Disease relevance of PRKCB1

• These results showed that enhanced ET-1 expression induced by hyperglycemia in diabetes is partly due to activation of PKC-beta and -delta isoforms, suggesting that inhibition of these PKC isoforms may prevent early changes in diabetic retinopathy and neuropathy [1].
• (86)Rb uptake studies showed that basolateral NKCC activity was down-regulated by both a conventional PKC inhibitor and specific inhibitors for PKCalpha, PKCbeta, and PKCvarepsilon and was up-regulated by an activator of conventional PKCs during 6-h hypoxia/aglycemia treatment [2].

High impact information on PRKCB1

• Thus, VEGF appears to mediate its mitogenic effects partly through the activation of the PLCgamma and PKC pathway, involving predominately PKC-beta isoform activation in endothelial cells [3].
• Previously, we and others have shown that one site in the 'activation loop' of PKCalpha (a threonine residue at position 497; T497) and PKCbeta (T500) is essential for the catalytic competence of these proteins [4].
• Treatment with 1,25-(OH)2-D3 (100 nM, 24 h) enhances plasma membrane association of PKC alpha and induces translocation of PKC beta to the nuclear membrane [5].
• TPA also induces translocation of PKC beta to the nuclear membrane [5].
• Use of a selective inhibitor of the beta isoform of PKC, LY379196, revealed that IGF-1 stimulation of glucose transport was mediated by PKC-beta; however, inhibition of PKC-beta had no effect on BREC proliferation [6].

Biological context of PRKCB1

• Coexpression of this PKC alpha mutant and wild type PKC beta demonstrates that the mutant has a dominant effect upon PKC beta phosphorylation [7].
• In contrast to rapid transient PKC translocation seen in response to agents which interact with membrane receptors to induce phospholipid hydrolysis, modulation of PKC alpha and PKC beta is observed after 24 h treatment with 1,25-(OH)2-D3 [5].
• 5. Transfection of PKCbeta-specific antisense oligonucleotide reduced PKCbetaI protein level and inhibited PMA-mediated PI reduction [8].
• In the parental cells, PKC-beta 2 expression results in increased homotypic cell aggregation and a prolonged doubling time [9].

Associations of PRKCB1 with chemical compounds

• Both Km and Vmax determined in the presence of Ca2+, phosphatidylserine and diacylglycerol were increased by the peptide epsilon modification for all three isoenzymes, while the only effect of MBP3-14 modification was a decrease in Km for PKCbeta [10].

Analytical, diagnostic and therapeutic context of PRKCB1

• PKC alpha immunofluorescence redistributed to the perinuclear region whereas PKC beta staining remained mostly cytosolic [11].

References