Title : Specific O-GlcNAc modification at Ser-615 modulates eNOS function.

Pub. Date : 2020 Sep

PMID : 32863226






5 Functional Relationships(s)
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1 Specific O-GlcNAc modification at Ser-615 modulates eNOS function. Serine O-linked N-acetylglucosamine (GlcNAc) transferase Homo sapiens
2 We recently demonstrated that glucose dysregulation results in augmented protein serine/threonine hydroxyl-linked N-Acetyl-glucosamine (O-GlcNAc) modification in IPAH. Serine O-linked N-acetylglucosamine (GlcNAc) transferase Homo sapiens
3 Here we show that increased protein O-GlcNAc occurs on eNOS in PAH and Ser-615 appears to be a novel site of O-GlcNAc modification resulting in reduced eNOS dimerization. Serine O-linked N-acetylglucosamine (GlcNAc) transferase Homo sapiens
4 Here we show that increased protein O-GlcNAc occurs on eNOS in PAH and Ser-615 appears to be a novel site of O-GlcNAc modification resulting in reduced eNOS dimerization. Serine O-linked N-acetylglucosamine (GlcNAc) transferase Homo sapiens
5 Here we demonstrate a previously unidentified regulatory mechanism of eNOS whereby the O-GlcNAc modification of Ser-615 results in reduced eNOS activity and endothelial dysfunction under conditions of glucose dysregulation. Serine O-linked N-acetylglucosamine (GlcNAc) transferase Homo sapiens