KAI DANG, HAFIZ MUHAMMAD UMER FAROOQ, YUAN GAO, XIAONI DENG, AIRONG QIAN^*

BIOCELL, Vol.47, No.2, pp. 269-281, 2023, DOI:10.32604/biocell.2023.023766

Abstract As a key coordinator of metabolism, AMP-activated protein kinase (AMPK) is vitally involved in skeletal muscle maintenance. AMPK exerts its cellular effects through its function as a serine/threonine protein kinase by regulating many downstream targets and plays important roles in the development and growth of skeletal muscle. AMPK is activated by phosphorylation and exerts its function as a kinase in many processes, including synthesis and degradation of proteins, mitochondrial biogenesis, glucose uptake, and fatty acid and cholesterol metabolism. Skeletal muscle atrophy is a result of various diseases or disorders and is characterized by a decrease in muscle mass. The pathogenesis… More >

KIVANÇ ERGEN^*, MUHAMMET BEKTAŞ^**, SINA GÖKÇE^**, RÜSTEM NURTEN^**

BIOCELL, Vol.31, No.1, pp. 61-66, 2007, DOI:10.32604/biocell.2007.31.061

Abstract Eukaryotic elongation factor 2 (eEF-2) can undergo ADP-ribosylation in the absence of diphtheria toxin. The binding of free ADP-ribose and endogenous transferase-dependent ADP-ribosylation were distinct reactions for eEF-2, as indicated by different findings. Incubation of eEF-2 tryptic fragment 32/33 kDa (32F) with NAD was ADP-ribosylated and gave rise to the covalent binding of ADP-ribose to eEF-2. 32F was revealed to be at the C-terminal by Edman degradation sequence analysis.
In our study, the elution of 32F from SDS-PAGE was ADP-ribosylated both in the presence and absence of diphtheria toxin. These results suggest that endogenous ADP-ribosylation of 32F might be related… More >