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Interaction of two brain annexins, CaBP33 and CaBP37, with membrane‐skeleton proteins
Author(s) -
Giambanco Ileana,
Pula Grazia,
Bianchi Roberta,
Donato Rosario
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80316-b
Subject(s) - cytoskeleton , actin , in vitro , biophysics , biochemistry , chemistry , spectrin , microbiology and biotechnology , biology , cell
CaPB33 and CaPB37, two annexins purified from bovine brain, interact with a Triton X‐100‐resistant fraction (cytoskeleton) from bovine brain membranes in a Ca 2+ ‐dependent way in vitro. The binding is saturable with respect to the CaBP33–CaBP37 concentration, half‐maximal binding occurring at ~15 μg of the CaBP33–CaBP37 mixture/ml. The binding of these two annexins to the crude cytoskeleton preparation as a function of free Ca 2+ concentration is biphasic, with half‐maximal binding at ~ 50 μM and ~ 400 μM free Ca 2+ for the first and the second component, respectively. By an overlay technique, CaBP33 and CaBP37 bind to a set of low M r polypeptides (10–20 kDa) in the crude cytoskeleton preparation, with formation of an 85–90 kDa complex as investigated in cross‐linking experiments. No binding of the CaBP33–CaBP37 mixture to either G‐or F‐actin has been observed. Identification of the CaBP33–CaBP37‐binding proteins in cytoskeletons would help elucidating the function(s) of these annexins in the brain.