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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 발행연도
- 2005.1
- 수록면
- 220 - 229 (10page)
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It has been known that O-linked β-N-acetylgluco-samine (O-GlcNAc) modification of proteins plays an important role in transcription, translation, increased flux of glucose through the hexosa-mine biosynthetic pathway (HBP) and increased O-GlcNAc modification of protein have been sug-gested as one of the causes in the development of insulin resistance. However, it is not clear at the molecular level, how O-GlcNAc protein modi-fication results in substantial impairment of in-sulin signaling. To clarify the asociation of O- GlcNAc protein modification and insulin resist-ance in rat primary adipocytes, we treated the adipocytes with O-(2-acetamido-2deoxy-Dpyranosylidene)amino-N-phenylcarbamate (PUGNAc), a potent inhibitor of O-GlcNAcase that catalyzes removal of O-GlcNAc from proteins. Prolonged treatment of PUGNAc (10 M for 12 h) increased O-GlcNAc modification on proteins in adipocytes. PUGNAc also drastically decreased insulin-stimulated 2-deoxyglucose (2DG) uptake and GLUT4 translocation in adipocytes, indicat-ing that PUGNAc developed impaired glucose utilization and insulin resistance in adipocytes. Interestingly, the O-GlcNAc modification of IRS-1 and Akt2 was increased by PUGNAc, accom-panied by a partial reduction of insulin-stimulated phosphorylations of IRS-1 and Akt2. The PUGNAc treatment has no effect on the expression level of GLUT4, whereas O-GlcNAc modification of GLUT4 was increased. These results suggest that the increase of O-GlcNAc modification on insulin signal pathway intermediates, such as IRS-1 and Akt2, reduces the insulin-stimulated phosphoryla-tion of IRS-1 and Akt2, subsequently leading to insulin resistance in rat primary adipocytes.
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참고문헌 (27)
참고문헌 신청
/ / A substantialpart of GLUT1 in crude membranes from muscle originatesfrom perineurial sheaths
/ / Mechanismof Ca2+-induced inhibition of insulin-stimulated glucose transport : 3352 ~ 6
/ / Phosphorylation ofthe glucose transporter in rat adipocytes Identification of theintracellular domain at the carboxyl terminus as a target forphosphorylation in intact-c
/ / Potential mechanism of insulinaction on glucose transport in the isolated rat adipose cell Apparent translocation of intracellular transport systems tothe plasma membran
/ 19321-30 / Purification and characterization of anO-GlcNAc selective N-acetyl-beta-D-glucosaminidase from ratspleen cytosol
/ / Mechanismof Ca2+-induced inhibition of insulin-stimulated glucose transport : 3352 ~ 6
/ / Phosphorylation ofthe glucose transporter in rat adipocytes Identification of theintracellular domain at the carboxyl terminus as a target forphosphorylation in intact-c
/ / Potential mechanism of insulinaction on glucose transport in the isolated rat adipose cell Apparent translocation of intracellular transport systems tothe plasma membran
/ 19321-30 / Purification and characterization of anO-GlcNAc selective N-acetyl-beta-D-glucosaminidase from ratspleen cytosol
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