Title : SENP2 is vital for optimal insulin signaling and insulin-stimulated glycogen synthesis in human skeletal muscle cells.

Pub. Date : 2021

PMID : 34909683






6 Functional Relationships(s)
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Protein Name
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1 SENP2 is vital for optimal insulin signaling and insulin-stimulated glycogen synthesis in human skeletal muscle cells. Glycogen SUMO specific peptidase 2 Homo sapiens
2 Acute (4 h) oleic acid oxidation was reduced in SENP2-knockdown (SENP2-KD) cells compared to control cells, with no difference in uptake. Oleic Acid SUMO specific peptidase 2 Homo sapiens
3 After prelabeling (24 h) with oleic acid, total lipid content and incorporation into triacylglycerol was decreased, while incorporation into other lipids, as well as complete oxidation and beta-oxidation was increased in SENP2-KD cells. Oleic Acid SUMO specific peptidase 2 Homo sapiens
4 Basal glucose uptake (i.e., not under insulin-stimulated conditions) was higher in SENP2-KD cells, whereas oxidation was similar to control myotubes. Glucose SUMO specific peptidase 2 Homo sapiens
5 Further, basal glycogen synthesis was not different in SENP2-KD myotubes, but both insulin-stimulated glycogen synthesis and AktSer473 phosphorylation was completely blunted in SENP2-KD cells. Glycogen SUMO specific peptidase 2 Homo sapiens
6 In conclusion, SENP2 plays an important role in fatty acid and glucose metabolism in human myotubes. Fatty Acids SUMO specific peptidase 2 Homo sapiens