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Vol. 9, Issue 1, 47-61, January 1998

Developmental Expression of Spectrins in Rat Skeletal Muscle

Daixing Zhou, Jeanine A. Ursitti, and Robert J. Bloch*

Department of Physiology, University of Maryland School of Medicine, Baltimore, Maryland 21201

Skeletal muscle contains spectrin (or spectrin I) and fodrin (or spectrin II), members of the spectrin supergene family. We used isoform-specific antibodies and cDNA probes to investigate the molecular forms, developmental expression, and subcellular localization of the spectrins in skeletal muscle of the rat. We report that beta -spectrin (beta I) replaces beta -fodrin (beta II) at the sarcolemma as skeletal muscle fibers develop. As a result, adult muscle fibers contain only alpha -fodrin (alpha II) and the muscle isoform of beta -spectrin (beta ISigma 2). By contrast, other types of cells present in skeletal muscle tissue, including blood vessels and nerves, contain only alpha - and beta -fodrin. During late embryogenesis and early postnatal development, skeletal muscle fibers contain a previously unknown form of spectrin complex, consisting of alpha -fodrin, beta -fodrin, and the muscle isoform of beta -spectrin. These complexes associate with the sarcolemma to form linear membrane skeletal structures that otherwise resemble the structures found in the adult. Our results suggest that the spectrin-based membrane skeleton of muscle fibers can exist in three distinct states during development.


Molecular Biology of the Cell
Vol. 9, 47-61, January 1998
Copyright © 1998 by The American Society for Cell Biology



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