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Hormone Research Center, Department of Veterinary Physiology, College of Veterinary Medicine, Chonnam National University, Kwangju 500-757, Korea
The renin-angiotensin system
plays an important role in the development of diabetic nephropathy.
However, the mechanism of ANG II receptor regulation in the renal
proximal tubule in the diabetic condition has not been elucidated. Thus
we investigated the signal pathways involved in high-glucose-induced
downregulation of ANG II binding in primary cultured renal proximal
tubule cells. Twenty-five millimolar glucose, but not mannitol and
L-glucose, induced downregulation of the AT1
receptor (AT1R) because of a significant decline in maximal
binding with no significant change in the affinity constant.
Twenty-five millimolar glucose also decreased AT1R mRNA and
protein levels. The 25 mM glucose-induced increase in the formation of
lipid peroxides was prevented by antioxidants, protein kinase C (PKC)
inhibitors, or L-type calcium channel blockers. These agents also
blocked 25 mM glucose-induced downregulation of 125I-ANG II
binding. In addition, 25 mM glucose increased transforming growth
factor (TGF)-
1 secretion, and anti-TGF- antibody significantly blocked 25 mM glucose-induced downregulation of 125I-ANG II
binding. Furthermore, the 25 mM glucose-induced increase in TGF-1
secretion was inhibited by PKC inhibitors, L-type calcium channel
blockers, or antioxidants. In conclusion, high glucose may induce
downregulation of 125I-ANG II binding via a PKC-oxidative
stress-TGF- signal cascade in primary cultured rabbit renal proximal
tubule cells.
angiotensin II receptor; protein kinase C; transforming growth
factor-1
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