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Protein thiophosphorylation associated with secretory inhibition in permeabilized chromaffin cells

Journal Article · · Life Sci.; (United States)

Permeabilized cells treated with the adenosine triphosphate analog, (/sup 35/S)adenosine-5'-0-3(3-thiotriphosphate) ((..gamma..-/sup 35/S)ATP), showed thiophosphorylation of a small number of cellular proteins. A 54 kilodalton (kDa) protein was heavily thiophosphorylated in unstimulated control cells and a 43 kilodalton protein was more heavily thiophosphorylated in calcium stimulated cells. Intact cells incorporated /sup 35/S into a series of higher molecular weight proteins. Stimulation of prelabelled, permeabilized cells resulted in a loss of /sup 35/S from the cells over a 20 min period. Treatment of permeabilized cells with ATP..gamma..S inhibited secretion and /sup 35/S incorporation into the cells. Pretreatment with ATP..gamma..S resulted in subsequent inhibition of both secretion and the ability of the cells to incorporate /sup 35/S from (..gamma..-/sup 35/S)ATP. These results indicate that the sites normally available for phosphorylation were inactivated by thiophosphorylation and were unavailable to participate in the secretory process. The inhibition of secretion associated with thiophosphorylation of these proteins suggests that they may play a role in the control of secretion by chromaffin cells. 15 references, 1 figure, 3 tables.

Research Organization:
Marquette Univ. School of Dentistry, Milwaukee, WI
OSTI ID:
6138606
Journal Information:
Life Sci.; (United States), Journal Name: Life Sci.; (United States) Vol. 37:20; ISSN LIFSA
Country of Publication:
United States
Language:
English