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Identification of a major endogenous substrate for phospholipid/Ca 2+ ‐dependent kinase in pancreatic acini as Gc (vitamin D‐binding protein)
Author(s) -
Wooten Marie W.,
Nel Andre E.,
Goldschmidt-Clermont Pascal J.,
Galbraith Robert M.,
Wrenn Robert W.
Publication year - 1985
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(85)81001-2
Subject(s) - endogeny , phospholipid , substrate (aquarium) , chemistry , vitamin d and neurology , biochemistry , protein kinase a , vitamin , kinase , endocrinology , biology , membrane , ecology
A major 56 kDa substrate for phospholipid/Ca 2+ ‐dependent kinase (C‐kinase) in pancreatic acinar cells is physicochemically and immunologically indistinguishable from the vitamin D‐binding protein, Gc or group‐specific component. Cellular Gc was also phosphorylated in intact cells following treatment with carbachol as a physiological stimulus. These findings indicate the potential usefulness of Gc as a defined substrate for further studies of the biological role of C‐kinase activity in pancreatic acini and possibly in other cells.