Abstract
ABSTRACT The immunoglobulin superfamily is the most abundant family of cell surface molecules, accounting for 50% of leukocyte surface glycoproteins. This evolutionary success story is thought to be due to the stability of the Ig domain, which is able to resist the harsh proteolytic and oxidative environment of the extracellular world. By mutation and selection, the Ig domain has evolved to serve many different functions including: receptors for growth factors (CSF-1 receptor, PDGF receptor, FGF receptors); receptors for the Fc region of Ig (IgG receptors; CD 16, CD32, CD64; CD89 IgA receptor); and as adhesion molecules, which now seems to be the function of the majority (CD2/CD58, CD28 and CTLA4, which bind to B7 and B70; CD4/class II, CD8/class I, CD31/CD31, CD50 (ICAM-3)/LFA-1, CD54 (ICAM-1)/LFA-1, CD102 (ICAM-2)/LFA-1, CD106 (VCAM)/VLA-4, NCAM/NCAM. L1, MAG, TAG-1, CEA) (Springer, 1990).
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
