Melanoma Inhibitory Activity Protein (MIA) is an autocrine growth regulatory protein secreted from chondrocytes and malignant melanoma cells, which was the first discovered member of a family of secreted cytokines termed the MIA/OTOR family. The four known members of this family: MIA, MIA2, OTOR and TANGO each contain a Src homology-3 (SH3)-like domain. MIA acts as a potent tumor cell growth inhibitor for malignant melanoma cells and some other neuroectodermal tumors, including gliomas, in an autocrine fashion and promotes melanoma metastasis by binding competitively to fibronectin and laminin in a manner that results in melanoma cell detachment from the extracellular matrix in vivo. The protein MIA has been shown to represent a very sensitive and specific serum marker for systemic malignant melanoma that might be useful for staging of primary melanomas, detection of progression from localized to metastatic disease during follow-up, and monitoring therapy of advanced melanomas. Elevated levels of MIA may represent a clinically useful marker for diagnosis of melanoma metastasis as well as a potential marker for rheumatoid arthritis.
MHC class I polypeptide-related sequence A, also known as MIC-A, PERB11.1 and MICA, is a single-pass type I membrane protein which belongs to the MHC class I family of MIC subfamily. MICA contains one Ig-like C1-type domain and is expressed on the cell surface, although unlike canonical class I molecules does not seem to associate with beta-2-microglobulin. It is thought that MICA functions as a stress-induced antigen that is broadly recognized by NK cells, NKT cells, and most of the subtypes of T cells. MICA is the ligand for NK cell activating receptor KLRK1/NKG2D. MICA seems to have no role in antigen presentation. MICA leads to cell lysis by binding to KLRK1.
MHC class I chain-related molecules A (MICA) is one of the genes in the HLA class I region, which belongs to the MHC class I family. It is the member of the non-classical class I family that displays the greatest degree of polymorphism. The MICA protein product is expressed on the cell surface, although unlike canonical class I molecules do not seem to associate with beta-2-microglobulin. It is thought that MICA functions as a stress-induced antigen that is broadly recognized by NK cells, NKT cells, and most of the subtypes of T cells. The Natural killer group 2D (NKG2D), a C-type lectin-like activating immunoreceptor, is a receptor of MICA, which was detected on most gamma-delta T cells, CD8+ alpha-beta T cells, and natural killer (NK) cells. Effector cells from all these subsets could be stimulated by the ligation of NKG2D. Engagement of NKG2D activated cytolytic responses of gamma-delta T cells and NK cells against transfectants and epithelial tumor cells expressing MICA. The MICA system is a novel, avidin-free immunohistochemical detection system that provides a significant increase in sensitivity compared to traditional immunodetection systems.
MHC Class I Polypeptide-Related Sequence A (MICA) is a transmembrane glycoprotein that functions as a ligand for human NKG2D. Unlike classical MHC class I molecules, MICA does not form a heterodimer with beta-2-microglobulin. MICA shares 85% amino acid identity with a closely related protein, MICB. MICA acts as a stress-induced self-antigen that is recognized by NK cells, NKT cells, and most of the subtypes of T cells. As a Ligand for the KLRK1/NKG2D receptor, MICA binds to KLRK1 leads to cell lysis. MICA functions as an antigen for gamma delta T cells and is frequently expressed in epithelial tumors. MICA antigens are able to elicit the synthesis of alloantibodies in transplant recipients. Studies have shown that anti-MICA antibodies are associated with acute renal allograft rejection and failure. MICA recognition is involved in tumor surveillance, viral infections, and autoimmune diseases.
MHC class I chain-related molecules A (MICA) is one of the genes in the HLA class I region, which belongs to MHC class I family. It is the member of the non-classical class I family that displays the greatest degree of polymorphism. The MICA protein product is expressed on the cell surface, although unlike canonical class I molecules does not seem to associate with beta-2-microglobulin. It is thought that MICA functions as a stress-induced antigen that is broadly recognized by NK cells, NKT cells, and most of the subtypes of T cells. The Natural killer group 2D (NKG2D), a C-type lectin-like activating immunoreceptor, is a receptor of MICA, which was detected on most gammadelta T cells, CD8+ alphabeta T cells, and natural killer (NK) cells. Effector cells from all these subsets could be stimulated by ligation of NKG2D. Engagement of NKG2D activated cytolytic responses of gammadelta T cells and NK cells against transfectants and epithelial tumor cells expressing MICA. The MICA system is a novel, avidin-free immunohistochemical detection system that provides a significant increase in sensitivity compared to traditional immunodetection systems.
This gene encodes a heavily glycosylated protein which is a ligand for the NKG2D type II receptor. Binding of the ligand activates the cytolytic response of natural killer (NK) cells, CD8 alphabeta T cells, and gammadelta T cells which express the receptor. This protein is stress-induced and is similar to MHC class I molecules, however, it does not associate with an beta-2-microglobulin or bind peptides. Alternative splicing results in multiple transcript variants.
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