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Engineering cellular trafficking via glycosyltransferase‐programmed stereosubstitution
Author(s) -
Sackstein Robert
Publication year - 2012
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.2011.06421.x
Subject(s) - selectin , microbiology and biotechnology , cd44 , glycoprotein , effector , glycosyltransferase , e selectin , glycolipid , biology , cell , chemistry , cell adhesion molecule , cell adhesion , biochemistry , gene
The proximate hurdle for cell trafficking to any anatomic site is the initial attachment of circulating cells to target tissue endothelium with sufficient strength to overcome prevailing forces of blood flow. E‐selectin, an endothelial molecule that is inducibly expressed at all sites of inflammation, is a potent effector of this primary braking process. This molecule is a member of a family of C‐type lectins known as selectins that bind sialofucosylated glycans displayed on either a protein (i.e., glycoprotein) or lipid (i.e., glycolipid) scaffold. On human cells, the predominant E‐selectin ligand is a specialized glycoform of CD44 known as hematopoietic cell E‐/L‐selectin ligand (HCELL). This review focuses on the biology of HCELL/E‐selectin interactions in cell migration, and discusses the utility and applicability of glycosyltransferase‐programmed stereosubstitution (GPS) for glycoengineering HCELL expression. Without compromising cell viability or native phenotype, this exoglycosylation technology literally “sweetens” CD44, licensing E‐selectin–dependent vascular delivery for all cell‐based therapeutics.