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activity is linked to
increased collagen IV in mesangial cells
1 Institute of Metabolic
Research and Exocell,
Albumin modified by Amadori-glucose adducts
induces coordinate increases in the expression of extracellular matrix
proteins, transforming growth factor (TGF)-
1, and the TGF- type
II receptor in glomerular mesangial cells. Because activation of
protein kinase C (PKC) accompanies the increased mesangial cell
expression of matrix proteins and TGF-1 induced by high ambient
glucose, we postulated that glycated albumin (GA) modulates PKC
activity and that PKC participates in mediating the GA-induced
stimulation of matrix production. To test this hypothesis, we examined
the effects of PKC inhibitors on collagen type IV production by mouse or rat mesangial cells incubated with GA, and the influence of GA on
PKC activity in these cells. Increased collagen type IV production
evoked by GA in 5.5 and 25 mM glucose in mouse mesangial cells was
prevented by both general (GF-109203X) and -specific (LY-379196) PKC
inhibitors. Total PKC activity, measured by phosphorylation of a
PKC-specific substrate, increased with time after exposure of rat
mesangial cells to GA compared with the nonglycated, glucose-free counterpart. GA caused an increase in PKC-1 membrane-bound fraction and in total PKC activity in media containing physiological (5.5 mM)
glucose concentrations in rat mesangial cells, confirming that the
glucose-modified protein, and not a "hyperglycemic" milieu, was
responsible. The findings indicate that Amadori-modified albumin stimulates mesangial cell PKC activity, and that activation of the
PKC- isoform is linked to the stimulation of collagen type IV production.
glucose; protein kinase C; amadori; glycation; diabetic nephropathy
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