Molecular and cellular effects of gold nanoparticles treatment in experimental diabetic myopathy

• DOI: 10.1016/j.heliyon.2022.e10358
• Publication Date: 2022-08-21T13:43:58Z
• Authors: Aseel Al-Shwaheen; Alaa A.A. Aljabali; Ghada Alomari; Mazhar Al Zoubi; Walhan Alshaer; Bahaa Al-Trad; Murtaza M. Tambuwala
• Keywords: H1-99; 0303 health sciences; Science (General); 610; H812 Pharmaceutical Engineering; Skeletal muscle; H812 - Pharmaceutical engineering; Diabetic myopathy; A100 - Pre-clinical medicine; 620; 3. Good health; Social sciences (General); Q1-390; 03 medical and health sciences; Diabetes mellitus; Nanomedicine; Gold nanoparticles; A100 Pre-clinical Medicine; Research Article

This study aims to address the effects of gold nanoparticles (AuNPs) on diabetic myopathy in streptozotocin (STZ)-induced diabetic rats.Adult male rats were separated into three groups (n = 15): non-diabetic control (ND), diabetic (D), and diabetic treated with AuNPs (2.5 mg/kg, D + AuNPs) intraperitoneally for 4 weeks. A single injection of 50 mg/kg STZ was used to induce diabetes.Treatment with AuNPs lowered blood glucose levels. Skeletal muscle mRNA expression of two muscle-specific E3 ubiquitin-ligases enzymes, F-box-only protein 32 (FBXO32) and muscle RING-finger protein-1 (MuRF1) were upregulated in the D group. Diabetic rats showed significant increases in the skeletal muscle expression levels of plasminogen activator inhibitor-1 (PAI-1), tumor necrosis factor-α (TNF-α), transforming growth factor-β1 (TGF-β1), and a decrease in glucose transporter 4 (GLUT4) expression. Superoxide dismutase (SOD) activity decreased and malondialdehyde (MDA) level increased in skeletal muscles of D group. Compared to the D group, expression levels of FBXO32, MuRF1, PAI-1 TNF-α, and TGF-β1 were decreased in the D + AuNPs group, and mRNA of GLUT4 increased. Furthermore, in D + AuNPs group, skeletal muscle MDA levels decreased while SOD activity increased.In experimental models, AuNPs can ameliorate muscle atrophy by reducing hyperglycemia, inflammation, and oxidative stress, and by suppressing the ubiquitin-proteasome proteolytic process.