Functions of cell surface galectin-glycoprotein lattices

被引:324
作者
Rabinovich, Gabriel A.
Toscanol, Marta A.
Jackson, Shawn S.
Vasta, Gerardo R.
机构
[1] Inst Biol & Med Expt IBYME, CONICET, Immunopathol Lab, Buenos Aires, DF, Argentina
[2] Univ Buenos Aires, Fac Ciencias Exactas & Nat, Dept Quim Biol, RA-1053 Buenos Aires, DF, Argentina
[3] Univ Maryland, Inst Biotechnol, Ctr Marine Biotechnol, Baltimore, MD 21202 USA
关键词
DIFFERENTIAL GLYCOSYLATION; LEISHMANIA-MAJOR; N-GLYCANS; T-CELLS; PRE-B; BINDING; LECTIN; NEUTROPHILS; ACTIVATION; RECEPTOR;
D O I
10.1016/j.sbi.2007.09.002
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Programmed remodeling of cell surface glycans by the sequential action of specific glycosyltransferases can control biological processes by generating or masking ligands for enclogenous lectins. Galectins, a family of animal lectins with affinity for beta-galactosides, can form multivalent complexes with cell surface glycoconjugates and deliver a variety of intracellular signals to modulate cell activation, differentiation, and survival, Recent efforts involving genetic or biochemical manipulation of O-glycosylation and N-glycosylation pathways, as well as blockade of the synthesis of enclogenous galectins, have illuminated essential roles for galectin-glycoprotein lattices in the control of biological processes including receptor turnover and endocytosis, host-pathogen interactions, and immune cell activation and homeostasis.
引用
收藏
页码:513 / 520
页数:8
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