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Wiedenmann, T.* ; Dietrich, N.* ; Fleming, T.* ; Altamura, S.* ; Deelman, L.E.* ; Henning, R.H.* ; Muckenthaler, M.U.* ; Nawroth, P.P. ; Hammes, H.P.* ; Wagner, A.H.* ; Hecker, M.*

Modulation of glutathione peroxidase activity by age-dependent carbonylation in glomeruli of diabetic mice.

J. Diab. Complic. 32, 130-138 (2018)

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Aims: Low levels of reactive oxygen species and resulting oxidative protein modifications may play a beneficial role in cellular function under stress conditions. Here we studied the influence of age-dependent protein carbonylation on expression and activity of the anti-oxidative selenoenzyme glutathione peroxidase(GPx) in insulin-deficient Ins2(Akita) mice and type 2 diabetic obese db/db mice in context of diabetic nephropathy. Methods: Protein carbonylation, GPx expression and activity were examined in kidney tissue and lysates by common histological and protein biochemical methods. Results: In kidneys of Ins2(Akita) mice, carbonylated proteins, GPx-1 and GPx-4 expression were mainly detected in podocytes and mesangial cells. GPx activity was increased in kidney cortex homogenates of these mice. Remarkably, young animals did not show a concomitant increase in GPx expression but enhanced GPx carbonylation. No carbonylation-dependent modification of GPx activity was detected in db/db mice. In cultured podocytes hyperglycemia induced an increase in GPx expression but had no effect on activity or carbonylation. In kidney tissue sections of type 1 or type 2 diabetes patients, GPx-1 and GPx-4 expression but not overall protein carbonylation was significantly decreased. Conclusions: These results indicate the existence of a threshold for beneficial carbonylation-dependent redox signaling during the progression of diabetic nephropathy. (C) 2017 Elsevier Inc. All rights reserved.

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