Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:2.7.11.12 (PKG)
 2,515 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

C-type natriuretic peptide (CNP) is a member of the natriuretic peptide family which is produced in vascular endothelial cells and may play an important paracrine role in the vasaculature. We sought to determine the regulation of CNP production by other vasoactive peptides from cultured aortic endothelial cells. The vasoconstrictors endothelin-1 and angiotensin II had little effect on the basal secretion of CNP. In contrast, atrial natriuretic peptide (ANP) and brain natriuretic peptide (BNP) strongly stimulated the secretion of CNP. BNP caused as much as a 400-fold enhancement above the basal accumulated secretion of CNP over 24 h at a concentration of 1 microM; this was 20 times greater than the stimulatory effect of ANP, BNP and ANP also significantly enhanced the production of new CNP protein (translation) and mRNA expressed in the BAEC. In contrast, C-ANP-4-23, a truncated form of ANP which selectively binds to the natriuretic peptide clearance receptor, did not stimulate CNP secretion. The enhanced production and secretion of CNP, caused by either ANP or BNP, was significantly prevented by LY 83583, an inhibitor of cGMP generation, and was also attenuated by KT 5823, an inhibitor of cGMP-dependent protein kinase. Our results indicate that ANP and BNP can stimulate CNP production through a guanylate cyclase receptor on endothelial cells. BNP is a much more potent stimulator of CNP secretion, compared to ANP. Our findings suggest that the vasodilatory, and anti-mitogenic effects of ANP and BNP in the vasculature could occur in part through CNP production and subsequent action if these interactions occur in vivo.
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PMID:Atrial and brain natriuretic peptides stimulate the production and secretion of C-type natriuretic peptide from bovine aortic endothelial cells. 788 64

A monoclonal antibody (MAb-46-1) specifically recognizing a 46 kDa basic protein solubilized from brain membranes was used to prepare an affinity column, which allowed a one-step purification of the 46 kDa protein to homogeneity starting from solubilized cerebellar membranes. MAb-46-1 could also immunoprecipitate the 46 kDa protein from solubilized pig or rat cerebellar membranes. Microsequence analysis of affinity purified 46 kDa protein treated with Lys C demonstrated the identity of the 46 kDa protein as a myelin associated protein, i.e. 2',3'-cyclic nucleotide 3'-phosphodiesterase (CNP, EC 3.1.4.37). The amino acid sequences obtained for the porcine CNP were nearly identical with the known sequences of the bovine and human isoforms but only partially with those of rat and mouse CNP. In SDS PAGE the porcine CNP appeared as a doublet of 44.6 and 45.9 kDa. Both bands of the doublet were equally well recognized by MAb-46-1. Porcine CNP was rapidly and specifically phosphorylated by both protein kinase A and cGMP-dependent protein kinase.
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PMID:The myelin protein CNP (2',3'-cyclic nucleotide 3'-phosphodiesterase): immunoaffinity purification of CNP from pig and rat brain using a monoclonal antibody and phosphorylation of CNP by cyclic nucleotide-dependent protein kinases. 801 Nov 77