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The Presence of Two Skeletal Muscle Alpha-actinins Correlates with Troponin-tropomyosin Expression and Z-line Width

Overview
Journal J Cell Biol
Specialty Cell Biology
Date 1985 Sep 1
PMID 4030889
Citations 14
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Abstract

Two species of alpha-actinin from rabbit fast skeletal muscles were identified with a monospecific antisera. Designated alpha-actinin1f and alpha-actinin2f, their distribution in muscles does not correlate with histochemically defined fast fiber type. Rather, the presence of each correlates with Z-line width and with the expression of different thin filament Ca2+-regulatory complexes. alpha-Actinin1f is expressed with troponin T 1f-alpha beta tropomyosin, and alpha-actinin2f with troponin T 2f-alpha 2 tropomyosin. CNBr peptide maps show that the fast alpha-actinin species differ in primary structure. In contrast, the slow alpha-actinin is indistinguishable from alpha-actinin1f. Further evidence for the similarity of alpha-actinin1f and slow alpha-actinin comes from electron microscopic studies which show that fibers that express these species exhibit thick Z-lines. So, unlike other contractile proteins, the multiple forms of alpha-actinin do not reflect the distinction between fast- and slow-twitch muscles.

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References
1.
Bronson D, Schachat F . Heterogeneity of contractile proteins. Differences in tropomyosin in fast, mixed, and slow skeletal muscles of the rabbit. J Biol Chem. 1982; 257(7):3937-44. View

2.
Callaway J, Bechtel P . C-protein from rabbit soleus (red) muscle. Biochem J. 1981; 195(2):463-9. PMC: 1162910. DOI: 10.1042/bj1950463. View

3.
Kobayashi R, Itoh H, Tashima Y . Polymorphism of alpha-actinin. Electrophoretic and immunological studies of rabbit skeletal muscle alpha-actinins. Eur J Biochem. 1983; 133(3):607-11. DOI: 10.1111/j.1432-1033.1983.tb07505.x. View

4.
Matsuda R, Spector D, Strohman R . Denervated skeletal muscle displays discoordinate regulation for the synthesis of several myofibrillar proteins. Proc Natl Acad Sci U S A. 1984; 81(4):1122-5. PMC: 344777. DOI: 10.1073/pnas.81.4.1122. View

5.
Kobayashi R, Itoh H, Tashima Y . Different muscle-specific forms of rabbit skeletal muscle alpha-actinin. Eur J Biochem. 1984; 143(1):125-31. DOI: 10.1111/j.1432-1033.1984.tb08351.x. View