Synexin protein is non-selective in its ability to increase Ca2+-dependent aggregation of biological and artificial membranes |
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Authors: | S J Morris J M Hughes |
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Affiliation: | Department of Neurochemistry Max Planck Institute for Biophysical Chemistry D-3400 Göttingen-Nikolausberg, FRG |
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Abstract: | Synexin, a soluble protein which increases the specificity of Ca2+ to aggregate isolated bovine chromaffin granules was prepared from bovine adrenal medullary tissue by the method of Creutz, Pazoles and Pollard (J. Biol. Chem. , 2858–2866, 1978). We also find that synexin increases both the initial rate and final amplitude of Ca2+-promoted aggregation of granule membranes. This effect is Ca2+-specific. However in contrast to Creutz , we find that synexin also potentiates aggregation of adrenal medulla and liver mitochondria and microsomes as well as phosphatidylserine vesicles. This lack of membrane specificity argues against the suggestion of Creutz that synexin specifically binds the granule to the plasma membrane prior to exocytosis . |
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Keywords: | HEPES 4-(2-hydroxyethyl)-l-piperazine-ethansulphonic acid PS phosphatidylserine |
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