Summary
Combined histochemical and biochemical analyses were performed on single fibers of rabbit soleus muscle. Histochemically, four fiber types (I, IC, IIC, IIA) were defined. Of these, types I and IIA were separate, histochemically homogeneous groups. A heterogeneous C fiber population exhibited a continuum of staining intensities between types I and IIA. Microelectrophoretic analyses of specific, histochemically defined fibers revealed that type I fibers contained exclusively HCI, whereas type IIA fibers contained only HCIIa. The C fibers were characterized by the coexistence of both heavy chains in varying ratios, type HC with a predominance of HCI and type IIC with a predominance of HCIIa. A direct correlation existed between the myosin heavy chain composition and the histochemical mATPase staining and was especially evident in the C fiber population with its variable HCI/HCIIa ratio. This correlation did not apply to the myosin light chain complement.
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References
Arndt T, Pepe FA (1975) Antigenic specificity of red and white muscle myosin. J Histochem Cytochem 23:159–168
Billeter R, Weber H, Lutz H, Howald H, Eppenberger HM, Jenny E (1980) Myosin types in human skeletal muscle fibers. Histochemistry 65:249–259
Billeter R, Heizmann CW, Howald H, Jenny E (1981) Analysis of myosin light and heavy chain types in single human skeletal muscle fibers. Eur J Biochem 116:389–395
Brooke MH, Kaiser KK (1970) Three “myosin adenosine triphosphatase” systems: the nature of their pH lability and sulfhydryl dependence. J Histochem Cytochem 18:670–672
Carraro U, Catani C (1983) A sensitive SDS-PAGE method separating myosin heavy chain isoforms of rat skeletal muscles reveals the heterogeneous nature of the embryonic myosin. Biochem Biophys Res Commun 116:793–802
Dalla Libera L, Sartore S, Pierobon-Bormioli S, Schiaffino S (1980) Fast-white and fast-red isomyosins in guinea pig muscles Biochem Biophys Res Commun 96:1662–1670
Gauthier GF, Lowey S (1977) Polymorphism of myosin among skeletal muscle fiber types. J Cell Biol 74:760–779
Gauthier GF, Lowey S (1979) Distribution of myosin isoenzymes among skeletal muscle fiber types. J Cell Biol 81:10–25
Gröschel-Stewart U, Meschede K, Lehr I (1973) Histochemical and immunochemical studies on mammalian striated muscle fibres. Histochemie 33:79–85
Guth L, Samaha FJ (1969) Qualitative differences between actomyosin ATPase of slow and fast mammalian muscle. Exp Neurol 25:138–152
Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680–685
Lowry OH, Passonneau JV (1972) A flexible system of enzymatic analysis. Academic Press, New York London
Lutz H, Weber R, Billeter R, Jenny E (1979) Fast and slow myosin within single skeletal fibres of adult rabbits. Nature 281:142–144
Mabuchi K, Pinter K, Mabuchi MS, Sréter F, Gergely J (1984) Characterization of rabbit masseter muscle fibers. Muscle Nerve 7:431–438
Oakley BR, Kirsch DR, Morris NR (1980)A simplified ultrasensitive silver stain for detecting proteins in polyacrylamide gels. Anal Biochem 105:361–363
Pierobon-Bormioli S, Sartore S, Dalla Libera L, Vitadello M, Schiaffino S (1981) “Fast” isomyosins and fiber types in mammalian skeletal muscle. J Histochem Cytochem 29:1179–1188
Reiser PJ, Moss RL, Giulian GG, Greaser ML (1985a) Shortening velocity in single fibers from adult rabbit soleus muscles is correlated with myosin heavy chain composition. J Biol Chem 260:9077–9080
Reiser PJ, Moss RL, Giulian GG (1985b) Shortening velocity and myosin heavy chains of developing rabbit muscle fibers. J Biol Chem 260:14403–14405
Rushbrock JI, Stracher A (1979) Comparison of adult, embryonic, and dystrophic myosin heavy chains from chicken muscle by sodium dodecyl sulfate/polyacrylamide gel electrophoresis and peptide mapping. Proc Natl Acad Sci USA 76:4331–4334
Salviati G, Betto R, Danieli Betto D (1982) Polymorphism of myofibrillar proteins of rabbit skeletal-muscle fibres. Biochem J 207:261–272
Salviati G, Betto R, Danieli Betto D, Zeviani M (1983) Myofibrillar-protein isoforms and sarcoplasmic-reticulum Ca2+-transport activity of single human muscle fibres. Biochem J 224:215–225
Staron RS, Pette D (1986a) The multiplicity of myosin light and heavy chain combinations in histochemically typed single fibres. II. Rabbit tibialis anterior muscle. Biochem J (in press)
Staron RS, Pette D (1986b) The multiplicity of myosin light and heavy chain combinations in histochemically types single fibres. I. Rabbit soleus muscle. Biochem J (in press)
Staron RS, Hikida RS, Hagerman FC (1983) Reevaluation of human muscle fast-twitch subtypes: evidence for a continuum. Histochemistry 78:33–39
Teutsch HF (1986) A new sample isolation procedure for microchemical analysis of functional liver cell heterogeneity. J Histochem Cytochem 34:263–267
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Staron, R.S., Pette, D. Correlation between myofibrillar ATPase activity and myosin heavy chain composition in rabbit muscle fibers. Histochemistry 86, 19–23 (1986). https://doi.org/10.1007/BF00492341
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DOI: https://doi.org/10.1007/BF00492341