Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:2.7.11.13 (protein kinase C)
 49,245 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

An improved differential display technique was used to search for changes in gene expression in the superior frontal cortex of alcoholics. A cDNA fragment was retrieved and cloned. Further sequence of the cDNA was determined from 5' RACE and screening of a human brain cDNA library. The gene was named hNP22 (human neuronal protein 22). The deduced protein sequence of hNP22 has an estimated molecular mass of 22.4 kDa with a putative calcium-binding site, and phosphorylation sites for casein kinase II and protein kinase C. The deduced amino acid sequence of hNP22 shares homology (from 67% to 42%) with four other proteins, SM22alpha, calponin, myophilin and mp20. Sequence homology suggests a potential interaction of hNP22 with cytoskeletal elements. hNP22 mRNA was expressed in various brain regions but in alcoholics, greater mRNA expression occurred in the superior frontal cortex, but not in the primary motor cortex or cerebellum. The results suggest that hNP22 may have a role in alcohol-related adaptations and may mediate regulatory signal transduction pathways in neurones.
 ...
PMID:Molecular cloning and characterization of hNP22: a gene up-regulated in human alcoholic brain. 1123 12

The expression of human neuronal protein 22 (hNP22) is up-regulated in the superior frontal cortex of chronic alcoholics. hNP22 shares significant homology with a number of proteins implicated in bundling of actin filaments. In addition, it contains domains similar to those found in microtubule-associated proteins. We investigated the ability of hNP22 to induce cytoskeletal changes by overexpression in Chinese hamster ovary cells. Overexpression of hNP22 resulted in process formation in these cells that increased upon treatment with cytochalasin D, an actin depolymerising agent. Transfection of mutant hNP22 containing either a deletion of the putative actin-binding domain or deletion of a consensus protein kinase C (PKC) phosphorylation site (Ser-180) failed to induce process formation. In contrast, a mutation to mimic persistent PKC phosphorylation resulted in a cellular morphology similar to that seen in wild-type hNP22 transfections. This observation suggests that hNP22 requires phosphorylation at Ser-180 by PKC to induce cytoskeletal rearrangements. hNP22 was also observed to colocalise with actin and tubulin in processes of transfected cells. An hNP22-specific antibody specifically immunoprecipitated a complex including tubulin from human brain indicating that hNP22 binds directly to microtubules. Taken together, this data suggests that NP22 is part of a signaling complex that associates with cytoskeletal elements to regulate neuronal morphology.
 ...
PMID:Neuronal protein 22 colocalises with both the microtubule and microfilament cytoskeleton in neurite-like processes. 1712 83