Diabetic conditions modulate the adenosine monophosphate-activated protein kinase of podocytes

Diabetic conditions modulate the adenosine monophosphate-activated protein kinase of podocytes
5 amino 4 imidazolecarboxamide riboside; advanced glycation end product; hydroxymethylglutaryl coenzyme A reductase kinase; hydroxymethylglutaryl coenzyme A reductase kinase activator; metformin; animal cell; animal tissue; article; cell damage; controlled study; cytoplasm; disease course; enzyme localization; enzyme phosphorylation; enzyme regulation; enzyme repression; experimental diabetic neuropathy; immunoblotting; immunofluorescence; intranuclear space; mouse; nonhuman; podocyte; priority journal; rat; streptozotocin-induced diabetes mellitus
Issue Date
Kidney Research and Clinical Practice, v.33, no.1, pp.26 - 32
Background Adenosine monophosphate-activated protein kinases (AMPKs), as a sensor of cellular energy status, have been known to play an important role in the pathophysiology of diabetes and its complications. Because AMPKs are known to be expressed in podocytes, it is possible that podocyte AMPKs could be an important contributing factor in the development of diabetic proteinuria. We investigated the roles of AMPKs in the pathological changes in podocytes induced by high-glucose (HG) and advanced glycosylation end products (AGEs) in diabetic proteinuria. Methods We prepared streptozotocin-induced diabetic renal tissues and cultured rat and mouse podocytes under diabetic conditions with AMPK-modulating agents. The changes in AMPK�� were analyzed with confocal imaging and Western blotting under the following conditions: (1) normal glucose (5mM, =control); (2) HG (30mM); (3) AGE-added; or (4) HG plus AGE-added. Results The density of glomerularphospho-AMPK�� in experimental diabetic nephropathy decreased as a function of the diabetic duration. Diabetic conditionsincluding HG and AGE changed the localization of phospho-AMPK�� from peripheral cytoplasm to internal cytoplasm and peri- and intranuclear areas in podocytes. HG reduced the AMPK�� (Thr172) phosphorylation of rat podocytes, and similarly, AGEs reduced the AMPK�� (Thr172) phosphorylation of mouse podocytes. The distributional and quantitative changes in phospho-AMPK�� caused by diabetic conditions were preventable using AMPK activators, metformin, and 5-aminoimidazole-4-carboxamide-1��-riboside. Conclusion We suggest that diabetic conditions induce the relocation and suppression of podocyte AMPK��, which would be a suggestive mechanism in diabetic podocyte injury. ? 2014. The Korean Society of Nephrology. Published by Elsevier. All rights reserved.
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