| Autor: |
Wrenn RW; School of Medicine, Medical College of Georgia, Augusta 30912-2000., Herman LE |
| Jazyk: |
angličtina |
| Zdroj: |
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 1995 Mar 28; Vol. 208 (3), pp. 978-84. |
| DOI: |
10.1006/bbrc.1995.1430 |
| Abstrakt: |
Ligation of beta 1 integrin receptors resulted in increased tyrosine phosphorylation of at least five proteins (Mrest = 110, 85, 55, 30 and 24 kD) from rat pancreatic acinar cells. Increased protein kinase C (PKC) activity and elevated amounts of immunoreactive PKC alpha were demonstrated in membrane fractions from integrin-ligated acinar cells. Membrane translocation of PKC alpha was confirmed using scanning confocal laser microscopy in immunocytochemical preparations of acinar cells following beta 1 integrin ligation. These studies establish the presence of a beta 1 integrin-linked protein tyrosine phosphorylation system in exocrine pancreatic cells and provide evidence for integrative activity of this system with PKC, a primary signalling pathway of central importance in these cells. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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