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α2,3-Sialylation regulates the stability of stem cell marker CD133

Identifieur interne : 001629 ( Main/Exploration ); précédent : 001628; suivant : 001630

α2,3-Sialylation regulates the stability of stem cell marker CD133

Auteurs : Fengbiao Zhou [République populaire de Chine] ; Chunhong Cui [République populaire de Chine] ; Yuqing Ge [République populaire de Chine] ; Hong Chen [République populaire de Chine] ; Qiuping Li [République populaire de Chine] ; Zhiyuan Yang [République populaire de Chine] ; Guoqiang Wu [République populaire de Chine] ; Shuhui Sun [République populaire de Chine] ; Kangli Chen [République populaire de Chine] ; Jianxin Gu [République populaire de Chine] ; Jianhai Jiang [République populaire de Chine] ; Yuanyan Wei [République populaire de Chine]

Source :

RBID : ISTEX:CFB4B378E6E6E25980E6039D44EFDC795C3FC29A

Abstract

CD133 is widely used as a marker for the isolation and characterization of normal and cancer stem cells. The dynamic alternation of CD133 glycosylation contributes to the isolation of normal and cancer stem cells, and is supposed to be associated with cell differentiation. Although CD133 has been identified as a N-glycosylated protein, the specific glycosylation status of CD133 remain unclear. Here, we found that CD133 could be sialylated in neural stem cells and glioma-initiating cells, and the sialyl residues attach to CD133 N-glycan terminal via α2,3-linkage. Furthermore, desialylation of CD133 by neuraminidase specifically accelerates its degradation in lysosomes-dependent pathway. Taken together, our results characterized CD133 as an α2,3-sialylated glycoprotein and revealed that the sialylation modification contributes to the stability of CD133 protein, providing clues to understanding the function of CD133 molecular and to understanding the utility of glycosylated CD133 epitopes in defining neural stem cells and tumour-initiating cells.

Url:
DOI: 10.1093/jb/mvq062


Affiliations:


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<div type="abstract">CD133 is widely used as a marker for the isolation and characterization of normal and cancer stem cells. The dynamic alternation of CD133 glycosylation contributes to the isolation of normal and cancer stem cells, and is supposed to be associated with cell differentiation. Although CD133 has been identified as a N-glycosylated protein, the specific glycosylation status of CD133 remain unclear. Here, we found that CD133 could be sialylated in neural stem cells and glioma-initiating cells, and the sialyl residues attach to CD133 N-glycan terminal via α2,3-linkage. Furthermore, desialylation of CD133 by neuraminidase specifically accelerates its degradation in lysosomes-dependent pathway. Taken together, our results characterized CD133 as an α2,3-sialylated glycoprotein and revealed that the sialylation modification contributes to the stability of CD133 protein, providing clues to understanding the function of CD133 molecular and to understanding the utility of glycosylated CD133 epitopes in defining neural stem cells and tumour-initiating cells.</div>
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