An altered phosphoprotein in cystic fibrosis.
Phosphorylation of calmodulin-dependent regulator proteins has been studied in control and CF submandibular glands. Results showed that a 61,000 molecular weight calmodulin-binding protein was less phosphorylated in CF glands than control (p less than 0.001 for difference). The altered calmodulin-binding protein cross-reacted with an antiserum against a known calmodulin-dependent protein phosphatase, calcineurin. An alteration in a protein with calcineurin-like activity in CF epithelial cells would provide a link between defective beta-adrenergic responses and altered Ca2(+)-mediated events in CF and thus might be directly related to the genetic defect.
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
D000293:Adolescent; D000328:Adult; D019703:Calcineurin; D002148:Calmodulin-Binding Proteins / Q000737:chemistry / Q000378:metabolism; D003550:Cystic Fibrosis / Q000378:metabolism*; D006801:Humans; D066298:In Vitro Techniques; D008970:Molecular Weight; D010749:Phosphoprotein Phosphatases / Q000737:chemistry / Q000378:metabolism; D010750:Phosphoproteins / Q000737:chemistry / Q000378:metabolism*; D013363:Submandibular Gland / Q000378:metabolism
D002148:Calmodulin-Binding Proteins; D010750:Phosphoproteins; D019703:Calcineurin; D010749:Phosphoprotein Phosphatases