CD103 is a type I transmembrane glycoprotein known as αE integrin or Integrin αIEL chain. It belongs to the integrin family and is primarily found on intestinal intraepithelial lymphocytes (IEL). CD103 is also expressed on a subpopulation of lamina propria T cells, epithelial dendritic cells, lamina propria-derived dendritic cells, and a small subset of peripheral lymphocytes. T regulatory cells express high level of CD103. The CD103 expression on lymphocytes can be induced upon activation and TGF-β stimulation. In association with integrin β7, CD103 is expressed as αE/β7 heterodimer. Mature CD103 protein can be cleaved into 2 chains, a 150 kD (C-terminal) chain and a 25 kD (N-terminal) chain, which remain linked by disulfide bonds. CD103 binds to E-cadherin and mediates homing of lymphocytes to the intestinal epithelium.
Endoglin (ENG, CD105) is a homodimeric cell membrane glycoprotein of 180 kDa, composed of disulphide-linked subunits of 90-95 kDa. Endoglin is a proliferation-associated and hypoxia-inducible protein mainly expressed on vascular endothelial cells. It acts as an accessory receptor for transforming growth factor beta (TFG-β) and is involved in vascular development and remodelling. The important role of Endoglin in angiogenesis and in tumor progression makes it an ideal target for antiangiogenic therapy and a good marker for tumor prognosis.
CD106 is a 110 kD glycosylphosphatidylinositol (GPI)-linked transmembrane protein, also known as VCAM-1 and INCAM-110. It is constitutively expressed on bone marrow stromal cells, myeloid progenitors, splenic dendritic cells, activated endothelial cells, as well as some lymphocytes. CD106 expression can be upregulated on endothelial cells by inflammatory cytokines. CD106 is involved in adhesion and acts as a counter-receptor for VLA-4 (α4/β1 integrin) and LPAM-1 (α4/β7 integrin).
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