Advanced glycation end-products induce skeletal muscle atrophy and dysfunction in diabetic mice via a RAGE-mediated, AMPK-down-regulated, Akt pathway

• Published in: The Journal of pathology Vol. 238; no. 3; pp. 470 - 482
• Main Authors: Chiu, Chen-Yuan, Yang, Rong-Sen, Sheu, Meei-Ling, Chan, Ding-Cheng, Yang, Ting-Hua, Tsai, Keh-Sung, Chiang, Chih-Kang, Liu, Shing-Hwa
• Format: Journal Article
• Language: English
• Published: Chichester, UK John Wiley & Sons, Ltd 01.02.2016; Wiley Subscription Services, Inc
• Subjects: advanced glycation end-products; Aged; alagebrium chloride; AMP-Activated Protein Kinases - metabolism; Animals; Atrophy - etiology; Atrophy - pathology; Case-Control Studies; Diabetes Mellitus - etiology; Diabetes Mellitus, Experimental - etiology; diabetic myopathy; Down-Regulation; Glycation End Products, Advanced - metabolism; Humans; Male; MAP Kinase Signaling System - physiology; Mice; Muscle Fatigue - physiology; Muscle Fibers, Skeletal - pathology; Muscle Proteins - metabolism; Muscle Weakness - etiology; Muscle Weakness - pathology; Muscle, Skeletal - pathology; Muscle, Skeletal - physiology; Muscular Diseases - etiology; Muscular Diseases - pathology; Receptor for Advanced Glycation End Products - physiology; Regeneration - physiology; Signal Transduction - physiology; SKP Cullin F-Box Protein Ligases - metabolism; Thiazoles - pharmacology; alagebrium chloride; diabetic myopathy; advanced glycation end-products

Diabetic myopathy, a less studied complication of diabetes, exhibits the clinical observations characterized by a less muscle mass, muscle weakness and a reduced physical functional capacity. Accumulation of advanced glycation end‐products (AGEs), known to play a role in diabetic complications, has...