Literature summary for 1.6.3.1 extracted from

Thallas-Bonke, V.; Thorpe, S.R.; Coughlan, M.T.; Fukami, K.; Yap, F.Y.; Sourris, K.C.; Penfold, S.A.; Bach, L.A.; Cooper, M.E.; Forbes, J.M.
Inhibition of NADPH oxidase prevents advanced glycation end product-mediated damage in diabetic nephropathy through a protein kinase C-alpha-dependent pathway (2008), Diabetes, 57, 460-469.

Search for more literature for 1.6.3.1

Application

Application	Comment	Organism
medicine	diabetes-induced translocation of protein kinase C, specifically PKC-alpha to renal membranes is associated with increased NADPH-dependent superoxide production. In both diabetic animals and in advanced glycation end products-treated mesangial cells, blockade of NADPH oxidase or PKC-alpha attenuates cytosolic superoxide and protein kinase C activation and increases vascular endothelial growth factor	Rattus norvegicus

Organism

Organism	UniProt	Comment	Textmining
Rattus norvegicus	-	-	-

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)