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Cyclic amp‐dependent protein phosphorylation on the surface of rat hepatocytes
Author(s) -
Sommarin Marianne,
Henriksson Thomas,
Jergil Bengt
Publication year - 1981
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(81)80225-6
Subject(s) - citation , phosphorylation , chemistry , theology , biochemistry , philosophy , library science , computer science
Proteins of isolated plasma membranes from rat liver cells can be phosphorylated either by endogenous [l-3] or exogenously added [4] protein kinases. Protein phosphorylation in plasma membranes presumably serves as a general regulatory mechanism as is the case in other subcellular fractions. An example is the phosphorylation and thereby activation of a cyclic nucleotide phosphodiesterase associated as a peripheral protein with rat liver plasma membranes [ 51. The phosphorylation of other, as yet unidentified, plasma membrane proteins appears to be modulated by insulin [31. No studies have been performed so far on the phosphorylation of proteins on the external surface of isolated rat hepatocytes. The phosphorylation of surface proteins in other kinds of cells has been described, however [6-81. An examination of surface protein phosphorylation may yield information about regulatory mechanisms on the plasma membrane level. Here we report on cyclic AMP-dependent and independent phosphorylation of proteins on the outer surface of rat hepatocytes.