0100488705

open access

Version of Record

MONOCLONAL ANTIBODIES AGAINST RAT BRAIN PROTEIN KINASE C

English (英語)

The Kobe journal of the medical sciences

33(3)

107-120

1987-06

Protein kinase Chas attracted great attention for the studies on the activation of cellular functions and proliferation, and the knowledge of possible roles of this enzyme in cell surface signal transduction is expanding rapidly. Under physiological conditions, protein kinase C is activated by diacylglycerol which may arise from receptor-mediated hydrolysis of inositol phospholipids. Three monoclonal antibodies were prepared against rat brain protein kinase C. Two of the antibodies, CKI-97 and CKII-90, showed weak binding to native protein kinase C. The third antibody, CKI-33 showed no binding. The mixture of these monoclonal antibodies exhibited much stronger binding activity to this protein kinase than any of the antibodies alone. None of these antibodies neutralized the enzymatic activity. These antibodies did not recognize cyclic AMP-dependent nor cyclic GMP-dependent protein kinase. In Purkinje cells, the immunoreactive material was present throughout the cytoplasm including dendrites and axons, but pooly represented in the cell nucleus. These monoclonal antibodies may be useful for immunocytochemical studies of protein kinase C in the nervous system.

immunocytochemistry

紀要論文