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cAMP‐dependent protein kinase activation affects vasopressin V 2 ‐receptor number and internalization in LLC‐PK 1 renal epithelial cells
Author(s) -
Jans David A.,
Hemmings Brian A.
Publication year - 1991
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(91)80408-u
Subject(s) - internalization , vasopressin , kinase , chemistry , microbiology and biotechnology , receptor , endocrinology , medicine , biology , biochemistry
The relationship between activation of the cAMP‐dependent protein kinase (cAMP‐PK) and ligand binding and internalization by the vasopressin renal (V 2 ‐type) receptor of LLC‐PK 1 renal epithelial cells was examined. Upon cAMP‐PK activation through 1 h treatment with the cAMP analogue 8‐bromo‐cAMP (BrcA), a marked reduction in V 2 ‐receptor steady state number and internalization in LLC‐PK 1 cells was effected. In cells treated for 17 h with BrcA and hence down‐regulated for cAMP‐PK 1 the V 2 ‐receptor number was normal but internalization was markedly reduced. Cells of the LLC‐PK 1 mutant FIB4, which possesses about 10% parental cAMP‐PK catalytic subunit activity, exhibited lower V 2 ‐receptor steady state number and internalization in comparison to untreated LLC‐PK 1 cells. A negative correlation was thus evident between cAMP‐PK activation and V 2 ‐receptor number and internalization. Phosphorylation by cAMP‐PK may effect ligand‐independent removal of receptor from the plasma membrane.