Earticle

초록

영어

When cellular glucose concentrations fall below normal levels, in general the extent of protein O-GlcNAc modification decreases. However, recent reports demonstrated increased GlcNAcylation by glucose deprivation in HepG2 and Neuro-2a cells. Here, we report increased O-GlcNAcylation in non-small cell lung carcinoma A549 cells and various other cells in response to glucose deprivation. Although the level of O-GlcNAc transferase was unchanged, the enzyme contained less O-GlcNAc and its activity was increased. Moreover, O-GlcNAcase activity was reduced. The studied cells contain glycogen and we show that its degradation in response to glucose deprivation provides a source for UDP-GlcNAc required for increased O-GlcNAcylation under this condition. This required active glycogen phosphorylase and resulted in increased glutamine: fructose-6-phosphate midotransferase, the first and rate-limiting enzyme in the hexosamine biosynthetic athway. Interestingly, glucose deprivation reduced the amount of phosphofructokinase 1, a regulatory glycolytic enzyme, and blocked ATP synthesis. These findings suggest that glycogen is the source for increased O-GlcNAcylation but not for generating ATP in response to glucose deprivation and that this may be useful for cancer cells to survive.

저자

• Jeong Gu Kang [ Dept. of Biology program, Yonsei University ]
• Sang Yoon Park [ Dept. of Biology program, Yonsei University ]
• Suena Ji [ Dept. of Biology program, Yonsei University ]
• Insook Jang [ Dept. of Biology program, Yonsei University ]
• Sujin Park [ Dept. of Biology program, Yonsei University ]
• Jong In Yook [ Oral Pathology, program, Yonsei University ]
• Yong-Il Park [ Oral Pathology, program, Yonsei University ]
• Jürgen Roth [ WCU program, Yonsei University ]
• Jin Won Cho [ Dept. of Biology program, Yonsei University ]

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간행물

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• 간행물명

  한국당과학회 학술대회

• 간기

  연간

• 수록기간

  2006~2022

• 십진분류

  KDC 517 DDC 614