Integrins play a critical role in cell adhesion and mediate cell signaling. This report identifies the association of serine protein kinase activity with the β1 integrin by immunoprecipitation and phosphoamino acid analysis techniques. Reprecipitation techniques suggested that the serine kinase activity was not a member of the protein kinase C family. By gel filtration, most of the protein kinase activity associated with β1 integrin as well as most of the cell-surface β1 integrin was present in large detergent resistant complexes. These results suggest that serine protein kinase activity associated with the β1 integrin may play a role in signaling via the β1 integrin.
Bibliographical noteFunding Information:
We would like to thank Drs. L. Furcht and A. Sonnenberg for providing antibodies and Dr. R. Bast, Jr. for providing cell lines and mAbs. Supported in part by NIH/NCI grant CA60658, the American Heart Association, Minnesota Affiliate, the Office of the Vice President for Research and Dean of the Graduate School of the University of Minnesota, the Minnesota Medical Foundation, and the Masonic Memorial Hospital Fund, Inc.
- Detergent resistant complex
- Ovarian carcinoma
- Protein kinase activity
- β1 integrin