Immunolocalization of Protein Kinase C Alpha, Delta, Epsilon, and Zeta During Preosteoclast Diffferentiation Induced by Receptor Activator of NF-Kappa B Ligand and Macrophage-Colony Stimulating Factor

Abstract

Protein kinase C is a family of serine-threonine kinases that are physiologically activated by a number of lipid cofactors and are important transducers in many agonistind uced signaling cascades. Bone morphogenesis, remodeling, and resorption are controlled in part by osteoclasts. These cells arise from hematopoietic precursors by physiologically controlled processes that involve growth factors, cytokines, peptide, and steroid hormone interactions with their receptors. Osteoclast differentiation and activation is now known to be positively and negatively controlled by members of the tumor necrosis factor and tumor necrosis factor receptor superfamily of proteins. Protein kinase C (PKC) plays a critical role in numerous signal transduction pathways regulating a diversity of cellular processes including replication, differentiation. and phenotypic expression (Nishizuka, 1988, 1992). Previous studies have suggested that PKC pathway is an important second messenger in osteoclast. With this paper we want to demonstrate the immunolocalization of PKC, alpha, delta, epsilon, and zeta during osteoclasts formation. (The J Histoteclznol 29:167, 2006)Submitted April 10, 2006; accepted with revisions July 17, 2006