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Protein kinase C (PKC) zeta is a member of the PKC family of serine/threonine kinases which are involved in a variety of cellular processes such as proliferation, differentiation and secretion. Unlike the classical PKC isoenzymes which are calcium-dependent, PKC zeta exhibits a kinase activity which is independent of calcium and diacylglycerol but not of phosphatidylserine. Furthermore, it is insensitive to typical PKC inhibitors and cannot be activated by phorbol ester. Unlike the classical

IL18 (IFN-gamma-inducing factor, IGIF) is a novel pro-inflammatory cytokine that augments natural killer (NK) activity in spleen cells. This cytokine can induce the IFN-gamma production of T cells. The combination of this cytokine and IL12 has been shown to inhibit IL4 dependent IgE and IgG1 production, and enhance IgG2a production of B cells. IL18 binding protein (IL18BP) can specifically interact with this cytokine, and thus negatively regulate its biological activity.

This gene represents a phospholipase A2 receptor. The encoded protein likely exists as both a transmembrane form and a soluble form. The transmembrane receptor may play a role in clearance of phospholipase A2, thereby inhibiting its action. Polymorphisms at this locus have been associated with susceptibility to idiopathic membranous nephropathy. Alternatively spliced transcript variants encoding different isoforms have been identified.[provided by RefSeq, Sep 2010]

Pituitary adenylate cyclase-activating polypeptide (PACAP) is a neuropeptide belonging to the vasoactive intestinal polypeptide/glucagon/ secretin family. It is widely distributed in the body, and a variety of biological actions have been reported. Recent studies have shown that there is a family of PACAP receptors (PACAPRs), and two members of this family have been identified. Mouse PACAPR-3 is a protein of 437 amino acids that has 50% and 51% identity with rat PACAP type I and type II rec

DMP-1 is a member of the small integrin ligand N-linked glycoprotein family. It is important for the mineralization of bone and dentin. DMP-1 is expressed in bone, tooth and hypertrophic cartilage. It is synthesized by preosteoblasts and contains a large number of acidic domains. DMP-1 localizes to the nucleus of undifferentiated osteoblasts where it functions as a transcriptional regulator for osteoblast-specific gene activation and induces osteoblast differentiation. During osteoblast mat

This gene encodes the D2 subtype of the dopamine receptor. This G-protein coupled receptor inhibits adenylyl cyclase activity. A missense mutation in this gene causes myoclonus dystonia; other mutations have been associated with schizophrenia. Alternative splicing of this gene results in two transcript variants encoding different isoforms. A third variant has been described, but it has not been determined whether this form is normal or due to aberrant splicing. [provided by RefSeq, Jul 2008]