Heterogeneity of human skeletal muscle tropomyosin.

Abstract:

:Six polypeptides resolved by two-dimensional electrophoresis of homogenates from human skeletal muscle have been identified as tropomyosin by electrophoretic and immunochemical methods. The 6 proteins are consistently present in approximately the same abundance in normal biceps, deltoid, gastrocnemius, and quadriceps muscle. Analysis of samples from individuals with Becker's dystrophy, Duchenne dystrophy, limb girdle dystrophy, polymyositis, myopathy related to vitamin E deficiency, type II fiber deficiency, and from an infant with indistinct fiber type differentiation, however, showed quantitative variations in the tropomyosin pattern. Muscle with histochemically demonstrated type II fiber deficiency lacked two of the normal tropomyosin proteins and the type II myosin light chains. Muscles lacking type I myosin light chains were deficient in a different pair of tropomyosin proteins. The results suggest that normal human skeletal muscle contains one major type of tropomyosin protein (beta-tropomyosin) common to both fast and slow fibers, together with two other major proteins (alpha-tropomyosin and alpha'-tropomyosin), one of which is specific to fast fibers and the other to slow fibers. Preliminary data from the reaction of muscle homogenates with alkaline phosphatase indicate that 3 of the 6 tropomyosin polypeptides resolved by two-dimensional electrophoresis are phosphorylated forms of the alpha-, alpha'-, and beta-tropomyosins.

journal_name

Ann Neurol

journal_title

Annals of neurology

authors

Giometti CS,Danon MJ

doi

10.1002/ana.410180211

subject

Has Abstract

pub_date

1985-08-01 00:00:00

pages

234-43

issue

2

eissn

0364-5134

issn

1531-8249

journal_volume

18

pub_type

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