By Jeffrey V. Ravetch (auth.), Max D. Cooper M.D., Toshiyuki Takai Ph.D., Jeffrey V. Ravetch M.D., Ph.D. (eds.)
A outstanding spectrum of novel immunoreceptors sharing comparable immunoglobulin-like domain names and signaling capability has been pointed out in recent times. those receptors have attracted common curiosity simply because they resemble the TCR, BCR, and FcR complexes of their skill to function activating or inhibitory receptors at the cells that endure them. in addition, they're good located to impact either innate and adaptive immunity. the whole variety of ligands for those new receptor households continues to be no longer recognized, and realizing in their physiological roles is much from entire. This quantity is the 1st try and summarize and spotlight all recognized facets of immunoglobulin-like receptors, supplying a topical review of the jobs and attribute positive factors of the immunoglobulin-like receptors and similar molecules within the immune method. Researchers in immunology, molecular biology, mobilephone biology, scientific drugs, and pharmacology will locate this e-book invaluable.
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Extra resources for Activating and Inhibitory Immunoglobulin-like Receptors
One of the first receptors to be characterized, Ly49A , was found to bind MHC class I molecules and inhibit the capacity of NK cells to kill their targets (Karlhofer et al. 1992). It is now clear that there is structural diversity in these receptors (Yokoyama 1998). In mice, most of the defined NK cell receptors belong to the C-type lectin superfamily. While it is still controversial whether these receptors bind carbohydrates, they nevertheless bear a structural relationship to molecules that bind carbohydrates in a Ca't-dependent manner (Tormo et al.
1990). FcyRs belong to the immunoglobulin (lg) superfamily and have been classified into three classes : FcyRI (CD64) , also known as the high affinity receptor (Kd -] O-xM), contains three Ig-like domains in the extracellular region while FcyRII (CD32) and FcyRIII (CD 16), the low affinity receptor s (Kd -1O-0 M), both contain two Ig-like domains . FcyRII is expressed on nearly all immunocompetent cells while the transmembrane form of FcyRIII (FcyRIIIa) is expressed on natural killer (NK) cells , macrophages and mast cells.
2000) . Therefore, decreased FcaR expression on monocytes could result from the release of soluble FcaR from the cell surface. The FeaR promoter polymorph isms may be involved in one of the mech anism s underlying susceptibility to and/or pathogenesis of IgAN through increasing FeaR gene expre ssion , which might lead to increase soluble FeaR. Acknowledgments We thank Drs. Shoichi Suzuki and Michael J. I . We also thank Dr. Shinsaku Togo for experimental help. This work was supported in part by Grants in Aids from the Japanese Ministries of Education, Health and Welfare, and EnvironmentAgency.
Activating and Inhibitory Immunoglobulin-like Receptors by Jeffrey V. Ravetch (auth.), Max D. Cooper M.D., Toshiyuki Takai Ph.D., Jeffrey V. Ravetch M.D., Ph.D. (eds.)