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A Possible Modulation Mechanism of Intramolecular and Intermolecular Interactions for NCAM Polysialylation and Cell Migration.
Lu, Bo; Liu, Xue-Hui; Liao, Si-Ming; Lu, Zhi-Long; Chen, Dong; Troy Ii, Frederic A; Huang, Ri-Bo; Zhou, Guo-Ping.
Afiliación
  • Lu B; The National Engineering Research Center for Non-Food Biorefinery, Guangxi Academy of Sciences, Nanning, Guangxi 530007, China.
  • Liu XH; Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
  • Liao SM; The National Engineering Research Center for Non-Food Biorefinery, Guangxi Academy of Sciences, Nanning, Guangxi 530007, China.
  • Lu ZL; The National Engineering Research Center for Non-Food Biorefinery, Guangxi Academy of Sciences, Nanning, Guangxi 530007, China.
  • Chen D; The National Engineering Research Center for Non-Food Biorefinery, Guangxi Academy of Sciences, Nanning, Guangxi 530007, China.
  • Troy Ii FA; Department of Biochemistry and Molecular Medicine, University of California School of Medicine, Davis, CA, 95817, United States.
  • Huang RB; The National Engineering Research Center for Non-Food Biorefinery, Guangxi Academy of Sciences, Nanning, Guangxi 530007, China.
  • Zhou GP; Life Science and Biotechnology College, Guangxi University, Nanning, Guangxi 530004, China.
Curr Top Med Chem ; 19(25): 2271-2282, 2019.
Article en En | MEDLINE | ID: mdl-31648641
Polysialic acid (polySia) is a novel glycan that posttranslationally modifies neural cell adhesion molecules (NCAMs) in mammalian cells. Up-regulation of polySia-NCAM expression or NCAM polysialylation is associated with tumor cell migration and progression in many metastatic cancers and neurocognition. It has been known that two highly homologous mammalian polysialyltransferases (polySTs), ST8Sia II (STX) and ST8Sia IV (PST), can catalyze polysialylation of NCAM, and two polybasic domains, polybasic region (PBR) and polysialyltransferase domain (PSTD) in polySTs play key roles in affecting polyST activity or NCAM polysialylation. However, the molecular mechanisms of NCAM polysialylation and cell migration are still not entirely clear. In this minireview, the recent research results about the intermolecular interactions between the PBR and NCAM, the PSTD and cytidine monophosphate-sialic acid (CMP-Sia), the PSTD and polySia, and as well as the intramolecular interaction between the PBR and the PSTD within the polyST, are summarized. Based on these cooperative interactions, we have built a novel model of NCAM polysialylation and cell migration mechanisms, which may be helpful to design and develop new polysialyltransferase inhibitors.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Ácidos Siálicos / Movimiento Celular / Moléculas de Adhesión de Célula Nerviosa Límite: Animals / Humans Idioma: En Revista: Curr Top Med Chem Asunto de la revista: QUIMICA Año: 2019 Tipo del documento: Article País de afiliación: China Pais de publicación: Emiratos Árabes Unidos
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Ácidos Siálicos / Movimiento Celular / Moléculas de Adhesión de Célula Nerviosa Límite: Animals / Humans Idioma: En Revista: Curr Top Med Chem Asunto de la revista: QUIMICA Año: 2019 Tipo del documento: Article País de afiliación: China Pais de publicación: Emiratos Árabes Unidos