Date of Defense

Spring 4-24-1990


Biological Sciences


Activation and translocation of protein kinase C (PKC) Type III were demonstrated in the IIC9 fibroblast cell line. Criteria that phorbol-12-myristate 13-acetate (PMA) treatment specifically increased PKC in the nuceleus was demonstrated by Western blot. The blots showed that monoclonal antibodies specific for Type III PKC detected only one protein, PKC at 82,000 Dalton molecular weight, whose level increased in nuclear lysates from PMA-treated cells. Secondly, thrombin, a natural hormone, was used as an activator of phosphoinositide (PI) turnover to activate PKC and revealed translocation by Western blot analysis. In extension of studies of translocation of PKC to the nucleus, nuclear envelope isolations were performed in an attempt to identify the precise nuclear location of PKC. These results demonstrate that PMA activation leads to a redistribution of Type III PKC to the nucleus and suggest that this isozyme may play a role in mediating PKC-induced changes in gene expression.

Access Setting

Honors Thesis-Campus Only