[논문]Analysis of Myosin Light and Heavy Chain Types in Single Human Skeletal Muscle Fibers

BILLETER, Rudolf; HEIZMANN, Claus W.; HOWALD, Hans; JENNY, Eduard

doi:10.1111/j.1432-1033.1981.tb05347.x

Analysis of Myosin Light and Heavy Chain Types in Single Human Skeletal Muscle Fibers

European journal of biochemistry, v.116 no.2, 1981년, pp.389 - 395

BILLETER, Rudolf , HEIZMANN, Claus W. , HOWALD, Hans , JENNY, Eduard

Abstract ▼ AI-Helper

In this study, myosin types in human skeletal muscle fibers were investigated with electrophoretic techniques. Single fibers were dissected out of lyophilized surgical biopsies and typed by staining for myofibrillar ATPase after preincubation in acid or alkaline buffers. After 14C-labelling of the fiber proteins in vitro by reductive methylation, the myosin light chain pattern was analysed on two-dimensional gels and the myosin heavy chains were investigated by one-dimensional peptide mapping. Surprisingly, human type I fibers, which contained only the slow heavy chain, were found to contain variable amounts of fast myosin light chains in addition to the two slow light chains LC1s and LC2s. The majority of the type I fibers in normal human muscle showed the pattern LC1s, LC2s and LC1f. Further evidence for the existence in human muscle of a hybrid myosin composed of a slow heavy chain with fast and slow light chains comes from the analysis of purified human myosin in the native state by pyrophosphate gel electrophoresis. With this method, a single band corresponding to slow myosin was obtained; this slow myosin had the light chain composition LC1s, LC2s and LC1f. Type IIA and IIB fibers, on the other hand, revealed identical light chain patterns consisting of only the fast light chains LC1f, LC2f and LC3f but were found to have different myosin havy chains. On the basis of the results presented, we suggest that the histochemical ATPase normally used for fibre typing is determined by the myosin heavy chain type (and not by the light chains). Thus, in normal human muscle a number of 'hybrid' myosins were found to occur, namely two extreme forms of fast myosins which have the same light chains but different heavy chains (IIA and IIB) and a continuum of slow forms consisting of the same heavy chain and slow light chains with a variable fast light chain composition. This is consistent with the different physiological roles these fibers are thought to have in muscle contraction.

참고문헌 (49)

1. A. G. Weeds, and D. Pette (1980 ) inPlasticity of Muscle () pp.55 -68 . De Gruyter, Berlin and New York.
Arch. Neurol. Brooke M. H. 369 23 1970 10.1001/archneur.1970.00480280083010

상세보기
Ann. N. Y. Acad. Sci. Brooke M. H. 121 10.1111/j.1749-6632.1974.tb20506.x 228

상세보기
Johnson, M.A., Polgar, J., Weightman, D., Appleton, D.. Data on the distribution of fibre types in thirty-six human muscles - An autopsy study. Journal of the neurological sciences, vol.18, no.1, 111-129.

상세보기
Histochemistry Billeter R. 249 65 1980 10.1007/BF00493174

상세보기
Biochim. Biophys. Acta Bailin G. 312 93 1976
J. Neurol. Sci. Sreter F. A. 99 27 1976 10.1016/0022-510X(76)90238-0

상세보기
Muscle & Nerve Dalla-Libera L. 280 1 1978 10.1002/mus.880010404

상세보기
Pette, D., Henriksson, J., Emmerich, M.. Myofibrillar protein patterns of single fibres from human muscle. FEBS letters, vol.103, no.1, 152-155.

상세보기
Acta Biochem. Biophys. Acad. Sci. Hung. Vandor E. 147 14 1979
11. M. Fardeau, J. Godet-Guillain, F. M. S. Tome, S. Carson, R. G. Whalen, A. J. Agnajo, and G. Karpati (1978 ) inCurrent Topics in Nerve and Muscle Research () pp.164 -177 , Excerpta Medica, Amsterdam, Oxford.
clin. Chem. Giometti C. S. 1152 26 1980 10.1093/clinchem/26.8.1152

상세보기
Eur. J. Cell Biol. Volpe P. 318 22 1980
A Flexible System of Enzymatic Analysis Lowry O. H. 1973
Acta Physiol. Scand. Essen B. 153 95 1975 10.1111/j.1748-1716.1975.tb10038.x

상세보기
Histochemistry Spamer C. 201 52 1977 10.1007/BF00495857

상세보기
J. Biol. Chem. Jentoft N. 4359 154 1979 10.1016/S0021-9258(17)30016-9

상세보기
J. Biol. Chem. O'Farrell P. H. 4007 250 1975 10.1016/S0021-9258(19)41496-8

상세보기
Eur. J. Biochem. Bonner W. M. 83 46 1974 10.1111/j.1432-1033.1974.tb03599.x

상세보기
Eur. J. Biochem. Laskey R. A. 335 56 1975 10.1111/j.1432-1033.1975.tb02238.x

상세보기
J. Biol. Chem. Cleveland D. W. 1102 252 1977 10.1016/S0021-9258(19)75212-0

상세보기
d'Albis, A., Pantaloni, C., Bechet, J.-J.. Structural relationship of myosin isoenzymes - Proteolytic digestion patterns of heavy chain components from fast muscles, and comparison with other muscle types. FEBS letters, vol.106, no.1, 81-84.

상세보기
Proc. Natl Acad. Sci. USA Rushbrook J. I. 4331 76 1979 10.1073/pnas.76.9.4331

상세보기
Nature (Lond.) Laemmli U. K. 680 227 1970 10.1038/227680a0

상세보기
Hoh, J.F.Y.. Light chain distribution of chicken skeletal muscle myosin isoenzymes. FEBS letters, vol.90, no.2, 297-300.

상세보기
Biochemistry Hoh J. F. Y. 742 14 1975 10.1021/bi00675a015

상세보기
Nature (Lond.) Hoh J. F. Y. 321 280 1979 10.1038/280321a0

상세보기
J. Cell Biol. Kundrat E. 340 48 1971 10.1083/jcb.48.2.340

상세보기
Hoppe-Serler's Z. Physiol. Chem. Schaub M. C. 325 365 1975 10.1515/bchm2.1975.356.1.325

상세보기
FEBS Lett. Pinset-Harstrom I. 227 34 1973 10.1016/0014-5793(73)80799-9

상세보기
Biochem. J. Means G. E. 2192 7 1968 10.1021/bi00846a023

상세보기
Anal. Biochem. Kuhn O. 274 105 1980 10.1016/0003-2697(80)90457-1

상세보기
Eur. J. Biochem. Farrel P. J. 517 89 1978 10.1111/j.1432-1033.1978.tb12556.x

상세보기
Anal. Biochem. Anderson N. L. 312 93 1979 10.1016/S0003-2697(79)80157-8

상세보기
Trends Biol. Sci. Garrels J. I. 281 5 1980 10.1016/0968-0004(80)90158-9

상세보기
Biochem. J. Frearson N. 99 151 1975 10.1042/bj1510099

상세보기
Muscle & Nerve Pette D. 264 2 1980
Eur. J. Biochem. D'Albis A. 261 99 1979 10.1111/j.1432-1033.1979.tb13253.x

상세보기
Histochemistry Pette D. 97 54 1977 10.1007/BF00489668

상세보기
Biochimie (Paris) Brevet A. 459 60 1978 10.1016/S0300-9084(78)80860-8

상세보기
J. Cell Biol. Gauthier G. 760 74 1977 10.1083/jcb.74.3.760

상세보기
J. Mol. Biol. Starr R. 17 81 1973 10.1016/0022-2836(73)90244-1

상세보기
Kugelberg, E.. Adaptive transformation of rat soleus motor units during growth - Histochemistry and contraction speed. Journal of the neurological sciences, vol.27, no.3, 269-289.

상세보기
Acta Physiol. Scand. Jansson E. 235 104 1978 10.1111/j.1748-1716.1978.tb06272.x

상세보기
45. S. Salmons, and D. Pette (1980 ) inPlasticity of Muscle () pp.387 -399 . De Gruyter, Berlin and New York.
Acta Physiol. Scand. Andersen P. 123 99 1977 10.1111/j.1748-1716.1977.tb10361.x

상세보기
J. Histochem. Cytochem. Spurway N. C. 1980
Bárány, Michael. ATPase Activity of Myosin Correlated with Speed of Muscle Shortening. The Journal of general physiology, vol.50, no.6, 197-218.

상세보기
J. Physiol. (Lond.) Garnett R. A. F. 33 287 1978 10.1113/jphysiol.1979.sp012643

상세보기

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Analysis of Myosin Light and Heavy Chain Types in Single Human Skeletal Muscle Fibers

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참고문헌 (49)

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