Defective phosphorylation of a calmodulin-binding protein in cystic-fibrosis submandibular glands.
Calmodulin-binding proteins in fractions purified from human submandibular glands by calmodulin-Sepharose were phosphorylated with [gamma-32P]ATP, in the absence of exogenous protein kinase. The major proteins phosphorylated had molecular masses of 45, 51 and 61 kDa. Phosphorylation was increased by activators of protein kinase C and inhibited by H-7. Phosphorylation of the 61 kDa band was markedly decreased in cystic-fibrosis submandibular glands.
Shori
D K
DK
Department of Medical Biochemistry, University of Wales College of Medicine, Cardiff, U.K.
Dormer
R L
RL
Goodchild
M C
MC
McPherson
M A
MA
D019307:1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine; D000255:Adenosine Triphosphate / Q000378:metabolism; D000293:Adolescent; D000328:Adult; D019703:Calcineurin; D002148:Calmodulin-Binding Proteins / Q000378:metabolism*; D000242:Cyclic AMP / Q000494:pharmacology; D003550:Cystic Fibrosis / Q000378:metabolism*; D004789:Enzyme Activation / Q000187:drug effects; D006801:Humans; D007546:Isoquinolines / Q000494:pharmacology; D010749:Phosphoprotein Phosphatases / Q000378:metabolism; D010766:Phosphorylation; D010879:Piperazines / Q000494:pharmacology; D011493:Protein Kinase C / Q000037:antagonists & inhibitors / Q000378:metabolism; D013363:Submandibular Gland / Q000378:metabolism*; D014268:Trifluoperazine / Q000494:pharmacology
D002148:Calmodulin-Binding Proteins; D007546:Isoquinolines; D010879:Piperazines; D014268:Trifluoperazine; D019307:1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine; D000255:Adenosine Triphosphate; D000242:Cyclic AMP; D011493:Protein Kinase C; D019703:Calcineurin; D010749:Phosphoprotein Phosphatases