Site-directed mutagenesis of putative protein kinase C phosphorylation sites in human AT1 receptor: effects on angiotensin-provoked intracellular calcium mobilisation in stably transfected Chinese hamster ovary cells.
Barker
S
S
Department of Chemical Endocrinology, St. Bartholomew's Hospital, London, UK.
Lavender
P M
PM
Clark
A J
AJ
D000804:Angiotensin II / Q000494:pharmacology*; D000818:Animals; D016466:CHO Cells; D002118:Calcium / Q000494:pharmacology*; D006224:Cricetinae; D006801:Humans; D007700:Kinetics; D016297:Mutagenesis, Site-Directed; D010766:Phosphorylation; D017354:Point Mutation; D011493:Protein Kinase C / Q000378:metabolism*; D011869:Radioligand Assay; D044140:Receptor, Angiotensin, Type 1; D044139:Receptor, Angiotensin, Type 2; D011945:Receptors, Angiotensin / Q000096:biosynthesis / Q000502:physiology*; D011994:Recombinant Proteins / Q000378:metabolism; D014162:Transfection
D044140:Receptor, Angiotensin, Type 1; D044139:Receptor, Angiotensin, Type 2; D011945:Receptors, Angiotensin; D011994:Recombinant Proteins; D000804:Angiotensin II; D011493:Protein Kinase C; D002118:Calcium