A calmodulin dependent protein kinase in parietal cells

An enriched population of isolated rabbit gastric parietal cells, from the fundic mucosa of New Zealand White rabbit, contained an active cytosolic calmodulin-dependant protein kinase activity with a prominent 100 kDa substrate (pp100). The latter focused as a doublet with isoelectric point of 6.8 –...

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Veröffentlicht in:Biochemical and biophysical research communications 1987-11, Vol.148 (3), p.1390-1397
Hauptverfasser: Oddsdottir, Margret, Modlin, Irvin M., Zucker, Karl A., Zdon, Michael J., Goldenring, James R.
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Sprache:eng
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Zusammenfassung:An enriched population of isolated rabbit gastric parietal cells, from the fundic mucosa of New Zealand White rabbit, contained an active cytosolic calmodulin-dependant protein kinase activity with a prominent 100 kDa substrate (pp100). The latter focused as a doublet with isoelectric point of 6.8 – 7.0. The pp100 protein was phosphorylated only on threonine residues on a single tryptic peptide. Trifluoperazine inhibited the pp100 kinase activity with a K I of 10 – 15 μM. Addition of exogenous calmodulin was able to restore activity to uninhibited levels. A protein band with a molecular weight and phosphopeptide map identical to pp100, phosphorylated by calcium-dependent kinase, was also observed in rabbit pancreatic cytosol. The data suggest that a type III calmodulin-dependent kinase is present in parietal cell cytosol.
ISSN:0006-291X
1090-2104
DOI:10.1016/S0006-291X(87)80286-3