The potential role of sialoadhesin as a macrophage recognition molecule in health and disease |
| |
Authors: | Paul R Crocker Adele Hartnell James Munday Deepa Nath |
| |
Affiliation: | (1) ICRF Laboratories, Institute of Molecular Medicine, University of Oxford, John Radcliffe Hospital, Headington Oxford, OX3 9DU, UK |
| |
Abstract: | Sialoadhesin is a macrophage-restricted transmembrane glycoprotein of 185 kDa that mediates cell–cell interactions through recognition of Neu5Acα2,3Gal in glycoconjugates. The extracellular region of sialoadhesin is composed of seventeen immunoglobulin-like domains, of which the amino-terminal two are highly-related structurally and functionally to the amino-terminal domains of CD22, myelin associated glycoprotein and CD33. These proteins, collectively known as the sialoadhesin family, are able to mediate sialic acid-dependent binding with distinct specificities for both the type of sialic acid and its linkage to subterminal sugars. In this review we discuss our recent studies on sialoadhesin and suggest how this molecule may contribute to a range of macrophage functions, both under normal conditions as well as during inflammatory reactions. Abbreviations: Ig, immunoglobulin; CEA, carcinoembryonic antigen; MAG, myelin associated glycoprotein; SMP Schwann cell myelin protein; mAb, monoclonal antibody; Chinese hamster ovary (CHO); UTR, untranslated region This revised version was published online in November 2006 with corrections to the Cover Date. |
| |
Keywords: | sialic acid cell adhesion immunoglobulin inflammation macrophage |
本文献已被 SpringerLink 等数据库收录! |
|