., and Murachi, T. (1986) Two different molecular species of pig calpastatin. Structural and functional relationship between 107 kDa and 68 kDa molecules. Biochem. J. 235, 97-102
    • (1986) Biochem. J. , vol.235 , pp. 97-102
    • Takano, E.1    Kitahara, A.2    Sasaki, T.3    Kannagi, R.4    Murachi, T.5
  • 37
    • 0026202068 scopus 로고
    • Direct measurement of calpastatin subtypes by sandwich enzyme immunoassay using monoclonal antibodies
    • Yokota, H., Katayama, M., Hino, F., Kato, I., Takano, E., Maki, M., Hatanaka, M., and Murachi, T. (1991) Direct measurement of calpastatin subtypes by sandwich enzyme immunoassay using monoclonal antibodies. Mol. Cell. Probes 5, 261-269
    • (1991) Mol. Cell. Probes , vol.5 , pp. 261-269
    • Yokota, H.1    Katayama, M.2    Hino, F.3    Kato, I.4    Takano, E.5    Maki, M.6    Hatanaka, M.7    Murachi, T.8
  • 39
    • 0023669255 scopus 로고
    • Calcium-activated neutral protease inhibitor from rabbit erythrocytes lacks the N-terminal region of the liver inhibitor but retains three inhibitor units
    • Imajoh, S., Kawasaki, H., Emori, Y., and Suzuki, K. (1987) Calcium-activated neutral protease inhibitor from rabbit erythrocytes lacks the N-terminal region of the liver inhibitor but retains three inhibitor units. Biochem. Biophys. Res. Commun. 146, 630-637
    • (1987) Biochem. Biophys. Res. Commun. , vol.146 , pp. 630-637
    • Imajoh, S.1    Kawasaki, H.2    Emori, Y.3    Suzuki, K.4
  • 40
    • 0028034815 scopus 로고
    • Calpastatin in erythrocytes of young and old individuals
    • Scharz-Benmeir, N., Glaser, T., Barnoy, S., and Kosower, N.S. (1994) Calpastatin in erythrocytes of young and old individuals. Biochem. J. 304, 365-370
    • (1994) Biochem. J. , vol.304 , pp. 365-370
    • Scharz-Benmeir, N.1    Glaser, T.2    Barnoy, S.3    Kosower, N.S.4
  • 41
    • 0032973838 scopus 로고    scopus 로고
    • Calpain-calpastatin: A novel, complete calcium-dependent protease system in human spermatozoa
    • Rojas, F.J., Brush, M., and Moretti-Rojas, I. (1999) Calpain-calpastatin: a novel, complete calcium-dependent protease system in human spermatozoa. Mol Human Reproduct. 5, 520-526
    • (1999) Mol Human Reproduct. , vol.5 , pp. 520-526
    • Rojas, F.J.1    Brush, M.2    Moretti-Rojas, I.3
  • 43
    • 0023546546 scopus 로고
    • Calcium-dependent proteases: An enzyme system active at cellular membranes?
    • Mellgren, R.L. (1987) Calcium-dependent proteases: an enzyme system active at cellular membranes?. FASEB J. 1, 110-115
    • (1987) FASEB J. , vol.1 , pp. 110-115
    • Mellgren, R.L.1
  • 44
    • 0032510276 scopus 로고    scopus 로고
    • The calpain-calpastatin system and protein degradation in fusing myoblasts
    • Barnoy, S., Glaser, T., Kosower, N.S. (1998) The calpain-calpastatin system and protein degradation in fusing myoblasts. Biochim. Biophys. Acta 1402, 52-60
    • (1998) Biochim. Biophys. Acta , vol.1402 , pp. 52-60
    • Barnoy, S.1    Glaser, T.2    Kosower, N.S.3
  • 46
    • 0023003514 scopus 로고
    • Calpain-calpastatin and fusion: Fusibility of erythrocytes is determined by a protease-protease inhibitor (calpain-calpastatin) balance
    • Glaser, T. and Kosower, N.S. (1986) Calpain-calpastatin and fusion: fusibility of erythrocytes is determined by a protease-protease inhibitor (calpain-calpastatin) balance. FEBS Lett. 206, 115-120
    • (1986) FEBS Lett. , vol.206 , pp. 115-120
    • Glaser, T.1    Kosower, N.S.2
  • 48
    • 79960655760 scopus 로고    scopus 로고
    • The DNA sequence of human chromosome 22
    • Dunham, L, Shimizu, N., Roe, B.A., Chissoe, S., et al. (1999) The DNA sequence of human chromosome 22. Nature 402, 489-495
    • (1999) Nature , vol.402 , pp. 489-495
    • Dunham, L.1    Shimizu, N.2    Roe, B.A.3    Chissoe, S.4
  • 49
    • 0029936752 scopus 로고    scopus 로고
    • Regulation of gene expression by alternative promoters
    • Ayoubi, T.A.Y. and Van de Ven, W.J.M. (1996) Regulation of gene expression by alternative promoters. FASEB J. 10, 453-460
    • (1996) FASEB J. , vol.10 , pp. 453-460
    • Ayoubi, T.A.Y.1    Van De Ven, W.J.M.2
  • 50
    • 0027402152 scopus 로고
    • Multiple promoters direct tissue-specific expression of the rat BDNF gene
    • Timmusk, T., Palm, K., Metsis, M., Reintam, T., Paalme, V., Saarma, M., and Persson, H. (1993) Multiple promoters direct tissue-specific expression of the rat BDNF gene. Neuron 10, 475-489
    • (1993) Neuron , vol.10 , pp. 475-489
    • Timmusk, T.1    Palm, K.2    Metsis, M.3    Reintam, T.4    Paalme, V.5    Saarma, M.6    Persson, H.7
  • 51
    • 0032899255 scopus 로고    scopus 로고
    • Gamma-glutamyl transpeptidase gene organization and expression: A comparative analysis in rat, mouse, pig and human species
    • Chikhi, N., Holic, N., Guellaen, G., and Laperche, Y. (1999) Gamma-glutamyl transpeptidase gene organization and expression: a comparative analysis in rat, mouse, pig and human species. Comparative Biochem. Physiol. Part B, 122, 367-380
    • (1999) Comparative Biochem. Physiol. Part B , vol.122 , pp. 367-380
    • Chikhi, N.1    Holic, N.2    Guellaen, G.3    Laperche, Y.4
  • 53
    • 0023659729 scopus 로고
    • All four internally repetitive domains of pig calpastatin possess inhibitory activities against calpains I and II
    • Maki, M., Takano, E., Mori, H., Sato, A., Murachi, T., and Hatanaka, M. (1987) All four internally repetitive domains of pig calpastatin possess inhibitory activities against calpains I and II. FEBS Lett. 223, 174-180
    • (1987) FEBS Lett. , vol.223 , pp. 174-180
    • Maki, M.1    Takano, E.2    Mori, H.3    Sato, A.4    Murachi, T.5    Hatanaka, M.6
  • 54
    • 0023835174 scopus 로고
    • All four repeating domains of the endogenous inhibitor for calcium-dependent protease independently retain inhibitory activity. Expression of the cDNA fragments in Escherichia coli
    • Emori, Y., Kawasaki, H., Imajoh, S., Minami, Y., and Suzuki, K. (1988) All four repeating domains of the endogenous inhibitor for calcium-dependent protease independently retain inhibitory activity. Expression of the cDNA fragments in Escherichia coli. J. Biol. Chem. 263, 2364-2370
    • (1988) J. Biol. Chem. , vol.263 , pp. 2364-2370
    • Emori, Y.1    Kawasaki, H.2    Imajoh, S.3    Minami, Y.4    Suzuki, K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.