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Two populations of β-spectrin in rat skeletal muscle

Academic Article
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Overview

authors

  • Porter, G. A.
  • Scher, M. G.
  • Resneck, W. G.
  • Porter, N. C.
  • Fowler, Velia
  • Bloch, R. J.

publication date

  • 1997

journal

  • Cell Motility and the Cytoskeleton  Journal

abstract

  • We use immunoblotting, immunoprecipitation, and centrifugation in sucrose density gradients to show that the product of the erythrocyte beta-spectrin gene in rat skeletal muscle (muscle beta-spectrin) is present in two states, one associated with fodrin, and another that is not associated with any identifiable spectrin or fodrin subunit. Immunofluorescence studies indicate that a significant amount of beta-spectrin without alpha-fodrin is present in the myoplasm of some muscle fibers, and, more strikingly, at distinct regions of the sarcolemma. These results suggest that alpha-fodrin and muscle beta-spectrin associate in muscle in situ, but that some muscle beta-spectrin without a paired alpha-subunit forms distinct domains at the sarcolemma.

subject areas

  • Animals
  • Carrier Proteins
  • Centrifugation, Density Gradient
  • Female
  • Fluorescent Antibody Technique
  • Immunoblotting
  • Microfilament Proteins
  • Muscle Fibers, Skeletal
  • Muscle Proteins
  • Muscle, Skeletal
  • Peptide Fragments
  • Precipitin Tests
  • Protein Structure, Tertiary
  • Rats
  • Sarcolemma
  • Spectrin
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Research

keywords

  • fodrin
  • membrane skeleton
  • skeletal muscle
  • spectrin
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Identity

International Standard Serial Number (ISSN)

  • 0886-1544

Digital Object Identifier (DOI)

  • 10.1002/(sici)1097-0169(1997)37:1<7::aid-cm2>3.3.co;2-n

PubMed ID

  • 9142435
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Additional Document Info

start page

  • 7

end page

  • 19

volume

  • 37

issue

  • 1

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