Analysis of protein kinase C isoforms involved in the activation of laminin receptor in Raw264.7 macrophages

Adherence of hematopoietic macrophages to a laminin (LM) substratum require s protein kinase C (PKC)-dependent activation of LM receptor This study was performed to analyze PKC isoform(s) leading to the activation of LM recept or during Raw264.7 macrophage-like cell adhesion to a LM substratum. Raw264 .7 cells expressed multiple PKC isoforms, including alpha, beta I, delta, e psilon, zeta, lambda/iota, and mu. Among the PKC isoforms expressed, select ive activation of PKC delta and epsilon was sufficient to induce cell adhes ion to LM. PKC-dependent cell adherence was blocked by the selective inhibi tion of PKC delta, suggesting that PKC delta was the responsible PKC isofor m leading to activation of LM receptor. PKC delta appeared to activate LM r eceptor in an intact microfilament-dependent pathway, because disruption of microfilament inhibited cell adhesion to LM without affecting PKC delta ac tivation.