Integrin α-IIb of is a protein encoded by a gene ITGA2B in humans. ITGA2B has code and integrin α chain 2b. Integrin is a heterodimer integral membrane protein consisting of one α and β chain from the chain. To form the expression fibrinogen receptor on platelets has an important role in blood coagulation, α chain 2b undergoes post-translational cleavage in order to obtain heavy and light chain disulfide bond is bonded to the beta 3 . Mutations that affect the outcome in this role Grants Man. That in addition to the adhesive, is involved in signal transduction integrins to cell surface through is known.

ITGA2B has code and integrin α chain 2b. Integrin is a heterodimer integral membrane protein consisting of one α and β chain from the chain. The α-chain 2b, to form the expression fibronectin receptor in platelets, heavy and light chain disulfide bond is bonded to the β 3 undergoes post-translational cleavage obtained has an important role in blood coagulation. Mutations that affect the outcome in this role Grants Man. That in addition to the adhesive, is involved in signal transduction integrins to cell surface through is known.

Modification of the cytoplasmic tail of the integrin αIIbβ3 integrin plays an important role in signal transduction of platelets. We for protein binding to αIIb cytoplasmic tail by a yeast two-hybrid assay with the DNA library proteins ancient ubiquitous protein 1 (Aup1) were identified expressing the ubiquitous human cells and megakaryocytes derived cell lines , Search. Observation of cells expressing Aup1 significant red fluorescent protein UT7/TPO showed localization in the cytoplasm. That about 40% of it is to form a complex with αIIbAup1 has been shown that immunoprecipitation of cells from antibody UT7/TPO Aup1. Glutathione and αIIb cytoplasmic tail peptides – related research and Aup1 related protein transferase revealed low affinity (KD = 90 mm). Connection has shown a Aup1 the cytoplasmic tail of the integrin α subunits other after the yeast two-hybrid analysis. The binding studies with purified a Aup1 various glutathione S-transferase-αIIbcytoplasmic tail peptide is conserved among the integrin α-subunit sequences proximal Aup1 film plays an important role in αIIbβ3 signaling integrin outward I made it clear, specific binding of the (KVGFFKR). As has Aup1 field is related to signal transduction, these results indicate the involvement of Aup1 in integrin signaling.

important role, KFR, is recognized in the regulation of platelet activation integrin αIIbβ3 integrin in maintaining the α-integrin cytoplasmic motif. To understand the molecular mechanism of this regulation, we tried to determine the nature of protein interactions in the cell pattern. Synthetic peptide high-density protein expression array for high affinity interaction to (37200 recombinant human protein)-labeled probe, we used the biotin KVGFFKR. I have identified the integrin-binding proteins some potential. Integrin – as an expression on platelets, its affinity for the peptide is highest, further, protein, chloride channel regulatory proteins, ICln Such characterized. We, PCR, Western blot, immunohistochemistry, and to verify the presence of ICln in human platelets by the co-relation between the integrin αIIbβ3 by surface plasmon resonance. Affinity of this reaction is 24.4 nM at 82.2 ± cell-free assay. Indicates a physiologically relevant, this interaction, co-immunoprecipitation with ICln integrin αIIbβ3 platelet lysate. In addition, not KVGFFKR peptide was immobilized, control peptide KAR, I will extract the ICln platelet lysate in particular. Acyclovir (100 microns to 5 mm), the pharmacological inhibitor of chloride channel ICln, platelet aggregation and (expression of PAC-1) integrin activation, P is, a specific role in the activation of integrin ICln especially The suppressed without affecting the expression of CD62 to confirm. To inhibit platelet function also in conjunction with the cell-penetrating peptide corresponding to the (ACE ,10-100 microns) integrin recognition domains ICln potential. Thus, we have found verification, and is characterized by new functional interaction ICln and platelet integrin in platelet membrane, between.

Alpha-IIb/beta-3 integrin is a receptor vitronectin fibrinogen, plasminogen, prothrombin, and thrombospondin, fibronectin. This recognizes the RGD sequence in a wide array of ligands. It recognizes the sequence HHLGGGAKQAGDV of fibrinogen γ chain. the results after the activation of integrin alpha-IIb/beta-3. Through binding of fibrinogen soluble, Interactions of platelets / platelet. Result of this step of rapid aggregation of platelets in the perforated surface of endothelial cells physically

Integrin is expressed adhesion molecules ubiquitously. These are cell surface receptors present and hetero of α as β subunit. Under physiological conditions, integrins are contained ions Mg 2 or Ca 2 of which is essential for ligand binding glycosylation very. Integrin receptor binding extracellular matrix to (ECM), is important to the cell, which is achieved integrin by fibronectin  Interaction of laminin vitronectin, and collagen. I will form a complex with proteins, including integrin adhesion Tallinn in the cell, vinculin, and paxillin, and α-actin. They also, to mediate attachment to regulate the kinase, such as Src family kinase and focal adhesion kinase, the actin cytoskeleton. Integrins can be activate protein kinase that plays an important role in cell signaling are involved in the regulation of cell
Apoptosis growth, division, survival, differentiation, and migration. It is an integrin receptor found on the surface glycoprotein II / IIIb group and platelets. Because it is involved in the cross-linking of fibrin plateletswith, I have played an important role in the formation of thrombus.

Genetic disorder common platelet aggregation: Grants Grants Man Man (GT). It is characterized by mucocutaneous bleeding of mild to moderate severity. GT can be classified into types I and II clinical. My type, I show a lack of complex-IIIa platelet glycoprotein IIb of the presence or absence of the possibility of clot retraction and fibrinogen and the surface. In type II, it is a detectable amount of the fibrinogen complex of GPIIb-IIIa on platelets express are regressed ability mochi low or moderate at a reduced level. = Please note are caused by mutations affecting gene disease has been represented in this position.