The recycling of a secretory granule membrane protein.

Abstract:

:We have used N-hydroxysuccinimido-d-biotin as a reagent for labeling proteins exposed at the surface of cultured bovine adrenal chromaffin cells during Ba2+-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 [125I] 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 b561, another major secretory granule membrane component.

journal_name

Exp Cell Res

authors

Hunter A,Phillips JH

doi

10.1016/0014-4827(89)90249-8

subject

Has Abstract

pub_date

1989-06-01 00:00:00

pages

445-60

issue

2

eissn

0014-4827

issn

1090-2422

journal_volume

182

pub_type

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