Background:The pathophysiological importance of autophagy in renal tubules during the development of diabetic nephropathy (DN) has been implicated. Results: Autophagy was inactivated because lysosomal membrane permeabilization and lysosomal dysfunction were triggered by advanced glycation end products. Conclusion:The autophagy-lysosome pathway is disrupted in renal tubules in DN. Significance:The findings open a new field for studying the mechanisms of DN.
Transforming growth factor beta1 (TGF-β1) is regarded as the important factor in many fibrotic kidney diseases. Autophagy is a vital mechanism which maintains intracellular homeostasis in eukaryotic cells and involves in various renal physiologic and pathological processes. Current studies indicate that autophagy in renal tubular epithelial cells serves as a renoprotective mechanism which modulates the course of diverse kidney disease. Thus, this review aims to show the possible linkage between TGF-β1 and autophagy in the renal tubular epithelial cells. RevieW ARTiCLeCheck for updates for degradation. Free amino acids and fatty acids generated on degradation of cellular components are recycled to synthesize new proteins and bioenergetic supplies of the cell. Thus, under normal physiological conditions, basal autophagy plays a homeostatic role that maintains cellular homeostasis and quality control. Autophagy is induced in response to many stressors including cell starvation, growth factor deprivation, hypoxia, and oxidant injury. Under stress conditions, autophagy induction is regarded as an adaptive role to ensure cell survival. The formation of an autophagosome is initiated by several autophagic protein complexes, including the unc-51-like kinase 1 or 2 (ULK1 or ULK2) complex, the class III phosphatidylinositol 3-kinase complex, Atg12-Atg5-Atg16 conjugation, and lipidation of microtubule-associated protein 1 light chain 3 (LC3) with phosphatidylethanolamine to form LC3-II. The elongation and expansion steps in autophagosome formation involve two ubiquitin-like proteins, Atg12 and Atg8/LC3-II. The conjugation of Atg12 to Atg5 is catalyzed by Atg7 and Atg10 (E1-and E2-like enzymes, respectively) to form covalently linked Atg12-Atg5. Following formation of the Atg12-Atg5 conjugate, Atg16L non-covalently associates with this conjugate to produce the Atg12-Atg5-Atg16 multimeric complex. These conjugation systems are recruited to the phagophore membrane for phagophore expansion to complete the formation of the autophagosome. Once the autophagosome is formed, most of the Atg proteins are dissociated, which allows fusion with the lysosome
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