Abstract
Regulation of Immune System Cell Functions by Protein Kinase C
Highlights
Discovered in 1977, by Nishizuka and coworkers, protein kinase C (PKC) was initially identified as a cyclic nucleotide-independent protein kinase that is capable of phosphorylating histone and protamine following Ca2+-dependent limited proteolysis of its proenzyme precursor [1, 2]
These findings and additional data established a new pathway of signal transduction and led to identification of biological roles for PKC in signaling pathways linked to a variety of surface receptors in many different cell types
The PKC family of serine/threonine kinases consists of 10 distinct isoforms that are differentially expressed in a wide range of cell types and tissues
Summary
Discovered in 1977, by Nishizuka and coworkers, PKC was initially identified as a cyclic nucleotide-independent protein kinase that is capable of phosphorylating histone and protamine following Ca2+-dependent limited proteolysis of its proenzyme precursor [1, 2]. This Research Topic focuses on recent developments relevant to the role of PKC in immune cell functions, and includes contributions by many of the leading experts in the field. PKCα [7] to antigen-induced T cell activation and argue that inhibition T cell-mediated responses, including allograft rejection and autoimmunity, requires the inhibition of both PKC isoforms.
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