Proteins of the membrane skeleton in rat Sertoli cells

J Cell Sci. 1986 Dec:86:145-54. doi: 10.1242/jcs.86.1.145.

Abstract

Analogues of the alpha, beta and gamma subunits of human spectrin and erythroid protein 4.1 have been detected in rat Sertoli cell primary cultures. Immunofluorescence of permeabilized cells showed that erythroid type spectrin, protein 4.1 and actin co-distribute within the cells as filamentous structures. Fodrin-like molecules were distributed in a diffuse manner, mostly associated with the plasma membrane. Immunoprecipitation and immunoblotting experiments indicated that the polypeptides present in rat Sertoli cells are immunologically related and display molecular weights similar to their analogues in the human erythroid and non-erythroid membrane skeleton.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins / analysis
  • Animals
  • Blood Proteins / analysis
  • Carrier Proteins / analysis
  • Cell Membrane / analysis
  • Cells, Cultured
  • Cytoskeletal Proteins*
  • Fluorescent Antibody Technique
  • Male
  • Membrane Proteins / analysis*
  • Microfilament Proteins / analysis
  • Neuropeptides*
  • Rats
  • Rats, Inbred Strains
  • Sertoli Cells / analysis*
  • Spectrin / analysis
  • Vimentin / analysis

Substances

  • Actins
  • Blood Proteins
  • Carrier Proteins
  • Cytoskeletal Proteins
  • Membrane Proteins
  • Microfilament Proteins
  • Neuropeptides
  • Vimentin
  • erythrocyte membrane band 4.1 protein
  • erythrocyte membrane protein band 4.1-like 1
  • fodrin
  • Spectrin