Integrin alpha-3 is a protein encoded by a gene ITGA3 in humans. ITGA3 is integrin α subunit. It is the impact of factors such as α3β1 integrin Liling half duplex, which plays a role in neuronal migration and corticogenesis and one beta subunit together, and netrin-1. ITGA3 encodes the integrin alpha 3 chain. Integrin is a heterodimer integral membrane protein consisting of one α and β chain from the chain. The alpha chain 3, to form integrins interact with extracellular matrix proteins numerous disulfide-bonded extracellular domain undergoes post-translational cleavage to prepare the heavy and light chains are bonded to R 1. (Activation) antigen 3 (“VLA-3 ‘), antigen 2 often (” VCA-2’), extracellular matrix receptor 1 (“ECMR1”), and the galactoprotein B3 very slow alpha 3 beta 1 integrin are different but are known (“GAPB3”). That it interacts with FHL2 and TSPAN4, LGALS8, CD9 has been shown to CD49c.
This protein gene encodes belong to the integrin family. Integrin is a heterodimer integral membrane protein consisting of one α chain and β chain, and because the function as a cell surface adhesion molecule. This gene, α3 to receive post-translational cleavage of the extracellular domain to obtain heavy and light chains disulfide bond is coupled to one subunit β to form an integrin that interacts with extracellular matrix proteins of many I encodes a subunit. transcript variants that are alternatively spliced encoding different isoforms have been identified for this gene.
Members (VLA-3), the integrin family of cell adhesion receptors α 3 β 1, can function as a receptor fibronectin, laminin, and collagen. CDNA clones to the partial human α3 subunit (2.4 kilobytes) is selected from the screening of endothelial cell lambda GT11 DNA library of specific antibodies. Thereafter, having a total length of 4,6 KB from various cDNA libraries, cDNA clones overlapping some were obtained. is expressed on the surface of Chinese hamster ovary 3-α of cDNA was reconstructed set by α-3 is – after transfected with specific monoclonal antibodies, suggesting that the DNA is genuine are. 32 residues in this array, and a long extracellular domain (residues 959), transmembrane domain (residues 28), an open reading encoding amino acids 1051 (s), including a signal peptide short cytoplasmic segment (32 residues) is a frame. ,3-Α-amino acid sequence is similar to integrin α subunits of other cut by the closest match α6 sequence (37%) typically 37-25 similar to that of the α-subunit domain (20% except 15, the I domain sequence itself) is that I am less than a percent. The position of cysteine residues in 18 19 minutes, such characteristics, and other α-subunit () 3 (b) the general structure DX (D / N) × (D / N) GXXD, the (c) The predicted transmembrane region is a metal binding domain One potential. Mass calculated from the amino acid sequence of α-3 is 113 505. 89% identical to hamster galactoprotein b3, and these polypeptides are 70% similar to the mean chicken strips 2 CSAT partial protein antigen sequence to be a homologue of the human α3 sequence of the human α3.
Is a cell surface glycoprotein of 24-27 kDa that can be associated with adhesion and migration of the Schwann cells CD9 molecule. In this study, I examined the expression of human CD9 in extravillous trophoblast invasion in the endometrium between the placenta and transplantation. Rather than a column of cells of the placenta during early pregnancy, CD9 was detected by immunohistochemistry in extravillous trophoblast in villous trophoblast. The term of the second and third, and glued laeve fetal membranes term placenta CD9 and is expressed in extravillous trophoblast base plate advanced placenta. Molecular weight of CD9 in smooth chorion, shows that blotting of 27 kDa in the western part. It is detected in the villus laeve by (RT-PCR) reverse transcription polymerase chain reaction CD9 mRNA. Protein was purified and Western blot α5 monoclonal antibodies and α3 of villi laeve by affinity chromatography with an anti-integrin CD9, revealed that it binds both integrins. These data suggest that CD9 related molecules differentiation is present in extravillous trophoblasts. In connection with the integrin α5, which can be adjusted until trophoblast invasion has been proposed, which may be involved in invasion of trophoblast fetal maternal interface CD9.
LIM protein contains two double zinc finger structures of one or more mediating specific contact between proteins involved in the formation of multi-protein complex (LIM domain). We, LIM domain protein of only LIM DRAL/FHL2, four and a half years to be associated with integrin β subunit some α3A, α3B, and α7A, as after over-expressed in human and yeast two-hybrid analysis cells are reported to be able to. C-terminal region is important for connecting the DRAL/FHL2 α or having patterns NXXY conservative integrin β subunits following the proximal region of the holding film integrin subunit immediately amino acid sequence. In addition, it is associated with other molecules that bind to the cytoplasmic domain of integrin subunit α and the DRAL/FHL2 itself. The DRAL/FHL2 deletion analysis, the combination of LIM LIM domain or domains revealed that connecting the different proteins in particular. And facts These results that are positioned suggest that full length DRAL/FHL2, an adapter / docking protein which is involved in integrin signaling pathways, complex cell adhesion together.
This protein gene encodes belong to the integrin family. Integrin is a heterodimer integral membrane protein consisting of one α chain and β chain, and because the function as a cell surface adhesion molecule. This gene, α3 to undergo post-translational cleavage of the extracellular domain in order to obtain heavy and light chain disulfide bond is coupled to one subunit β to form an integrin that interacts with extracellular matrix proteins of many I encodes a subunit. transcript variants that are alternatively spliced encoding different isoforms have been identified for this gene.