메뉴 건너뛰기




Volumn 15, Issue 2, 2004, Pages 145-157

Cloning of the calpain regulatory subunit cDNA from fish reveals a divergent domain-V

Author keywords

Calpain; CDNA; Cpns; Muscle library; Phylogenetic tree; Rainbow trout; Regulatory subunit

Indexed keywords

CALPAIN; CDNA; CPNS; MUSCLE LIBRARY; PHYLOGENETIC TREES; RAINBOW TROUT; REGULATORY SUBUNITS;

EID: 9944265039     PISSN: 10495398     EISSN: None     Source Type: Journal    
DOI: 10.1081/LABT-200036706     Document Type: Article
Times cited : (13)

References (31)
  • 2
    • 0033573028 scopus 로고    scopus 로고
    • 2+-dependent protease activity and a novel mode of enzyme activation
    • 2+-dependent protease activity and a novel mode of enzyme activation. EMBO J 1999; 18(24):6880-6889.
    • (1999) EMBO J , vol.18 , Issue.24 , pp. 6880-6889
    • Hosfield, C.M.1    Elce, J.S.2    Davies, P.L.3    Jia, Z.4
  • 4
    • 0025831476 scopus 로고
    • Calcium activated neutral protease (calpain) system: Structure-function and regulation
    • Croall DE, DeMartino GN. Calcium activated neutral protease (calpain) system: structure-function and regulation. Physiol Rev 1991; 71(3):813-847.
    • (1991) Physiol Rev , vol.71 , Issue.3 , pp. 813-847
    • Croall, D.E.1    DeMartino, G.N.2
  • 5
    • 0029922373 scopus 로고    scopus 로고
    • Investigation of the interaction of calpain with phospholipids
    • Arthur JSC, Crawford C. Investigation of the interaction of calpain with phospholipids. Biochim Biophys Acta 1996; 1293(2):201-206.
    • (1996) Biochim Biophys Acta , vol.1293 , Issue.2 , pp. 201-206
    • Arthur, J.S.C.1    Crawford, C.2
  • 6
    • 0036436859 scopus 로고    scopus 로고
    • Domain V of m-calpain shows the potential to form an oblique-orientated alpha-helix, which may modulate the enzyme's activity via interactions with anionic lipid
    • Brandenburg K, Harris F, Dennison S, Seydel U, Phoenix D. Domain V of m-calpain shows the potential to form an oblique-orientated alpha-helix, which may modulate the enzyme's activity via interactions with anionic lipid. Eur J Biochem 2002; 269(22):5414-5422.
    • (2002) Eur J Biochem , vol.269 , Issue.22 , pp. 5414-5422
    • Brandenburg, K.1    Harris, F.2    Dennison, S.3    Seydel, U.4    Phoenix, D.5
  • 7
    • 0034116930 scopus 로고    scopus 로고
    • Disruption of the murine calpain small subunit gene, capn4: Calpain is essential for embryonic development but not for cell growth and division
    • Arthur JSC, Elce JS, Hegadorn C, Williams K, Green PA. Disruption of the murine calpain small subunit gene, capn4: calpain is essential for embryonic development but not for cell growth and division. Mol Cell Biol 2000; 20(12):4474-4481.
    • (2000) Mol Cell Biol , vol.20 , Issue.12 , pp. 4474-4481
    • Arthur, J.S.C.1    Elce, J.S.2    Hegadorn, C.3    Williams, K.4    Green, P.A.5
  • 8
    • 0032514704 scopus 로고    scopus 로고
    • Role of calpain in skeletal-muscle protein degradation
    • Huang J, Forsberg NE. Role of calpain in skeletal-muscle protein degradation. Proc Nat Acad Sci 1998; 95(21):12100-12105.
    • (1998) Proc Nat Acad Sci , vol.95 , Issue.21 , pp. 12100-12105
    • Huang, J.1    Forsberg, N.E.2
  • 9
    • 0037397906 scopus 로고    scopus 로고
    • Roles of mu-calpain in cultured L8 muscle cells: Application of a skeletal muscle-specific gene expression system
    • Xiao YY, Wang MC, Purintrapiban J, Forsberg NE. Roles of mu-calpain in cultured L8 muscle cells: application of a skeletal muscle-specific gene expression system. Comp Biochem Physiol 2003; 134(4):439-450.
    • (2003) Comp Biochem Physiol , vol.134 , Issue.4 , pp. 439-450
    • Xiao, Y.Y.1    Wang, M.C.2    Purintrapiban, J.3    Forsberg, N.E.4
  • 10
    • 0026591107 scopus 로고
    • 2+-dependent proteases in post-mortem proteolysis and meat tenderness
    • 2+-dependent proteases in post-mortem proteolysis and meat tenderness. Biochimie 1992; 74(3):239-245.
    • (1992) Biochimie , vol.74 , Issue.3 , pp. 239-245
    • Koohmaraie, M.1
  • 11
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate phenol-chloroform extraction
    • Chomczynski P, Saccihi N. Single-step method of RNA isolation by acid guanidinium thiocyanate phenol-chloroform extraction. Anal Biochem 1987; 162(1):156-159.
    • (1987) Anal Biochem , vol.162 , Issue.1 , pp. 156-159
    • Chomczynski, P.1    Saccihi, N.2
  • 12
    • 0035199767 scopus 로고    scopus 로고
    • Temporal expression of growth factor genes during myogenesis of satellite cells derived from the biceps femoris and pectoralis major muscles of the chicken
    • Kocamis H, Mcfarland D, Killefer J. Temporal expression of growth factor genes during myogenesis of satellite cells derived from the biceps femoris and pectoralis major muscles of the chicken. J Cell Physiol 2001; 186(1):146-152.
    • (2001) J Cell Physiol , vol.186 , Issue.1 , pp. 146-152
    • Kocamis, H.1    Mcfarland, D.2    Killefer, J.3
  • 13
    • 0000778479 scopus 로고    scopus 로고
    • Extraction, purification and analysis of mRNA from eukaryotic cells
    • 3rd ed. Cold Spring Harbor, New York: Cold Spring Harbor Laboratory Press
    • Sambrook J, Russell D. Extraction, purification and analysis of mRNA from eukaryotic cells. Molecular Cloning a Laboratory Manual. Vol. 1. 3rd ed. Cold Spring Harbor, New York: Cold Spring Harbor Laboratory Press, 2001:7.1-7.88.
    • (2001) Molecular Cloning A Laboratory Manual. , vol.1
    • Sambrook, J.1    Russell, D.2
  • 14
    • 0031452173 scopus 로고    scopus 로고
    • Structure and physiological function of calpains
    • Sorimach H, Ishiura S, Suzuki K. Structure and physiological function of calpains. Biochem J 1997; 328(Pt 3):721-732.
    • (1997) Biochem J , vol.328 , Issue.PART 3 , pp. 721-732
    • Sorimach, H.1    Ishiura, S.2    Suzuki, K.3
  • 15
    • 0026911137 scopus 로고
    • Is calpain activity regulated by membranes and autolysis or by calcium and calpastatin?
    • Goll DE, Thompson VF, Taylor RG, Zalewska T. Is calpain activity regulated by membranes and autolysis or by calcium and calpastatin? BioEssays 1992; 14(8):549-556.
    • (1992) BioEssays , vol.14 , Issue.8 , pp. 549-556
    • Goll, D.E.1    Thompson, V.F.2    Taylor, R.G.3    Zalewska, T.4
  • 16
    • 0022783480 scopus 로고
    • Limited autolysis of calcium-activated neutral protease reduction of the calcium requirement is due to the amino processing of the large subunit
    • Imajoh S, Kawasaki H, Suzuki K. Limited autolysis of calcium-activated neutral protease reduction of the calcium requirement is due to the amino processing of the large subunit. J Biochem (Tokyo) 1986; 100(3):633-642.
    • (1986) J Biochem (Tokyo) , vol.100 , Issue.3 , pp. 633-642
    • Imajoh, S.1    Kawasaki, H.2    Suzuki, K.3
  • 17
    • 13844276995 scopus 로고    scopus 로고
    • Isolation and in vitro characterization of the calpains from rainbow trout (Oncorhynchus mykiss) muscle and their role in texture development
    • In press
    • Salem M, Kenney PB, Killefer J, Nath J. Isolation and in vitro characterization of the calpains from rainbow trout (Oncorhynchus mykiss) muscle and their role in texture development. J Muscle Foods, 2004. In press.
    • (2004) J Muscle Foods
    • Salem, M.1    Kenney, P.B.2    Killefer, J.3    Nath, J.4
  • 19
    • 85008119839 scopus 로고
    • Purification and some properties of a calpain from carp muscle
    • Taneda T, Watanabe T, Seki N. Purification and some properties of a calpain from carp muscle. Bull Jpn Soc Sci Fish 1983; 49(2):219-228.
    • (1983) Bull Jpn Soc Sci Fish , vol.49 , Issue.2 , pp. 219-228
    • Taneda, T.1    Watanabe, T.2    Seki, N.3
  • 20
    • 0024540109 scopus 로고
    • Comparison of calpain I and calpain II from carp muscle
    • Toyohara H, Makinodan Y. Comparison of calpain I and calpain II from carp muscle. Comp Biochem Physiol 1989; 92(3):577-581.
    • (1989) Comp Biochem Physiol , vol.92 , Issue.3 , pp. 577-581
    • Toyohara, H.1    Makinodan, Y.2
  • 21
    • 0032557553 scopus 로고    scopus 로고
    • Molecular and functional properties of a calpain activator protein specific for mu-isoforms
    • Melloni E, Michetti M, Salamino F, Pontremoli S. Molecular and functional properties of a calpain activator protein specific for mu-isoforms. J Biol Chem 1998;273(21):12827-12831.
    • (1998) J Biol Chem , vol.273 , Issue.21 , pp. 12827-12831
    • Melloni, E.1    Michetti, M.2    Salamino, F.3    Pontremoli, S.4
  • 23
    • 0025096669 scopus 로고
    • Investigation of the structural basis of the interaction of calpain II with phospholipid and with carbohydrate
    • Crawford C, Brown N, Willis A. Investigation of the structural basis of the interaction of calpain II with phospholipid and with carbohydrate. Biochem J 1990; 265(2):575-579.
    • (1990) Biochem J , vol.265 , Issue.2 , pp. 575-579
    • Crawford, C.1    Brown, N.2    Willis, A.3
  • 25
    • 0028171412 scopus 로고
    • 2+-activated neutral protease is active in the erythrocyte membrane in its nonautolyzed 80-kDa form
    • 2+-activated neutral protease is active in the erythrocyte membrane in its nonautolyzed 80-kDa form. J Biol Chem 1994; 269(45):27992-27998.
    • (1994) J Biol Chem , vol.269 , Issue.45 , pp. 27992-27998
    • Molinari, M.1    Anagli, J.2    Carafoli, E.3
  • 26
    • 0030892186 scopus 로고    scopus 로고
    • A cytosolic proteinase active at the membranes
    • Molinari M, Carafoli E. A cytosolic proteinase active at the membranes. J Membrane Biol 1997; 156(1):1-8.
    • (1997) J Membrane Biol , vol.156 , Issue.1 , pp. 1-8
    • Molinari, M.1    Carafoli, E.2
  • 27
    • 0022612971 scopus 로고
    • The amino-terminal hydrophobic region of the small subunit of calcium-activated neutral protease (CANP) is essential for its activation by phosphatidylinositol
    • Imajoh S, Kawasaki H, Suzuki K. The amino-terminal hydrophobic region of the small subunit of calcium-activated neutral protease (CANP) is essential for its activation by phosphatidylinositol. J Biochem 1986; 99(4):1281-1284.
    • (1986) J Biochem , vol.99 , Issue.4 , pp. 1281-1284
    • Imajoh, S.1    Kawasaki, H.2    Suzuki, K.3
  • 29
    • 0030921118 scopus 로고    scopus 로고
    • EF-hands embrace
    • Kretsinger RH. EF-hands embrace. Nat Struct Biol 1997; 4(7):514-515.
    • (1997) Nat Struct Biol , vol.4 , Issue.7 , pp. 514-515
    • Kretsinger, R.H.1
  • 30
    • 0032783288 scopus 로고    scopus 로고
    • The evolution of the calpain family as reflected in paralogous chromosome regions
    • Jékely G, Friedrich P. The evolution of the calpain family as reflected in paralogous chromosome regions. J Moli Evol 1999; 49(2):272-281.
    • (1999) J Moli Evol , vol.49 , Issue.2 , pp. 272-281
    • Jékely, G.1    Friedrich, P.2
  • 31
    • 0030023247 scopus 로고    scopus 로고
    • Determining divergence times of the major kingdoms of living organisms with a protein clock
    • Doolittle RF, Feng DF, Tsang S, Cho G, Little E. Determining divergence times of the major kingdoms of living organisms with a protein clock. Science 1996; 271(5248):470-477.
    • (1996) Science , vol.271 , Issue.5248 , pp. 470-477
    • Doolittle, R.F.1    Feng, D.F.2    Tsang, S.3    Cho, G.4    Little, E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.