Redistribution of a 120 kDa Phosphoprotein in the Parietal Cell Associated with Stimulation

Redistribution of a 120 kDa Phosphoprotein in the Parietal Cell Associated with Stimulation When rabbit isolated gastric glands were stimulated via the cyclic AMP pathway, a phosphorylated protein band of about 120 kDa (pp120) was markedly increased in the apical membrane-rich fraction, concomitant with an increase in the amount of H,K-ATPase and the phosphorylation of the cytoskeletal protein ezrin in the same fraction. The cytosolic fraction, but not other membrane fractions, also contained a protein with common features to the membrane-bound pp120, i.e., comigration in two-dimensional gels with a pI of ∼4.5, anomalous mobility in SDS-PAGE, reactivity to antibodies, and phosphorylation, indicating that these two proteins were identical. The possibility that pp120 is vinculin was completely excluded. Using antibody against pp120, this protein was found to be almost exclusively in the gastric parietal cell. Biochemical and immunohistochemical analyses suggest that pp120 exists mainly in the cytosol, and that a small part of the protein binds to the apical membrane when the parietal cell is stimulated via the cyclic AMP pathway. In the presence of histone, purified pp120 produced phosphorylation on pp120 as well as histone. The inhibitor profile of this kinase activity is not consistent with any known kinase. We conclude that pp120 is closely associated with a new type of kinase, and translocates from cytosol to the apical membrane when the parietal cell is stimulated. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png The Journal of Membrane Biology Springer Journals

Redistribution of a 120 kDa Phosphoprotein in the Parietal Cell Associated with Stimulation

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Publisher
Springer-Verlag
Copyright
Copyright © Inc. by 1999 Springer-Verlag New York
Subject
Life Sciences; Biochemistry, general; Human Physiology
ISSN
0022-2631
eISSN
1432-1424
D.O.I.
10.1007/s002329900510
Publisher site
See Article on Publisher Site

Abstract

When rabbit isolated gastric glands were stimulated via the cyclic AMP pathway, a phosphorylated protein band of about 120 kDa (pp120) was markedly increased in the apical membrane-rich fraction, concomitant with an increase in the amount of H,K-ATPase and the phosphorylation of the cytoskeletal protein ezrin in the same fraction. The cytosolic fraction, but not other membrane fractions, also contained a protein with common features to the membrane-bound pp120, i.e., comigration in two-dimensional gels with a pI of ∼4.5, anomalous mobility in SDS-PAGE, reactivity to antibodies, and phosphorylation, indicating that these two proteins were identical. The possibility that pp120 is vinculin was completely excluded. Using antibody against pp120, this protein was found to be almost exclusively in the gastric parietal cell. Biochemical and immunohistochemical analyses suggest that pp120 exists mainly in the cytosol, and that a small part of the protein binds to the apical membrane when the parietal cell is stimulated via the cyclic AMP pathway. In the presence of histone, purified pp120 produced phosphorylation on pp120 as well as histone. The inhibitor profile of this kinase activity is not consistent with any known kinase. We conclude that pp120 is closely associated with a new type of kinase, and translocates from cytosol to the apical membrane when the parietal cell is stimulated.

Journal

The Journal of Membrane BiologySpringer Journals

Published: Apr 1, 1999

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