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Volumn 19, Issue 4, 2004, Pages 286-289

Effects of caldesmon, calponin, and tropomyosin on the Mg2+ -ATPase activities of smooth muscle myosin

Author keywords

Actin binding proteins; Ca 2+ independent phosphorylation; Ca2+ dependent phosphorylation; Myosin Mg2+ ATPase activity

Indexed keywords

ACTIN BINDING PROTEIN; ADENOSINE TRIPHOSPHATASE (MAGNESIUM); CALCIUM; CALDESMON; CALPONIN; MYOSIN; MYOSIN LIGHT CHAIN KINASE; TROPOMYOSIN;

EID: 12344315306     PISSN: 10019294     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (5)

References (22)
  • 2
    • 0029948178 scopus 로고    scopus 로고
    • Effects of calponin on force generation by single smooth muscle cells
    • Horowitz A, Clement-chomienne O, Walsh MP, et al. Effects of calponin on force generation by single smooth muscle cells. Am J Physiol 1996;270(5pt2):H1858-63.
    • (1996) Am J Physiol , vol.270 , Issue.5 PART 2
    • Horowitz, A.1    Clement-Chomienne, O.2    Walsh, M.P.3
  • 3
    • 0032555992 scopus 로고    scopus 로고
    • Caldesmon inhibits active crossbridgs in unstimulated vascular smooth muscle: An antisense oligodeoxynucleotide approach
    • Earley JJ, Su X, Moreland RS. Caldesmon inhibits active crossbridgs in unstimulated vascular smooth muscle: an antisense oligodeoxynucleotide approach. Circ Res 1998;83:661-7.
    • (1998) Circ Res , vol.83 , pp. 661-667
    • Earley, J.J.1    Su, X.2    Moreland, R.S.3
  • 4
    • 0032836236 scopus 로고    scopus 로고
    • Thin-filament linked regulation of smooth muscle myosin
    • Haeberle JR. Thin-filament linked regulation of smooth muscle myosin. J Muscle Res Cell Motil 1999;20:347-9.
    • (1999) J Muscle Res Cell Motil , vol.20 , pp. 347-349
    • Haeberle, J.R.1
  • 5
    • 0033798958 scopus 로고    scopus 로고
    • The maximal velocity of vascular smooth muscle shortening is independent of the expression of calponin
    • Facemire C, Brozovich FV, Jin JP. The maximal velocity of vascular smooth muscle shortening is independent of the expression of calponin. J Muscle Res Cell Motil 2000;21:367-73.
    • (2000) J Muscle Res Cell Motil , vol.21 , pp. 367-373
    • Facemire, C.1    Brozovich, F.V.2    Jin, J.P.3
  • 6
    • 0027193675 scopus 로고
    • Stimulatory effect of calpponin on myosin ATPase activity
    • Lin Y, Ye LH, Ishikawa R, et al. Stimulatory effect of calpponin on myosin ATPase activity. J Biochem 1993;113:643-5.
    • (1993) J Biochem , vol.113 , pp. 643-645
    • Lin, Y.1    Ye, L.H.2    Ishikawa, R.3
  • 7
    • 0027272489 scopus 로고
    • Role of myosin in the stimulatory effect of caldesmon on the interaction between actin, myosin and ATP
    • Tokyo
    • Lin Y, Ish R, Kohama K. Role of myosin in the stimulatory effect of caldesmon on the interaction between actin, myosin and ATP. J Biochem (Tokyo) 1993;114:279-83.
    • (1993) J Biochem , vol.114 , pp. 279-283
    • Lin, Y.1    Ish, R.2    Kohama, K.3
  • 8
    • 12344336291 scopus 로고
    • The bi-directional regulation mechanism in the modulation of smooth muscle contraction
    • Beijing: China Science and Technology Publishing House
    • Lin Y. The bi-directional regulation mechanism in the modulation of smooth muscle contraction. The book of the First Conference of the New Theory and New Opinion on Life Science. Beijing: China Science and Technology Publishing House 1993.p.98-102.
    • (1993) The Book of the First Conference of the New Theory and New Opinion on Life Science , pp. 98-102
    • Lin, Y.1
  • 9
    • 0032575646 scopus 로고    scopus 로고
    • N-terminal myosin-binding fragment of talin
    • Lin Y, Kohama K. N-terminal myosin-binding fragment of talin. Biochem Biophys Res Comm 1998;249:656-9.
    • (1998) Biochem Biophys Res Comm , vol.249 , pp. 656-659
    • Lin, Y.1    Kohama, K.2
  • 10
    • 0347982646 scopus 로고    scopus 로고
    • Bi-directional regulation of filamin on the ATPase activity of smooth muscle myosin
    • Lin Y, Sun HJ, Dai SF, et al. Bi-directional regulation of filamin on the ATPase activity of smooth muscle myosin. Chin Med Sci J 2000;15:162-4.
    • (2000) Chin Med Sci J , vol.15 , pp. 162-164
    • Lin, Y.1    Sun, H.J.2    Dai, S.F.3
  • 11
    • 0025900837 scopus 로고
    • Caldesmon, a novel regulatory protein in smooth muscle and nonmuscle actomyosin systems
    • Sobue K, Sellers JR. Caldesmon, a novel regulatory protein in smooth muscle and nonmuscle actomyosin systems. J Biol Chem 1991;266:12115-8.
    • (1991) J Biol Chem , vol.266 , pp. 12115-12118
    • Sobue, K.1    Sellers, J.R.2
  • 12
    • 0025879757 scopus 로고
    • Molecular cloning and sequence analysis of smooth muscle calponin
    • Takahashi K, Nadal-Ginard B. Molecular cloning and sequence analysis of smooth muscle calponin. J Biol Chem 1991;266:13284-8.
    • (1991) J Biol Chem , vol.266 , pp. 13284-13288
    • Takahashi, K.1    Nadal-Ginard, B.2
  • 13
    • 0019423570 scopus 로고
    • Effects of phosphorylation, calcium ion, and tropomyosin on actin-activated adenosine 5′-triphosphatase activity of mammalian smooth muscle myosin
    • Samuel C. Effects of phosphorylation, calcium ion, and tropomyosin on actin-activated adenosine 5′-triphosphatase activity of mammalian smooth muscle myosin. Biochemistry 1981;20:702-7.
    • (1981) Biochemistry , vol.20 , pp. 702-707
    • Samuel, C.1
  • 14
    • 0347982647 scopus 로고    scopus 로고
    • 2+-independent phosphorylation of smooth muscle myosin by myosin light chain kinase
    • 2+-independent phosphorylation of smooth muscle myosin by myosin light chain kinase. Sci Technol Engineer 2002;2:37-9.
    • (2002) Sci Technol Engineer , vol.2 , pp. 37-39
    • Lin, Y.1    Tang, Z.Y.2    Chen, H.3
  • 15
    • 0347594332 scopus 로고    scopus 로고
    • 2+-calmodulin independent phosphorylation of myosin light chains by a fragment from MLCK
    • 2+-calmodulin independent phosphorylation of myosin light chains by a fragment from MLCK. Acta Biochim Biophys Sin 2003;35:793-800.
    • (2003) Acta Biochim Biophys Sin , vol.35 , pp. 793-800
    • Yang, J.X.1    Wang, X.M.2    Tang, Z.Y.3
  • 16
    • 0026634314 scopus 로고
    • Regulation of contraction and relaxation in arterial smooth muscle
    • Rembold CM. Regulation of contraction and relaxation in arterial smooth muscle. Hypertension 1992;20:129-37.
    • (1992) Hypertension , vol.20 , pp. 129-137
    • Rembold, C.M.1
  • 17
    • 0028124493 scopus 로고
    • Calcium and smooth muscle contraction
    • Jiang H, Stephens NL. Calcium and smooth muscle contraction. Mol Cell Biochem 1994;135:1-9.
    • (1994) Mol Cell Biochem , vol.135 , pp. 1-9
    • Jiang, H.1    Stephens, N.L.2
  • 18
    • 0032436268 scopus 로고    scopus 로고
    • Myosin light chain kinase: Functional domains and structural motifs
    • Stull JT, Lin PJ, Krueger JK, et al. Myosin light chain kinase: functional domains and structural motifs. Acta Physiol Scand 1998;164:471-82.
    • (1998) Acta Physiol Scand , vol.164 , pp. 471-482
    • Stull, J.T.1    Lin, P.J.2    Krueger, J.K.3
  • 21
    • 0028335358 scopus 로고
    • Calponin decreases the rate of cross-bridge cycling and increases maximum force production by smooth muscle myosin in and in vitro motility assay
    • Haeberle JR. Calponin decreases the rate of cross-bridge cycling and increases maximum force production by smooth muscle myosin in and in vitro motility assay. J Biol Chem 1994;269:12424-31.
    • (1994) J Biol Chem , vol.269 , pp. 12424-12431
    • Haeberle, J.R.1
  • 22
    • 0034595986 scopus 로고    scopus 로고
    • Phosphorylation of smooth muscle myosin heads regulates the head-induced movement of tropomyosin
    • Graceffa P. Phosphorylation of smooth muscle myosin heads regulates the head-induced movement of tropomyosin. J Biol Chem 2000;275:17143-8.
    • (2000) J Biol Chem , vol.275 , pp. 17143-17148
    • Graceffa, P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.