Cellular distribution of three mammalian Ca2+‐binding proteins related to Torpedo calelectrin.

Authors:
  • MGM. Geisow
    M. Geisow
  • JCJ. Childs
    J. Childs
  • BDB. Dash
    B. Dash
  • AHA. Harris
    A. Harris
  • GPG. Panayotou
    G. Panayotou
  • TST. Südhof
    T. Südhof
  • JWJ.H. Walker
    J.H. Walker
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Abstract
Addition of Ca2+ to post‐microsomal fractions of bovine adrenal or liver produced a sedimentable complex of membrane vesicles and cytoplasmic proteins. Proteins with apparent mol. wts. 70 000, 36 000 and 32 500 were solubilized from this complex by Ca2+ chelation. The 36 000 mol. wt. protein (p36) was immunoprecipitated by an antiserum specific for pp36, a major substrate for Rous sarcoma virus src‐gene tyrosine kinase. This protein was present in many mesenchymal cells and associated with membrane cytoskeleton of bovine fibroblasts in a Ca2+‐dependent manner. The 70 000 and 32 500 mol. wt. proteins were widely distributed in established cell lines, but were not clearly associated with cell organelles in tissue sections, nor retained in cytoskeleton preparations. On immunoblots p36 reacted strongly with antibodies produced against the electric fish protein Torpedo calelectrin and the similar Ca2+‐binding properties and subunit mol. wts. of these proteins suggests that they might be functionally related. Since Torpedo calelectrin, p70, p36 and p32.5 were bound by lipid vesicles or microsomal membranes at micromolar free Ca2+ concentrations, regulated association with intrinsic membrane components may be involved in the functions of these widespread proteins.

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