메뉴 건너뛰기




Volumn 275, Issue 3 44-3, 1998, Pages

Differences in contractile protein content and isoforms in phasic and tonic smooth muscles

Author keywords

Actin; Caldesmon; Calponin; Esophageal smooth muscle; Lower esophageal sphincter; Myosin; Opossum; Tropomyosin; Visceral smooth muscle

Indexed keywords

CONTRACTILE PROTEIN;

EID: 0031668167     PISSN: 03636143     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpcell.1998.275.3.c684     Document Type: Article
Times cited : (75)

References (48)
  • 1
    • 0001848811 scopus 로고    scopus 로고
    • Myosin structure and function
    • edited by M. Barany. San Diego, CA: Academic
    • Adelstein, R. S., and J. R. Sellers. Myosin structure and function. In: Biochemistry of Smooth Muscle Contraction, edited by M. Barany. San Diego, CA: Academic, 1996, p, 3-20.
    • (1996) Biochemistry of Smooth Muscle Contraction , pp. 3-20
    • Adelstein, R.S.1    Sellers, J.R.2
  • 2
    • 0027166908 scopus 로고
    • Tissue-specific and developmentally regulated alternative splicing of a visceral isoform of smooth muscle myosin heavy chain
    • Babij, P. Tissue-specific and developmentally regulated alternative splicing of a visceral isoform of smooth muscle myosin heavy chain. Nucleic Acids Res. 21: 1467-1471, 1993.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 1467-1471
    • Babij, P.1
  • 3
    • 0002447331 scopus 로고    scopus 로고
    • Myosin light chains
    • edited by M. Barany. San Diego, CA: Academic
    • Barany, M., and K. Barany. Myosin light chains. In: Biochemistry of Smooth Muscle Contraction, edited by M. Barany. San Diego, CA: Academic, 1996, p. 21-36.
    • (1996) Biochemistry of Smooth Muscle Contraction , pp. 21-36
    • Barany, M.1    Barany, K.2
  • 4
  • 5
    • 0027093717 scopus 로고
    • Actin mediated regulation of muscle contraction
    • Chalovich, J. M. Actin mediated regulation of muscle contraction. Pharmacol. Ther. 55: 95-148, 1992.
    • (1992) Pharmacol. Ther. , vol.55 , pp. 95-148
    • Chalovich, J.M.1
  • 6
    • 0017823252 scopus 로고
    • Differences in cellular contractile protein contents among porcine smooth muscles
    • Cohen, D. M., and R. A. Murphy. Differences in cellular contractile protein contents among porcine smooth muscles. Gen. Physiol. Biophys, 72: 369-380, 1978.
    • (1978) Gen. Physiol. Biophys , vol.72 , pp. 369-380
    • Cohen, D.M.1    Murphy, R.A.2
  • 7
    • 0031137872 scopus 로고    scopus 로고
    • 2-terminal-inserted myosin II heavy chain is expressed in smooth muscle of small muscular arteries
    • Cell Physiol. 41
    • 2-terminal-inserted myosin II heavy chain is expressed in smooth muscle of small muscular arteries. Am. J. Physiol. 272 (Cell Physiol. 41): C1532-C1542, 1997.
    • (1997) Am. J. Physiol. , vol.272
    • Disanto, M.E.1    Cox, R.H.2    Wang, Z.3    Chacko, S.4
  • 8
    • 0023664431 scopus 로고
    • Two smooth muscle myosin heavy chains in cultured aorta smooth muscle cells. a comparative study
    • Eddinger, T. J., and R. A. Murphy. Two smooth muscle myosin heavy chains in cultured aorta smooth muscle cells. A comparative study. J. Biol. Chem. 262: 7282-7288, 1987.
    • (1987) J. Biol. Chem. , vol.262 , pp. 7282-7288
    • Eddinger, T.J.1    Murphy, R.A.2
  • 9
    • 0021687082 scopus 로고
    • Actin and tropomyosin variants in smooth muscles
    • Fatigati, V., and R. A. Murphy. Actin and tropomyosin variants in smooth muscles. J. Biol. Chem. 259: 14383-14388, 1984.
    • (1984) J. Biol. Chem. , vol.259 , pp. 14383-14388
    • Fatigati, V.1    Murphy, R.A.2
  • 14
    • 0001068154 scopus 로고
    • Biochemistry of the contractile process in smooth muscle
    • edited by L. R. Johnson, New York: Raven
    • Hartshorne, D. J. Biochemistry of the contractile process in smooth muscle. In: Physiology of the Gastrointestinal Tract, edited by L. R. Johnson, New York: Raven, 1987, p. 423-482.
    • (1987) Physiology of the Gastrointestinal Tract , pp. 423-482
    • Hartshorne, D.J.1
  • 15
    • 0026771997 scopus 로고
    • Role of 17-kDa essential light chain isoforms of aorta smooth muscle myosin
    • Hasegawa, Y., and F. Morita. Role of 17-kDa essential light chain isoforms of aorta smooth muscle myosin. J. Biochem. (Tokyo) 111: 804-809, 1992.
    • (1992) J. Biochem. (Tokyo) , vol.111 , pp. 804-809
    • Hasegawa, Y.1    Morita, F.2
  • 16
    • 0023874625 scopus 로고
    • Two isoforms of 17-kDa essential light chain of aorta media smooth muscle myosin
    • Hasegawa, Y., H. Ueno, K. Horie, and F. Morita. Two isoforms of 17-kDa essential light chain of aorta media smooth muscle myosin. J. Biochem. (Tokyo) 103: 15-18, 1988.
    • (1988) J. Biochem. (Tokyo) , vol.103 , pp. 15-18
    • Hasegawa, Y.1    Ueno, H.2    Horie, K.3    Morita, F.4
  • 17
    • 0023756765 scopus 로고
    • Distribution of isoelectric variants of the 17,000-dalton myosin light chain in mammalian smooth muscle
    • Helper, D. J., J. A. Lash, and D. R. Hathway. Distribution of isoelectric variants of the 17,000-dalton myosin light chain in mammalian smooth muscle. J. Biol. Chem. 263: 15748-15753, 1988.
    • (1988) J. Biol. Chem. , vol.263 , pp. 15748-15753
    • Helper, D.J.1    Lash, J.A.2    Hathway, D.R.3
  • 18
    • 0027394195 scopus 로고
    • Correlations between myosin heavy chain isoforms and mechanical parameters in rat myometrium
    • Hewett, T. E., A. F. Martin, and R. J. Paul. Correlations between myosin heavy chain isoforms and mechanical parameters in rat myometrium. J. Physiol. (Lond.) 460: 351-364, 1993.
    • (1993) J. Physiol. (Lond.) , vol.460 , pp. 351-364
    • Hewett, T.E.1    Martin, A.F.2    Paul, R.J.3
  • 20
    • 0017819887 scopus 로고
    • Calcium sensitivity of contractile proteins from chicken gizzard muscle
    • Ikebe, M., T. Aiba, H. Onishi, and S. Watanabe. Calcium sensitivity of contractile proteins from chicken gizzard muscle. J. Biochem. (Tokyo) 83: 1643-1655, 1978.
    • (1978) J. Biochem. (Tokyo) , vol.83 , pp. 1643-1655
    • Ikebe, M.1    Aiba, T.2    Onishi, H.3    Watanabe, S.4
  • 22
    • 0023664431 scopus 로고
    • Characterization of myosin heavy chains in cultured aorta smooth muscle cells. a comparative study
    • Kawamoto, S., and R. S. Adelstein. Characterization of myosin heavy chains in cultured aorta smooth muscle cells. A comparative study. J. Biol. Chem. 262: 7282-7288, 1987.
    • (1987) J. Biol. Chem. , vol.262 , pp. 7282-7288
    • Kawamoto, S.1    Adelstein, R.S.2
  • 23
    • 0027258646 scopus 로고
    • An insert of seven amino acids confers functional differences between smooth muscle myosins from the intestines and vasculature
    • Kelley, C. A., M. Takahashi, J. H. Yu, and R. S. Adelstein. An insert of seven amino acids confers functional differences between smooth muscle myosins from the intestines and vasculature. J. Biol. Chem. 268: 12848-12854, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12848-12854
    • Kelley, C.A.1    Takahashi, M.2    Yu, J.H.3    Adelstein, R.S.4
  • 24
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685, 1970.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 25
    • 0025817957 scopus 로고
    • Correlation between isoform composition of the 17 kDa myosin light chain and maximal shortening velocity in smooth muscle
    • Malmqvist, U., and A. Arner. Correlation between isoform composition of the 17 kDa myosin light chain and maximal shortening velocity in smooth muscle. Eur. J. Biochem. 418: 523-530, 1991.
    • (1991) Eur. J. Biochem. , vol.418 , pp. 523-530
    • Malmqvist, U.1    Arner, A.2
  • 27
    • 0024370066 scopus 로고
    • Vertebrate smooth muscle myosin heavy chains (MHCs) exist as two isoforms with molecular masses of 204 and 200 kDa (MHC204 and MHC200) that are generated from single gene by alternative splicing of mRNA
    • Nagai, R., M. Kuro-o, P. Babij, and M. Periasamy. Vertebrate smooth muscle myosin heavy chains (MHCs) exist as two isoforms with molecular masses of 204 and 200 kDa (MHC204 and MHC200) that are generated from single gene by alternative splicing of mRNA. J. Biol. Chem. 264: 9734-9737, 1989.
    • (1989) J. Biol. Chem. , vol.264 , pp. 9734-9737
    • Nagai, R.1    Kuro-o, M.2    Babij, P.3    Periasamy, M.4
  • 28
    • 0025371590 scopus 로고
    • Do thin filaments of smooth muscle contain calponin? a new method for the preparation
    • Nishida, W., M. Abe, K. Takahashi, and K. Hiwada. Do thin filaments of smooth muscle contain calponin? A new method for the preparation. FEBS Lett. 268: 165-168, 1990.
    • (1990) FEBS Lett. , vol.268 , pp. 165-168
    • Nishida, W.1    Abe, M.2    Takahashi, K.3    Hiwada, K.4
  • 29
    • 0016711037 scopus 로고
    • High resolution two-dimentional electrophoresis of proteins
    • O'Farrell, P. H. High resolution two-dimentional electrophoresis of proteins. J. Biol. Chem. 250: 4007-4021, 1975.
    • (1975) J. Biol. Chem. , vol.250 , pp. 4007-4021
    • O'Farrell, P.H.1
  • 30
    • 0017848680 scopus 로고
    • Effects of tryptic digestion on the enzymatic activities of chicken gizzard myosin
    • Okamoto, T., and T. Sekine. Effects of tryptic digestion on the enzymatic activities of chicken gizzard myosin. J. Biochem. (Tokyo) 83: 1375-1379, 1978.
    • (1978) J. Biochem. (Tokyo) , vol.83 , pp. 1375-1379
    • Okamoto, T.1    Sekine, T.2
  • 31
    • 0014829125 scopus 로고
    • An electrophoretic study of the low-molecular-weight components of myosin
    • Perrie, W. T., and S. V. Perry. An electrophoretic study of the low-molecular-weight components of myosin. Biochem. J. 119: 31-38, 1970.
    • (1970) Biochem. J. , vol.119 , pp. 31-38
    • Perrie, W.T.1    Perry, S.V.2
  • 32
    • 0031031962 scopus 로고    scopus 로고
    • An insert in the motor domain determines the functional properties of expressed smooth muscle myosin isoforms
    • Rovner, A. S., Y. Freyzon, and K. M. Trybus. An insert in the motor domain determines the functional properties of expressed smooth muscle myosin isoforms. J. Muscle Res. Cell Motil. 18: 103-110, 1997.
    • (1997) J. Muscle Res. Cell Motil. , vol.18 , pp. 103-110
    • Rovner, A.S.1    Freyzon, Y.2    Trybus, K.M.3
  • 33
    • 0022521409 scopus 로고
    • Two different heavy chains are found in smooth muscle myosin
    • Cell Physiol. 19
    • Rovner, A. S., M. M. Thompson, and R. A. Murphy. Two different heavy chains are found in smooth muscle myosin. Am. J. Physiol. 250 (Cell Physiol. 19): C861-C870, 1986.
    • (1986) Am. J. Physiol. , vol.250
    • Rovner, A.S.1    Thompson, M.M.2    Murphy, R.A.3
  • 34
    • 0017852051 scopus 로고
    • Morphological evaluation of opossum lower esophageal sphincter
    • Seelig, L. L., and R. K. Goyal. Morphological evaluation of opossum lower esophageal sphincter. Gastroenterology 75: 51-58, 1978.
    • (1978) Gastroenterology , vol.75 , pp. 51-58
    • Seelig, L.L.1    Goyal, R.K.2
  • 35
    • 0023630568 scopus 로고
    • Atypical localization of myenteric neurons in the opossum lower esophageal sphincter
    • Sengupta, A., W. G. Paterson, and R. K. Goyal. Atypical localization of myenteric neurons in the opossum lower esophageal sphincter. Am. J. Anat. 180: 342-348, 1987.
    • (1987) Am. J. Anat. , vol.180 , pp. 342-348
    • Sengupta, A.1    Paterson, W.G.2    Goyal, R.K.3
  • 36
    • 0002393531 scopus 로고    scopus 로고
    • Tropomyosin
    • edited by M. Barany. San Diego, CA: Academic
    • Smille, L. B. Tropomyosin. In: Biochemistry of Smooth Muscle Contraction, edited by M. Barany. San Diego, CA: Academic, 1996, p. 63-75.
    • (1996) Biochemistry of Smooth Muscle Contraction , pp. 63-75
    • Smille, L.B.1
  • 37
    • 0014386880 scopus 로고
    • Vascular smooth muscle. I. Normal structure, pathology, biochemistry
    • Somlyo, A. P., and A. V. Somlyo. Vascular smooth muscle. I. Normal structure, pathology, biochemistry. Pharmacol. Rev. 20: 197-272, 1968.
    • (1968) Pharmacol. Rev. , vol.20 , pp. 197-272
    • Somlyo, A.P.1    Somlyo, A.V.2
  • 38
    • 0023690482 scopus 로고
    • Myosin composition and functional properties of smooth muscle from the uterus of pregnant and nonpregnant rats
    • Sparrow, M. P., A. M. Mohammed, A. Arner, P. Hellstrand, and J. C. Ruegg. Myosin composition and functional properties of smooth muscle from the uterus of pregnant and nonpregnant rats. Pflügers Arch. 412: 624-633, 1988.
    • (1988) Pflügers Arch. , vol.412 , pp. 624-633
    • Sparrow, M.P.1    Mohammed, A.M.2    Arner, A.3    Hellstrand, P.4    Ruegg, J.C.5
  • 39
    • 0027146195 scopus 로고
    • Interaction between calponin and smooth muscle myosin
    • Szymanski, P. T., and T. Tao. Interaction between calponin and smooth muscle myosin. FEBS Lett. 331: 256-259, 1993.
    • (1993) FEBS Lett. , vol.331 , pp. 256-259
    • Szymanski, P.T.1    Tao, T.2
  • 40
    • 0022930623 scopus 로고
    • Isolation and characterization of a 34000-dalton calmodulin and F-actin-binding protein from chicken gizzard smooth muscle
    • Takahashi, K., K. Hiwada, and T. Kokobu. Isolation and characterization of a 34000-dalton calmodulin and F-actin-binding protein from chicken gizzard smooth muscle. Biochem. Biophys. Res. Commun. 141: 20-26, 1986.
    • (1986) Biochem. Biophys. Res. Commun. , vol.141 , pp. 20-26
    • Takahashi, K.1    Hiwada, K.2    Kokobu, T.3
  • 41
    • 0027934341 scopus 로고
    • Regulation of expressed truncated smooth muscle myosins. Role of the essential light chain and tail length
    • Trybus, K. M. Regulation of expressed truncated smooth muscle myosins. Role of the essential light chain and tail length. J. Biol. Chem. 269: 20819-20822, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20819-20822
    • Trybus, K.M.1
  • 42
    • 0018553475 scopus 로고
    • The complete amino acid sequence of actins from bovine aorta, bovine heart, bovine fast skeletal muscle and rabbit slow skeletal muscle
    • Vandekerckhove, J., and K. Weber. The complete amino acid sequence of actins from bovine aorta, bovine heart, bovine fast skeletal muscle and rabbit slow skeletal muscle. Differentiation 14: 123-133, 1979.
    • (1979) Differentiation , vol.14 , pp. 123-133
    • Vandekerckhove, J.1    Weber, K.2
  • 43
    • 0020020860 scopus 로고
    • Preparation and fractionation of myosin light chains and exchange of the essential light chains
    • edited by D. W. Frederiksen and L. W. Cunningham. New York: Academic
    • Wagner, P. D. Preparation and fractionation of myosin light chains and exchange of the essential light chains. In: Methods in Enzymology, edited by D. W. Frederiksen and L. W. Cunningham. New York: Academic, 1982, p. 72-81.
    • (1982) Methods in Enzymology , pp. 72-81
    • Wagner, P.D.1
  • 44
    • 0022098807 scopus 로고
    • Myosin phosphorylation and contraction of feline esophageal smooth muscle
    • Cell Physiol. 18
    • Weisbrodt, N. W., and R. A. Murphy. Myosin phosphorylation and contraction of feline esophageal smooth muscle. Am. J. Physiol. 249 (Cell Physiol. 18): C9-C14, 1985.
    • (1985) Am. J. Physiol. , vol.249
    • Weisbrodt, N.W.1    Murphy, R.A.2
  • 45
    • 0014216425 scopus 로고
    • Free adenosine diphosphate as an intermediary in the phosphorylation by creatine phosphate of adenosine bound to actin
    • West, J. J., B. Nagy, and J. Gergely. Free adenosine diphosphate as an intermediary in the phosphorylation by creatine phosphate of adenosine bound to actin. J. Biol. Chem. 242: 1140-1145, 1967.
    • (1967) J. Biol. Chem. , vol.242 , pp. 1140-1145
    • West, J.J.1    Nagy, B.2    Gergely, J.3
  • 46
    • 0027223294 scopus 로고
    • Identification of a novel smooth muscle myosin heavy chain cDNA: Isoform diversity in the SI head region
    • Cell Physiol. 33
    • White, S. A., A., F. Martin, and M. Periasamy. Identification of a novel smooth muscle myosin heavy chain cDNA: isoform diversity in the SI head region. Am. J. Physiol. 264 (Cell Physiol. 33): C1252-C1258, 1993.
    • (1993) Am. J. Physiol. , vol.264
    • White, S.A.1    Martin, A.F.2    Periasamy, M.3
  • 47
    • 0025348420 scopus 로고
    • Smooth muscle calponin. Inhibition of actomyosin MgATPase and regulation by phosphorylation
    • Winder, S. J., and M. P. Walsh. Smooth muscle calponin. Inhibition of actomyosin MgATPase and regulation by phosphorylation. J. Biol. Chem. 265: 10148-10155, 1990.
    • (1990) J. Biol. Chem. , vol.265 , pp. 10148-10155
    • Winder, S.J.1    Walsh, M.P.2
  • 48
    • 0027749388 scopus 로고
    • Calponin: Thin filament-linked regulation of smooth muscle contraction
    • Winder, S. J., and M. P. Walsh. Calponin: thin filament-linked regulation of smooth muscle contraction. Cell. Signal. 5: 677-686, 1993.
    • (1993) Cell. Signal. , vol.5 , pp. 677-686
    • Winder, S.J.1    Walsh, M.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.