메뉴 건너뛰기




Volumn 206, Issue 3, 2003, Pages 561-575

Cloning of a muscle-specific calpain from the American lobster Homarus americanus: Expression associated with muscle atrophy and restoration during moulting

Author keywords

Arthropoda; Atrophy; Calcium dependent proteinase; Calpain; cDNA; Crustacea; Gene expression; Homarus americanus; Lobster; Moulting; mRNA; Muscle

Indexed keywords

AMINO ACID SEQUENCE; ANIMALS; BASE SEQUENCE; BLOTTING, WESTERN; CALPAIN; CLONING, MOLECULAR; DNA, COMPLEMENTARY; GENE EXPRESSION REGULATION, ENZYMOLOGIC; IMMUNOHISTOCHEMISTRY; MOLECULAR SEQUENCE DATA; MOLTING; MUSCLE, SKELETAL; MUSCULAR ATROPHY; NEPHROPIDAE; PHYLOGENY; SEQUENCE ANALYSIS, DNA; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 0037323269     PISSN: 00220949     EISSN: None     Source Type: Journal    
DOI: 10.1242/jeb.00097     Document Type: Article
Times cited : (18)

References (50)
  • 1
    • 0025837971 scopus 로고
    • Characterization of cDNA clones encoding a novel calcium-activated neutral proteinase from Schistosoma mansoni
    • Andresen, K., Tom, T. D. and Strand, M. (1991). Characterization of cDNA clones encoding a novel calcium-activated neutral proteinase from Schistosoma mansoni. J. Biol. Chem. 266, 15085-15090.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15085-15090
    • Andresen, K.1    Tom, T.D.2    Strand, M.3
  • 2
    • 0029165075 scopus 로고
    • Active site residues in m-calpain: Identification by site-directed mutagenesis
    • Arthur, J. S. C., Gauthier, S. and Elce, J. S. (1995). Active site residues in m-calpain: Identification by site-directed mutagenesis. FEBS Lett. 368, 397-400.
    • (1995) FEBS Lett. , vol.368 , pp. 397-400
    • Arthur, J.S.C.1    Gauthier, S.2    Elce, J.S.3
  • 3
    • 0015221791 scopus 로고
    • Preparation and properties of plasma membrane and endoplasmic reticulum fragments from isolated rat fat cells
    • Avruch, J. and Wallach, D. F. H. (1971). Preparation and properties of plasma membrane and endoplasmic reticulum fragments from isolated rat fat cells. Biochim. Biophys. Acta 233, 334-337.
    • (1971) Biochim. Biophys. Acta , vol.233 , pp. 334-337
    • Avruch, J.1    Wallach, D.F.H.2
  • 4
    • 0031568219 scopus 로고    scopus 로고
    • 2+-dependent proteinases from lobster striated muscles: Relationship to mammalian and Drosophila calpains
    • 2+-dependent proteinases from lobster striated muscles: Relationship to mammalian and Drosophila calpains. Arch. Biochem. Biophys. 337, 232-238.
    • (1997) Arch. Biochem. Biophys. , vol.337 , pp. 232-238
    • Beyette, J.R.1    Emori, Y.2    Mykles, D.L.3
  • 5
    • 0027534408 scopus 로고
    • Purification and autolytic degradation of a calpain-like calcium-dependent proteinase from lobster (Homarus americanus) striated muscle
    • Beyette, J. R., Ma, J.-S. and Mykles, D. L. (1993). Purification and autolytic degradation of a calpain-like calcium-dependent proteinase from lobster (Homarus americanus) striated muscle. Comp. Biochem. Physiol. 104B, 95-99.
    • (1993) Comp. Biochem. Physiol. , vol.104 B , pp. 95-99
    • Beyette, J.R.1    Ma, J.-S.2    Mykles, D.L.3
  • 6
    • 0030963085 scopus 로고    scopus 로고
    • Autolysis and biochemical properties of a lobster muscle calpain-like proteinase
    • Beyette, J. R. and Mykles, D. L. (1997). Autolysis and biochemical properties of a lobster muscle calpain-like proteinase. J. Exp. Zool. 277, 106-119.
    • (1997) J. Exp. Zool. , vol.277 , pp. 106-119
    • Beyette, J.R.1    Mykles, D.L.2
  • 7
    • 0013265411 scopus 로고    scopus 로고
    • Crustacean calcium-dependent proteinases
    • ed. K. K. W. Wang and P.-W. Yuen. Washington, DC: Taylor & Francis
    • Beyette, J. R. and Mykles, D. L. (1999). Crustacean calcium-dependent proteinases. In The Pharmacology of Calpain (ed. K. K. W. Wang and P.-W. Yuen), pp. 409-427. Washington, DC: Taylor & Francis.
    • (1999) The Pharmacology of Calpain , pp. 409-427
    • Beyette, J.R.1    Mykles, D.L.2
  • 8
    • 0034893933 scopus 로고    scopus 로고
    • Calpain 3 gene mutations: Genetic and clinico-pathologic findings in limb-girdle muscular dystrophy
    • Chae, J., Minami, N., Jin, Y., Nakagawa, M., Murayama, K., Igarashi, F. and Nonaka, I. (2001). Calpain 3 gene mutations: genetic and clinico-pathologic findings in limb-girdle muscular dystrophy. Neuromusc. Disord. 11, 547-555.
    • (2001) Neuromusc. Disord. , vol.11 , pp. 547-555
    • Chae, J.1    Minami, N.2    Jin, Y.3    Nakagawa, M.4    Murayama, K.5    Igarashi, F.6    Nonaka, I.7
  • 9
    • 0027918541 scopus 로고
    • Cloning of a crustacean myosin heavy chain isoform: Exclusive expression in fast muscle
    • Cotton, J. L. S. and Mykles, D. L. (1993). Cloning of a crustacean myosin heavy chain isoform: exclusive expression in fast muscle. J. Exp. Zool. 267, 578-586.
    • (1993) J. Exp. Zool. , vol.267 , pp. 578-586
    • Cotton, J.L.S.1    Mykles, D.L.2
  • 10
    • 0032722011 scopus 로고    scopus 로고
    • Diverse mRNA expression patterns of the mouse calpain genes Capn5, Capn6 and Capn11 during development
    • Dear, T. N. and Boehm, T. (1999). Diverse mRNA expression patterns of the mouse calpain genes Capn5, Capn6 and Capn11 during development. Mech. Dev. 89, 201-209.
    • (1999) Mech. Dev. , vol.89 , pp. 201-209
    • Dear, T.N.1    Boehm, T.2
  • 11
    • 0034657159 scopus 로고    scopus 로고
    • Roles of individual EF-hands in the activation of m-calpain by calcium
    • Dutt, P., Arthur, J. S. C., Grochulski, P., Cygler, M. and Elce, J. S. (2000). Roles of individual EF-hands in the activation of m-calpain by calcium. Biochem. J. 348, 37-43.
    • (2000) Biochem. J. , vol.348 , pp. 37-43
    • Dutt, P.1    Arthur, J.S.C.2    Grochulski, P.3    Cygler, M.4    Elce, J.S.5
  • 12
    • 0027985149 scopus 로고
    • Calpain localization changes in coordination with actin-related cytoskeletal changes during early embryonic development of Drosophila
    • Emori, Y. and Saigo, K. (1994). Calpain localization changes in coordination with actin-related cytoskeletal changes during early embryonic development of Drosophila. J. Biol. Chem. 269, 25137-25142.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25137-25142
    • Emori, Y.1    Saigo, K.2
  • 14
    • 0033050067 scopus 로고    scopus 로고
    • Expression and functional characteristics of calpain 3 isoforms generated through tissue-specific transcriptional and posttranscriptional events
    • Herasse, M., Ono, Y., Fougerousse, F., Kimura, E., Stockholm, D., Beley, C., Montarras, D., Pinset, C., Sorimachi, H., Suzuki, K. et al. (1999). Expression and functional characteristics of calpain 3 isoforms generated through tissue-specific transcriptional and posttranscriptional events. Mol. Cell. Biol. 19, 4047-4055.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 4047-4055
    • Herasse, M.1    Ono, Y.2    Fougerousse, F.3    Kimura, E.4    Stockholm, D.5    Beley, C.6    Montarras, D.7    Pinset, C.8    Sorimachi, H.9    Suzuki, K.10
  • 15
    • 0034895593 scopus 로고    scopus 로고
    • CAP5.5, a life-cycle-regulated, cytoskeleton-associated protein is a member of a novel family of calpain-related proteins in Topanosoma brucei
    • Hertz-Fowler, C., Ersfeld, K. and Gull, K. (2001). CAP5.5, a life-cycle-regulated, cytoskeleton-associated protein is a member of a novel family of calpain-related proteins in Topanosoma brucei. Mol. Biochem. Parasitol. 116, 25-34.
    • (2001) Mol. Biochem. Parasitol. , vol.116 , pp. 25-34
    • Hertz-Fowler, C.1    Ersfeld, K.2    Gull, K.3
  • 16
  • 18
    • 0034903587 scopus 로고    scopus 로고
    • The calpain family and human disease
    • Huang, Y. H. and Wang, K. K. W. (2001). The calpain family and human disease. Trends Mol. Med. 7, 355-362.
    • (2001) Trends Mol. Med. , vol.7 , pp. 355-362
    • Huang, Y.H.1    Wang, K.K.W.2
  • 19
    • 0003055542 scopus 로고
    • Differential molt-induced atrophy in the dimorphic claws of male fiddler crabs, Uca pugnax
    • Ismail, S. Z. M. and Mykles, D. L. (1992). Differential molt-induced atrophy in the dimorphic claws of male fiddler crabs, Uca pugnax. J. Exp. Zool. 263, 18-31.
    • (1992) J. Exp. Zool. , vol.263 , pp. 18-31
    • Ismail, S.Z.M.1    Mykles, D.L.2
  • 20
    • 0039702848 scopus 로고    scopus 로고
    • Characterization of two recombinant Drosophila calpains - CALPA and a novel homolog, CALPB
    • Jékely, G. and Friedrich, P. (1999). Characterization of two recombinant Drosophila calpains - CALPA and a novel homolog, CALPB. J. Biol. Chem. 274, 23893-23900.
    • (1999) J. Biol. Chem. , vol.274 , pp. 23893-23900
    • Jékely, G.1    Friedrich, P.2
  • 21
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W. and Sander, C. (1983). Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22, 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 22
    • 0036214494 scopus 로고    scopus 로고
    • How calpain is activated by calcium
    • Khorchid, A. and Ikura, M. (2002). How calpain is activated by calcium. Nature Struct. Biol. 9, 239-241.
    • (2002) Nature Struct. Biol. , vol.9 , pp. 239-241
    • Khorchid, A.1    Ikura, M.2
  • 23
    • 0036591364 scopus 로고    scopus 로고
    • Ubiquitin and actin expression in claw muscles of land crab, Gecarcinus lateralis, and American lobster, Homarus americanus: Differential expression of ubiquitin in two slow muscle fibre types during moult-induced atrophy
    • Koenders, A., Yu, X. L., Chang, E. S. and Mykles, D. L. (2002). Ubiquitin and actin expression in claw muscles of land crab, Gecarcinus lateralis, and American lobster, Homarus americanus: differential expression of ubiquitin in two slow muscle fibre types during moult-induced atrophy. J. Exp. Zool. 292, 618-632.
    • (2002) J. Exp. Zool. , vol.292 , pp. 618-632
    • Koenders, A.1    Yu, X.L.2    Chang, E.S.3    Mykles, D.L.4
  • 24
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 26
    • 84993839704 scopus 로고
    • Differential degradation of myofibrillar proteins by four calcium-dependent proteinase activities from lobster muscle
    • Mattson, J. M. and Mykles, D. L. (1993). Differential degradation of myofibrillar proteins by four calcium-dependent proteinase activities from lobster muscle. J. Exp. Zool. 265, 97-106.
    • (1993) J. Exp. Zool. , vol.265 , pp. 97-106
    • Mattson, J.M.1    Mykles, D.L.2
  • 28
    • 0000944696 scopus 로고
    • Multiple variants of myofibrillar proteins in single fibers of lobster claw muscles: Evidence for two types of slow fibers in the cutter closer muscle
    • Mykles, D. L. (1985). Multiple variants of myofibrillar proteins in single fibers of lobster claw muscles: evidence for two types of slow fibers in the cutter closer muscle. Biol. Bull. 169, 476-483.
    • (1985) Biol. Bull. , vol.169 , pp. 476-483
    • Mykles, D.L.1
  • 29
    • 0023971529 scopus 로고
    • Histochemical and biochemical characterization of two slow fiber types in decapod crustacean muscles
    • Mykles, D. L. (1988). Histochemical and biochemical characterization of two slow fiber types in decapod crustacean muscles. J. Exp. Zool. 245, 232-243.
    • (1988) J. Exp. Zool. , vol.245 , pp. 232-243
    • Mykles, D.L.1
  • 30
    • 0025005910 scopus 로고
    • Calcium-dependent proteolysis in crustacean claw closer muscle maintained in vitro
    • Mykles, D. L. (1990). Calcium-dependent proteolysis in crustacean claw closer muscle maintained in vitro. J. Exp. Zool. 256, 16-30.
    • (1990) J. Exp. Zool. , vol.256 , pp. 16-30
    • Mykles, D.L.1
  • 31
    • 0032426798 scopus 로고    scopus 로고
    • Intracellular proteinases of invertebrates: Calcium-dependent and proteasome/ubiquitin-dependent systems
    • Mykles, D. L. (1998). Intracellular proteinases of invertebrates: calcium-dependent and proteasome/ubiquitin-dependent systems. Int. Rev. Cytol. 184, 157-289.
    • (1998) Int. Rev. Cytol. , vol.184 , pp. 157-289
    • Mykles, D.L.1
  • 32
    • 33745974594 scopus 로고    scopus 로고
    • Proteolytic processes underlying molt-induced claw muscle atrophy in decapod crustaceans
    • Mykles, D. L. (1999). Proteolytic processes underlying molt-induced claw muscle atrophy in decapod crustaceans. Am. Zool. 39, 541-551.
    • (1999) Am. Zool. , vol.39 , pp. 541-551
    • Mykles, D.L.1
  • 33
    • 0033658237 scopus 로고    scopus 로고
    • Purification and characterization of crustacean calpain-like proteinases
    • Mykles, D. L. (2000). Purification and characterization of crustacean calpain-like proteinases. Meth. Mol. Biol. 144, 55-66.
    • (2000) Meth. Mol. Biol. , vol.144 , pp. 55-66
    • Mykles, D.L.1
  • 34
    • 0034161350 scopus 로고    scopus 로고
    • Immunocytochemical localization of actin and tubulin in the integument of land crab (Gecarcinus lateralis) and lobster (Homarus americanus)
    • Mykles, D. L., Haire, M. F. and Skinner, D. M. (2000). Immunocytochemical localization of actin and tubulin in the integument of land crab (Gecarcinus lateralis) and lobster (Homarus americanus). J. Exp. Zool. 286, 329-342.
    • (2000) J. Exp. Zool. , vol.286 , pp. 329-342
    • Mykles, D.L.1    Haire, M.F.2    Skinner, D.M.3
  • 35
    • 0019830947 scopus 로고
    • Preferential loss of thin filaments during molt-induced atrophy in crab claw muscle
    • Mykles, D. L. and Skinner, D. M. (1981) Preferential loss of thin filaments during molt-induced atrophy in crab claw muscle. J. Ultrastr. Res. 75, 314-325.
    • (1981) J. Ultrastr. Res. , vol.75 , pp. 314-325
    • Mykles, D.L.1    Skinner, D.M.2
  • 36
    • 0020173753 scopus 로고
    • Molt cycle-associated changes in calcium-dependent proteinase activity that degrades actin and myosin in crustacean muscle
    • Mykles, D. L. and Skinner, D. M. (1982). Molt cycle-associated changes in calcium-dependent proteinase activity that degrades actin and myosin in crustacean muscle. Dev. Biol. 92, 386-397.
    • (1982) Dev. Biol. , vol.92 , pp. 386-397
    • Mykles, D.L.1    Skinner, D.M.2
  • 37
    • 0020975118 scopus 로고
    • 2+-dependent proteolytic activity in crab claw muscle. Effects of inhibitors and specificity for myofibrillar proteins
    • 2+-dependent proteolytic activity in crab claw muscle. Effects of inhibitors and specificity for myofibrillar proteins. J. Biol. Chem. 258, 10474-10480.
    • (1983) J. Biol. Chem. , vol.258 , pp. 10474-10480
    • Mykles, D.L.1    Skinner, D.M.2
  • 39
    • 0029584113 scopus 로고
    • Polyubiquitin in crustacean striated muscle: Increased expression and conjugation during molt-induced claw muscle atrophy
    • Shean, B. S. and Mykles, D. L. (1995). Polyubiquitin in crustacean striated muscle: Increased expression and conjugation during molt-induced claw muscle atrophy. Biochim. Biophys. Acta 1264, 312-322.
    • (1995) Biochim. Biophys. Acta , vol.1264 , pp. 312-322
    • Shean, B.S.1    Mykles, D.L.2
  • 40
    • 0013965112 scopus 로고
    • Breakdown and reformation of somatic muscle during the molt cycle of the land crab, Gecarcinus lateralis
    • Skinner, D. M. (1966). Breakdown and reformation of somatic muscle during the molt cycle of the land crab, Gecarcinus lateralis. J. Exp. Zool. 163, 115-124.
    • (1966) J. Exp. Zool. , vol.163 , pp. 115-124
    • Skinner, D.M.1
  • 41
    • 0034655551 scopus 로고    scopus 로고
    • Proteolysis in Caenorhabditis elegans sex determination: Cleavage of TRA-2A by TRA-3
    • Sokol, S. B. and Kuwabara, P. E. (2000). Proteolysis in Caenorhabditis elegans sex determination: cleavage of TRA-2A by TRA-3. Genes Dev. 14, 901-906.
    • (2000) Genes Dev. , vol.14 , pp. 901-906
    • Sokol, S.B.1    Kuwabara, P.E.2
  • 46
    • 0028851344 scopus 로고
    • CalpA, a Drosophila calpain homolog specifically expressed in a small set of nerve, midgut, and blood cells
    • Theopold, U., Pintér, M., Daffre, S., Tryselius, Y., Friedrich, P., Nässel, D. R. and Hultmark, D. (1995). CalpA, a Drosophila calpain homolog specifically expressed in a small set of nerve, midgut, and blood cells. Mol. Cell. Biol. 15, 824-834.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 824-834
    • Theopold, U.1    Pintér, M.2    Daffre, S.3    Tryselius, Y.4    Friedrich, P.5    Nässel, D.R.6    Hultmark, D.7
  • 47
    • 0009482260 scopus 로고
    • Electrophoretic transfer of protein from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., Stahelin, T. and Gordon, J. (1979). Electrophoretic transfer of protein from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76, 4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Stahelin, T.2    Gordon, J.3
  • 48
    • 0026582795 scopus 로고
    • Molecular cloning, functional expression and tissue distribution of the cDNA encoding frog skeletal muscle calsequestrin
    • Treves, S., Vilsen, B., Chiozzi, P., Andersen, J. P. and Zorzato, F. (1992). Molecular cloning, functional expression and tissue distribution of the cDNA encoding frog skeletal muscle calsequestrin. Biochem. J. 283, 767-772.
    • (1992) Biochem. J. , vol.283 , pp. 767-772
    • Treves, S.1    Vilsen, B.2    Chiozzi, P.3    Andersen, J.P.4    Zorzato, F.5
  • 49
    • 0030774905 scopus 로고    scopus 로고
    • Functional properties of recombinant calpain I and of mutants lacking domains III and IV of the catalytic subunit
    • Vilei, E. M., Calderara, S., Anagli, J., Berardi, S., Hitomi, K., Maki, M. and Carafoli, E. (1997). Functional properties of recombinant calpain I and of mutants lacking domains III and IV of the catalytic subunit. J. Biol. Chem. 272, 25802-25808.
    • (1997) J. Biol. Chem. , vol.272 , pp. 25802-25808
    • Vilei, E.M.1    Calderara, S.2    Anagli, J.3    Berardi, S.4    Hitomi, K.5    Maki, M.6    Carafoli, E.7
  • 50
    • 0032797384 scopus 로고    scopus 로고
    • Sepsis stimulates release of myofilaments in skeletal muscle by a calcium-dependent mechanism
    • Williams, A. B., Decourten-Myers, G. M., Fischer, J. E., Luo, G. J., Sun, X. Y. and Hasselgren, P. O. (1999). Sepsis stimulates release of myofilaments in skeletal muscle by a calcium-dependent mechanism. FASEB J. 13, 1435-1443.
    • (1999) FASEB J. , vol.13 , pp. 1435-1443
    • Williams, A.B.1    Decourten-Myers, G.M.2    Fischer, J.E.3    Luo, G.J.4    Sun, X.Y.5    Hasselgren, P.O.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.