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The recycling of a secretory granule membrane protein

Journal Article · · Experimental Cell Research; (United States)
;  [1]
  1. Univ. of Edinburgh Medical School (United Kingdom)
The authors have used N-hydroxysuccinimido-d-biotin as a reagent for labeling proteins exposed at the surface of cultured bovine adrenal chromaffin cells during Ba{sup 2+}-stimulated secretion. A specific secretory granule membrane constituent, dopamine-{beta}-hydroxylase (DBH), has been investigated using immunoprecipitation followed by electrophoresis. Within 30 min of stimulation, exposed DBH had been cleared from the cell surface. Nevertheless, quantitation of labeled DBH using ({sup 125}I)streptavidin suggested that it remained undegraded over a period of 24 h, a time during which secretory granule stores of catecholamines were being replenished. Subcellular fractionation of the cultured cells suggested that, after 3 or 4 h, the biotinylated DBH, which was still membrane-bound, was located in particulate material that also contained cytochrome b{sub 561}, another major secretory granule membrane component.
OSTI ID:
5745062
Journal Information:
Experimental Cell Research; (United States), Journal Name: Experimental Cell Research; (United States) Vol. 182:2; ISSN ECREA; ISSN 0014-4827
Country of Publication:
United States
Language:
English

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