ITGA8

α-8, membrane protein belonging to the single-pass type I integrin α chain integrin family also known as ITGA8. Repetition of ITGA8 7 FG-GAP is included. Mesenchymal cells, including the smooth muscles of internal organs and blood vessels in the stellar lung myofibroblasts, renal mesangial cells, cells, and liver, ITGA8 represented by (at the protein level). ITGA8 is a heterodimer of α and β subunit. α subunit heavy, and a light chain linked by a disulfide bond.

In addition, ITGB1 fibronectin receptor β subunit, VLA-4 subunit β, and CD29, integrin β-1, which is known as an I membrane protein belonging to the integrin family of single-pass type β chain,. VWFA domain is included in it. Alpha-V or -11 are associated, -4, α5, α6, α7, α8, 9α, and α-10 – α-1, α-2, 3 or integrin β-1 / ITGB1. It binds, instead of α-7, LGALS3BP ITGB1BP3 attached to the α-5,. Integrin β interacts 1 / ITGB1 FLNA, and RANBP9 and FLNB. Combined with human echovirus 1 capsid protein, and 8, integrin β-1 / ITGB1 acts as a receptor for these viruses.

By controlling the mobilization of mesenchymal cells in epithelial tissue probably α-8 / β-1, and function, in the development of kidney, integrins, to other organs. 8 integrin α/β-1 recognizes the RGD sequence in a wide range of ligands, including VTN and, FN1, SPP1 TGFB1, TGFB3 TNC.

By adjusting the recruitment of mesenchymal cells in epithelial structure and ITGA8 alpha-8/beta-1 integrin function in the origin of other organs and possibly kidney. It recognizes a wide variety of RGD sequence of ligands including VTN and, FN1, SPP1 TGFB1, TGFB3 TNC. NPNT think its ligand function kidney origin. I regulate neurite outgrowth of sensory and motor neurons and TNC nerve receptor-mediated cell-cell interactions. I belong to the integrin α chain family. Note: This description may include information from UniProtKB

Integrin family of adhesion receptors are composed of dimeric transmembrane protein 21 heterozygous least specificity of the ligands and their tissue distribution are different. Per, in adult cells and other tissues smooth muscle contraction, I have expressed in nerve cells and mesenchymal development mainly. Now, display extracellular matrix protein that 8, seeded in vitronectin or on fibronectin, we will look for the contact of the focus of specific intracellular associated with the 8 integrin subunit and fake recently. In addition, on the surface 8 expressly DNA sham human embryonic kidney cells were transfected in a can for adhesion to fibronectin and vitronectin, and 8 1, they use this receptor we, (293) that I shows. In addition, 18 the vitronectin and fibronectin – You could be eluted aspartic acid (RGD), from GRGDSP – glycine – arginine bound to both of Sepharose, containing the peptide or protein matrix in particular. Because it seems adhesion of vitronectin and fibronectin to be mediated by the RGD, we Tested additional RGD-containing proteins such as denatured collagen type I., tenascin, fibrinogen, thrombospondin, and osteopontin, tenascin is fake 8 It has been found that it can mediate adhesion of 293 cells transfected. By using a recombinant fragment of tenascin in adhesion assay, we were able to find tenascin of RGD-containing, 81 binding domain of fibronectin type III repeat of the third. Fake V content integrin and fake – that vitronectin tenascin, and fibronectin is a ligand of 8 伪尾 1, and these data, each of these ligands by a mechanism in which it is clearly separated from the 5 This suggests strongly that it binds to integrin RGD site in.

Further double mutant cell line, and more than 18,000 cDNA deletion is, it was used in the screen and the GDAS nylon filter after. The overlapping sequences, cDNA P made from reverse transcription of each RNA sample are probed with labeled 33. The analysis by genome phosphoimage file system in which they are presented 705 cDNA is changed at least twice during the 11 RNA sample mK10/pCMV-Hoxa and MK10. Were examined manually to remove artifacts caused by forty blotting error of the most promising cDNA was selected for validation by Northern blot analysis, each cDNA that has been removed. Expression levels using phosphoric again, normalized to the expression of GAPDH. The two clones is small, the differential expression, reliability has been shown. Expressed sequence tag clusters were set Mm.112139 homology EHD1 weak EH domain-containing protein expressed developing limb bud, testis, the kidney is one branch. Involvement EH domain protein ligand-induced endocytosis and signaling. Acts as an antagonist of the ETS domain transcription activity of (ERF) other EST2 repressor factor, in gene ETS domain transcription factor for the majority of adult

ITGA7

Integrin α-7 is a protein encoded by a gene ITGA7 in humans. ITGA7 is encoding the integrin α chain 7. Integrin is a heterodimer integral membrane protein consisting of one α and β chain from the chain. To form the integrin that binds extracellular matrix proteins and laminin, prepared disulfide α chain 7 undergoes post-translational cleavage in the extracellular domain, by binding the heavy and light chains are bonded to R 1 was. Is expressed in differentiated cells, alpha 7 beta 1 is a major integrin complex. Is present in the mice, splice variants of alpha 7 different in both of the cytoplasmic domain and outside date only one type of transcript human Isolated in: respectively, and extracellular mouse corresponding to the variants B and X2 I include the cytoplasmic domain. It represents the minor species apparently biological significance is unknown, although the outer splice variants distinctive, was identified in humans.

ITGA7

Α7 integrin gene expression of (ITGA7) are regulated during the development of the formation of skeletal muscle. Increase in the production level and expression of isoforms, including the extracellular domain and cytoplasmic various, accompanied by muscle formation. Diversity of α7 basic structural gene of one or more associated with the development in the α chain, to determine by Southern blotting and whether examined the human genome and in situ hybridization rats we. Our results, I have shown that there is an α7 only one gene in the genome of both rat and human. ITGA7 to present on chromosome 12q13 in humans. Phylogenetic analysis of the sequence, the integrin α chain, in order to form the I-integrin, early gene integrin is an indication that you are in the Zu I-integrin and evolution methods. I-integrin alpha chain comprises a sequence of additional amino acids to about 180 due to the early introduction of non-I-gene. I-chain subfamily, evolution repeated further the same chromosome. No-I-integrin α chain gene is a local cluster of 17 and chromosome 2, 12, it matches the position of the human homeobox gene cluster closely. No-I-integrin α chain gene, appears to have evolved in the vicinity of the Hox cluster and parallel. Thus, cell-cell interactions in the end – Hox genes are fundamental to the design of integrin gene and the vehicle body, appears to have evolved in parallel inform matrix, coordinate fashion.

protein this gene encodes belong to the integrin α chain family. Integrin is a heterodimer integral membrane protein consisting of one α and β chain from the chain. Cells and – – cells they mediate a wide range of matrix interactions, cell migration, morphological development, differentiation, and plays an important role in metastasis thereby. This protein acts as a receptor for membrane protein laminin. This can be skeletal muscle and is expressed in the heart mainly involved in the migration process and differentiation during myogenesis. Defects in this gene are associated with congenital myopathy. Code alternatively spliced ​​transcript variants have been marked for this gene different isoforms.

protein this gene encodes belong to the integrin α chain family. Integrin is a heterodimer integral membrane protein consisting of one α and β chain from the chain. Cells and – Cell – They can mediate a wide range of matrix interactions, play an important role in cell migration, morphological development, and differentiation Thus, Transition. This protein acts as a receptor for membrane protein laminin. This can be skeletal muscle and is expressed in the heart mainly involved in the migration process and differentiation during myogenesis. Defects in this gene are associated with congenital myopathy. Code alternatively spliced ​​transcript variants have been marked for this gene different isoforms.
Alpha-7/beta-1 integrin is a major laminin receptor of adult muscle fibers and skeletal myoblasts. Between the muscle differentiation, it is possible to cause a change in mobility and the shape of the myoblasts to facilitate their positions in laminin-rich sites of the secondary fiber formation. Was to maintain the muscle fibers it Cellular architecture, and functional integrity and viability that attached. The Alpha-7X1B isolation and alpha-7X2B isoforms, is -1 2/4 and laminin myoblast laminin, laminin -1 activity to promote the transition of iso-alpha-7X1B is low. I will act as a Schwann cell receptor for laminin -2. And act as its effect and receptor-mediated COMP Vascular smooth muscle cell maturation (the VSMC) (similarity). Required to promote contraction obtain phenotype airway smooth muscle that is differentiated in (ASM) cells
Alpha-7/beta-1 integrin is a major laminin receptor of adult muscle fibers and skeletal myoblasts. Between the muscle differentiation, it is possible to cause a change in mobility and the shape of the myoblasts to facilitate their positions in laminin-rich sites of the secondary fiber formation. And their attachments muscle fibers cytoarchitecture was to survival and to maintain functional integrity it. Alpha-7X1B isolation and alpha-7X2B isoform, to facilitate the transition of -1 2/4 and laminin myoblast laminin, activity is low (in vitro) laminin-1 isoform alpha-7X1B. I will act as a Schwann cell receptor for laminin -2. Action to address the impact on (similarity) vascular smooth muscle cells and receptor-mediated senescence (the VSMC). This is necessary in order to facilitate the acquisition contraction phenotype airway smooth muscle that is differentiated in (ASM) cells.

ITGA6

Integrin alpha 6 is a protein encoded by a gene ITGA6 in humans. Integrin α chain, is alpha 6 ITGA6 protein product. Integrin is a cell surface protein of integrated consisting of one α and β chain from the chain. Chain can be combined with different partners on the results of various integrins. For example, β4 integrin May 6 in combination or TSP180, and many β-1 integrin VLA-6. Integrin to be involved in signal transduction to the cell surface through cell adhesion and are known. transcript variants encoding two different isoforms have been found for this gene.

ITGA6

Integrin α chain, is alpha 6 ITGA6 protein product. Integrin is a cell surface protein of integrated consisting of one α and β chain from the chain. Chain can be combined with different partners on the results of various integrins. For example, β4 integrin May 6 in combination or TSP180, and many β-1 integrin VLA-6. Integrin to be involved in signal transduction to the cell surface through cell adhesion and are known. transcript variants encoding two different isoforms have been found for this gene.

Through-4 superfamily (TM4SF) protein forms a complex with cell surface proteins and other integrins. Immunoprecipitated with CD81 from MDA-MB-435 cancer cells of the breast for further characterization of the major protein present in TM4SF protein complex in a typical combined monoclonal antibodies to both proteins. Only two types of cell surface proteins that are recognized by antibodies that are 35 our choice. These included (NAG-2 and CD9, CD63,) protein TM4SF three different and (α6β1) integrin. NAG-2 protein (novelantigen-2), which is up to a cell surface protein of 30 kDa unknown. To isolate NAG-2 by using the protocol of cDNA encoding for expression cloning. The deduced amino acid sequence TM4SF, the NAG-2 showed maximum identity for CD53 (34%) when aligned with other proteins. Immunohistochemistry flow cytometry and Northern blotting showed to be present in a variety of cell types NAG-2 and the tissue, brain, lymphocytes, and not present in platelets. the organization in a different, strong staining was observed in fibroblasts, endothelial cells, in mesothelial cells and follicular dendritic cells. as nonstringent preparation, (CD81 and CD9), and NAG-2 protein was co-immunoprecipitated with integrin (α3β1andα6β1) members TM4SF other. In addition, immunofluorescence two color was shown to co-localize NAG-2 and CD81 on the surface of the growth of HT1080 cells. These results confirm the presence of TM4SF integrin complex with NAG-2-specific TM4SF · TM4SF.

Alpha-6/beta-1 integrin is a receptor on platelets laminin. Is a receptor for laminin in epithelial cells, integrin alpha-6/beta-4 is an alpha 6 integrin α chain, which plays an important role in the structural hemidesmosome.The ITGA6 protein production. Integrin is a cell surface protein of integrated consisting of one α and β chain from the chain. Chain can be combined with different partners on the results of various integrins. For example, β4 integrin May 6 in combination or TSP180, and many β-1 integrin VLA-6. Integrin to be involved in signal transduction to the cell surface through cell adhesion and are known. transcript variants encoding two different isoforms have been found for this gene.

ITGA6 gene provides instructions for making (α6 division) of the two proteins called integrins α6β1 and integrin α6β4. The integrin molecules of the other groups of proteins that control the adhesion of cells to each other, and protein (cell adhesion) – a web around the (cell matrix adhesion). Integrins transmits chemical signals that regulate cell growth and activity of specific genes.

protein is located in the epithelial cells, which are cells that line the surface of the body cavity mainly to α6β4 integrin. This protein plays a particularly important role in stabilizing and strengthening the skin. This is part of hemidesmosomes, is a microscopic structure for fixing the outer layer of skin (epidermis) to the lower layer. As part of a complex network of protein hemidesmosomes, α6β4 integrin, helps to keep the skin layer.
Made integrin subunits other forming the tissue or organ before birth α6, with α6β1 integrin function. α6β1 integrin protein is not considered as α6β4 integrin as well.

5 mutation was found to cause epidermolysis bullosa with pyloric atresia (EB-PA) at least the gene ITGA6. In addition, people with blistering of the skin, the EB-PA is born with a lethal blockage of the digestive tract called pyloric atresia. Mutations in the gene ITGA6 accounts for about 5% of all cases of EB-PA.  Can lead to loss of α6β4 integrin function ITGA6 of cause gene mutations in EB-PA. These mutations alter the structure and function of normal cells, preventing or α6 integrin subunits to produce enough of this subset. cause the cells of the epidermis result lack of α6β4 integrin function is fragile, as fragile. Minor trauma other, can result in the formation of extensive blister, and to separate the skin layer or friction. How ITGA6 mutation is associated with pyloric atresia in the gene it is not so clear.

I believe that researchers, and may play a decisive role in the development of malignant tumors of both α6β4 integrin and α6β1 integrin is called a cancer. These arise in epithelial cells, these cancers can be breast cancer, lung cancer, liver cancer, prostate cancer, and may affect the organs and many tissues, including the skin. Changes in α6β4 integrin α6β1 integrin activities and places and cancer cells is associated with the development of cancer. Integrin protein, to activate the major signaling molecules to move through the body and invade other tissues, causing the cancer cells. These signals, the cancer cells to self-destruct, so that there is more resistant. Recent studies, in addition to their role in the evolution of cancers existing show integrin α6β1, α6β4 integrin, that it is possible and included in the initial formation of these tumors.

ITGA5

Is a protein encoded by integrin α-5, by gene ITGA5 in humans. The product of this gene belongs to the integrin alpha chain family. Integrin is a heterodimer integral membrane protein consisting of one α and β chain from the chain. This gene encodes the 5 integrin chain. Alpha circuit 5 was heavy and light chains were disulfide bond that is prepared is combined with R 1 to form a fibronectin receptor undergo post-translational cleavage of the extracellular domain. That in addition to the adhesive, is involved in signal transduction integrins to cell surface through is known.

ITGA5

Integrin cell – cell and cell – for heterodimeric complex and α related membrane receptor family involved in matrix interactions is a β subunit. To begin to understand the evolution of these complexes, we examined the genomic organization of the integrin β subunit and some α. In both the in situ hybridization and somatic cell hybrids, we vitronectin receptor (VNR a), the GPIIb the complex of platelet glycoprotein IIb group / IIIa fibronectin receptor (FNR a) is, α sub I have identified the chromosomal location of the unit of α-subunit gene. I was identified hetero of GPIIb / IIIa, the position on the chromosome of GPIIIa of β subunit gene, also. In our study, it can not find the locus of the α subunit is shown, each of which is located on chromosome different. Located in chromosome 17q21 —- 23 on GPIIb gene is located on chromosome 12q11 is located on chromosome 2, the gene of FNR with —- 13 gene for VNT. Unlike the chromosome of the alpha subunit gene of GPIIIa and GPIIb of, is located in chromosome 17q21 —- 23 and also is close to the dispersion GPIIIa gene physically. In these studies, GPIIIa and GPIIb for suggesting that genes integrin family of α subunits are scattered throughout the evolution during the close physical proximity. These two can be the physical proximity of GPIIIa and GPIIb of involved in co-expression of these proteins from megakaryocytes, limiting the use of polymorphism length limited to study the relationship between / the GPIIb can lead to linkage disequilibrium between genetic abnormalities IIIa small tribe.

The product of this gene belongs to the integrin alpha chain family. Integrin is a heterodimer integral membrane protein consisting of one α and β chain from the chain. This gene encodes the 5 integrin chain. Alpha circuit 5 was heavy and light chains were disulfide bond that is prepared is combined with R 1 to form a fibronectin receptor undergo post-translational cleavage of the extracellular domain. That in addition to the adhesive, is involved in signal transduction integrins to cell surface through is known.

Alpha-5/beta-1 integrin is a receptor for fibrinogen and fibronectin. This recognizes the RGD sequence in the ligand. In the case of HIV-1 infection, it appears interactions with extracellular viral Tat protein to enhance angiogenesis in Kaposi’s sarcoma lesions

Integrin is expressed adhesion molecules ubiquitously. These are cell surface receptors present and hetero of α as β subunit. Under physiological conditions, Mg2 ion of which is essential for ligand binding and CA2 and glycosyl strongly integrin is included. 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. Glycoprotein II / IIIb group
Is an integrin receptor on the surface of platelets. We are involved in the crosslinking of platelets to fibrin, which plays an important role in thrombus formation.

hetero β subunit and α. α subunit is composed of a light chain and a binding heavy chain by a disulfide bond. It is associated with alpha 5 beta 1. Interact with NISCH and HPS5. I will interact with and address RAB21. Reaction and Tat of HIV-1

ITGA4

CD49d is an integrin alpha subunit. It makes half of lymphocyte homing receptor α4β1. Product of the gene belongs to the family of integrin alpha chain protein. Integrin is a heterodimer integral membrane protein consisting of one α and β chain from the chain. This gene encodes the α chain 4. I-domain also undergo cleavage disulfide bonds integrin alpha 4 is contained unlike other the α chain. Alpha associated with single or beta chain in β chain 7 4 chain.

Product of the gene belongs to the family of integrin alpha chain protein. Integrin is a heterodimer integral membrane protein consisting of one α and β chain from the chain. This gene encodes the α chain 4. I-domain also undergo cleavage disulfide bonds integrin alpha 4 is contained unlike other the α chain. Alpha associated with single or beta chain in β chain 7 4 chain.

ITGA4

Embryogenesis of α4 integrin, hematopoiesis, heart development, and play an important role in the immune response. Because the α4 subunit regulates cellular functions different from the integrin subunits α other, perhaps, α4 integrin subunit, is required for biological processes such. Be coupled paxillin, an intracellular signaling adapter molecule firmly directly to the α4 cytoplasmic domain previously been reported, some of the abnormal functional response of α4 integrin-mediated cell adhesion, we reacted the account. In addition, it interferes with the α4-paxillin interaction, save 9 α4cytoplasmic domain is sufficient for Paki Shirin binding Tyr991within or reverse Glu983 this area is the effect of the α4 cytoplasmic domain – amino acid region and (Glu983-Tyr991), migration and cell proliferation discover the alanine substitution. In this study, mapped the use α4 binding site in paxillin mutation analysis, we examined the effect on the α4tail mediated functional response. That you are fully sequence between residues Asp275 and Ala176 of paxillin to connect to the queue α4 is reported. We targeted adhesion plaques, and found that it is possible to form a ternary complex queue α4, paxillin, fat, and pp125FAK α4-binding fragment Paki cylinder, P (Ala176-Asp275) is more efficient than in particular that it is blocking the paxillin binding to α4 tails manner combines block of FAT. In addition, α4 ​​tail paxillin suppresses be stimulated cell migration α4-binding fragment when expressed in cells. Thus, the binding paxillin increases in α4 tail, leading to suppression of α4-paxillin reaction block the α4-dependent cell response cell migration, selection.

Alpha-4/beta-7 and (VLA-4) integrin alpha-4/beta-1 is a receptor for fibronectin. They recognize one or more domains of the CS-5 domain of fibronectin alternative splicing and CS-1. They also, is a receptor for VCAM1. Integrin alpha-4/beta-1 recognizes the QIDS consecutive in VCAM1. Alpha-4/beta-7 integrin is a receptor for MADCAM1. It recognizes the sequence LDT of MADCAM1. Activated endothelial cells integrin VLA-4 led to the white blood cell line of VLA-4-positive aggregates most of the same type. It also is possible to participate in the interaction of cytolytic T cells and target cells

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. Glycoprotein II / IIIb group
Is an integrin receptor on the surface of platelets. We are involved in the crosslinking of platelets to fibrin, which plays an important role in thrombus formation.

hetero β subunit and α. α subunit, can be split into fragments of two non-covalently bind sometimes. 4 that are associated with, or α-or β-1, a β-7. α-4 interacts with the TGFB1I1/HIC5 PXN, and LPXN. Interact with CSPG4 in CSPG4 chondroitin sulfate glycosaminoglycan

Alpha-4/beta-7 and (VLA-4) ITGA4 alpha-4/beta-1 integrin is a receptor for fibronectin. They recognize one or more domains of the CS-5 domain of fibronectin alternative splicing and CS-1. They also, is a receptor for VCAM1. Alfa-4/beta-1 integrin recognizes the sequence QIDS in VCAM1. Alfa-4/beta-7 integrin is a receptor for MADCAM1. It recognizes the sequence LDT of MADCAM1. Activated endothelial cells integrin VLA-4 led to the white blood cell line of VLA-4-positive aggregates most of the same type. It also is possible to participate in the interaction of cytolytic T cells and target cells. hetero β subunit and α. α subunit, can be split into fragments of two non-covalently bind sometimes. 4 that are associated with, or α-or β-1, a β-7. α-4 interacts with the TGFB1I1/HIC5 PXN, and LPXN. Interact with CSPG4 in CSPG4 chondroitin sulfate glycosaminoglycan. I belong to the integrin α chain family. Note: This description may include information from UniProtKB.

ITGA3

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.

ITGA3

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.

ITGA2

CD49b is a protein encoded by a gene in human CD49b. CD49b protein is α integrin subunit. This makes the α2β1 integrin half duplex. Integrin is a hetero integral membrane glycoprotein composed from a common β chain of the single α chain. These are various T cells (NKT cells on), cell types, including platelets NK cells, and fibroblasts. It is involved in cell adhesion, integrin have joined the mediated signaling on the cell surface. DX5 is a monoclonal antibody that binds specifically to CD49b.

ITGA2

This gene encodes a transmembrane receptors for collagen and related proteins the α subunits. The encoded protein forms a heterodimer with the β subunit I mediates the adhesion of other cells and platelets in the extracellular matrix. Loss of the encoded protein is associated with bleeding disorders, platelet-type 9. Antibodies against this protein have been found in immune disorders, including some neonatal thrombocytopenia platelets. This gene is located in close proximity to the gene associated with the α subunit. Result of alternative splicing in the transfer multiple variants.

From all strains of mice, DX5 monoclonal antibody is a useful reagent for inspection it is dirty NK cells. The retrovirus-mediated expression cloning system, we have identified a DX5 molecules recognized by monoclonal antibodies. DNA 5 KB of which encodes a protein that reacts with the monoclonal antibody DX5 was the same (2 silver, late integrin α2 very) and CD49b this molecule and, isolated from NK cell cDNA library. Reacts with the transformant expressing CD49b in DX5 monoclonal antibody, the binding of transfectants and NK-DX5 cells was blocked in the presence of anti-CD49b mAb other CD49b. The NK1.1 When cultured in IL-2, NK cells, they lose reactivity with the result of gradual monoclonal antibody DX5 cell proliferation. It was significantly higher cytotoxicity mediated by DX5 NK cells when compared to DX5-NK cells. Therefore, DX5 monoclonal antibodies may be used in order to recognize CD49b, to determine the subset of functionally distinct NK cells.

Integrin alpha-2/beta-1 is a receptor for E-cadherin laminin, collagen, collagen C-propeptides, and fibronectin. It proline in collagen – recognizes the hydroxyl sequence GFPGER. It is responsible for the adhesion of other cells and platelets in the regulation of organization of extracellular matrix which is synthesized de novo expression and collagenase gene force collagen, collagen

This gene encodes a transmembrane receptors for collagen and related proteins the α subunits. The encoded protein forms a heterodimer with the β subunit I mediates the adhesion of other cells and platelets in the extracellular matrix. Loss of the encoded protein is associated with bleeding disorders, platelet-type 9. Antibodies against this protein have been found in immune disorders, including some neonatal thrombocytopenia platelets. This gene is located in close proximity to the gene associated with the α subunit. Result of alternative splicing in the transfer multiple variants.

hetero β subunit and α. I have been associated with the alpha 2 beta 1. Interact with RAB21 and HPS5. Bound to 8 and 1 capsid protein to echo human viruses, I will function as a receptor for these viruses. It acts on each other (via ITAG2 I-domain) and rotavirus VP4, this interaction occurs only in rotavirus strain ITGA2 of integrin dependent
Function as a receptor

ITGA2 alpha-2/beta-1 integrin is a receptor of the E-cadherin laminin, collagen, collagen C-propeptide, and fibronectin. It proline in collagen – recognizes the hydroxyl sequence GFPGER. It is responsible for the adhesion of other cells and platelets to collagen, which regulate the expression of the organization of the extracellular matrix to the power generation of the collagenase gene and collagen newly synthesized. I belong to the integrin α chain family. Note: This description may include information from UniProtKB.

ITGA1

CD49a, is an integrin alpha subunit. This makes the α1β1 integrin half duplex. This gene encodes the α1 subunit of the integrin receptor. In order to form a cell surface receptor for laminin and collagen, this protein, heteroaryl and β 1 subunit. It can be involved in cell adhesion and play a role in inflammation and fibrosis – cell receptor heterodimer. Alpha 1 subunit contains a von Willebrand factor type I domain that has been added is considered to be involved in collagen binding.

ITGA1

This gene encodes the α1 subunit of the integrin receptor. In order to form a cell surface receptor for laminin and collagen, this protein, heteroaryl and β 1 subunit. It can be involved in cell adhesion and play a role in inflammation and fibrosis – cell receptor heterodimer. Alpha 1 subunit contains a von Willebrand factor type I domain that has been added is considered to be involved in collagen binding.

In order to form a heterodimer that unctions as a dual laminin / collagen receptor in hematopoietic cells and nerve cells to beta 1 specifically binding ITGA1 chain (ITGB1) the chain. The N-terminal half-life of 06 transmembrane domains and short terminal cytoplasmic tail and the binding site of the cation of ITGA1 3 value followed – amino acid I domain,. He also, I have a potential N-glycosylation of 28 PMF. People ITGA1 to expression of the mouse fibroblast cell line 180-III protein. ITGA1 had played an important role in the regulation of the production of cartilage growth and esenchymal stem cells involved in the early remodeling of osteoarthritic cartilage. In addition, I have played an important role in EGULATION of cartilage and production MSC proliferation.

This gene encodes the α1 subunit of the integrin receptor. In order to form a cell surface receptor for laminin and collagen, this protein, heteroaryl and β 1 subunit. It can be involved in cell adhesion and play a role in inflammation and fibrosis – cell receptor heterodimer. α1 subunit comprises adding the I domain, which is considered the type of von Willebrand factor, to be involved in (I) collagen binding.

Molecular sequence of this clone is equal to the number of genes accession only as a starting point. However, the sequence of a portion of the same gene transcript, may be different from each that has (for example, polymorphism) variants that exist in nature, the working life of its own. This branch is essentially the same as the reference, but I recommend to use before a full review of variants of all current.

As well as adult human kidney and in the development and integrin α-, we investigated the distribution of cultured cells of β-subunit and other organizations that have been selected. When placed in the appropriate ligand in cultured cells, (β1, α1, and α2 α 5) is localized in focal adhesions Tallinn part of the integrin subunit. Similarly, it appears as shown adhesive as shown in glomeruli and mature into tissue polarization β1 integrin in the co-localized with talin complex. The human kidney integrin α subunit, i.e., have been reported on the route, it was expressed mainly in fetal tissues. In glomerular mesangial cells of the features of α1 integrin sub-groups, respectively, and α2 α 3 subunit whereas showed immunoreactivity in podocytes and endothelial cells. The tubules of the α6 subunit complex subunits β1, α3, α2 subunit, shows a polarization distribution coaligning typical film tubular while expressed in distal tubular cell.

These results kidneys of α6β1 integrin α2β1, and α3β1, suggesting that it can be made to function as a receptor basement membrane. It is expressed in smooth muscle cells of several mainly did not exist substantially in the kidney in the α5 subunit appears. In other tissues, different methods of expression of integrins has been found. Therefore, you can be while dispersing in the chest, such as polarized place in many glandular epithelial cells of the α3β1 integrin, and a variety of epithelium, and appears to function as a receptor for basement membrane, to find for integrin α6β4. Nerve cells, none of the integrin cerebellum and adult brain and nerve cells of human development, and can not while presenting the polarization distribution of the β1 integrin obviously the end, one of the α-subunit is also found in skeletal muscle cells and cardiac α6β1 integrin complex was included abundantly in peripheral tissues in which can not be detected. In human tumors, tumor cells, including tumor metastastatic, announced the organization of their origin and the same integrin in general. Lack of dismantling or expression of basement membrane receptor integrin and poorly differentiated tumor some was obvious in both population heterogeneity even.

Collagen plays a central role in maintaining the stability and integrity of the vascular wall undiseased, and atherosclerosis. Can lead to uncontrolled accumulation of collagen results in a blockage or arterial thrombosis often unbalanced metabolism, reducing the speed of the vessel wall. The reduced production of degradation uncontrolled collagen, which can affect the stability of the vessel wall, particularly in atherosclerotic plaques prone to rupture them aneurysm. This assessment provides an overview of the four groups of role in atherogenesis collagen and blood vessels. The main focus was to emphasize the importance and exemplary role of short-chain network form type VIII collagen in the extracellular matrix of atherosclerotic plaque and undiseased artery. The molecular structure of collagen type VIII, the cellular origin, are reflected in atherogenesis, and modulating the expression in experimental models are not the lowest, with humans, the expression pattern of time and spatial potential, atheroma, factors function are discussed.

Integrin

And around the cell, integrins and is mediated transmembrane receptor binding between the extracellular matrix or other cells of the (ECM). It is integrin signaling for transmitting information about the mechanical state of the ECM in the cell and chemical composition. Thus, in addition to the transmission of the film vulnerable against mechanical forces or else, they are involved in the regulation of movement and cell cycle intracellular signaling, and shape. I will inform cell receptor on the cell and molecular response of normal environment. Not only do this in signaling outside, integrins, but not operating mode from the inside. Therefore, in order to convert the information from the ECM into the cells, allowing the aggregation of platelets, for example, they show the outer state of the cell that allows a flexible response quickly to changes in the environment.

Integrin

There are many types of integrin there, and has a number of types of cells on the surface of those many. Integrin is essential for all animals, and is found in all test animals from sponges to mammals. Integrin, has been extensively studied in humans. And cells – cells – cell integrin cadherin like to mediate communication and matrix interactions, cell adhesion molecules of the immunoglobulin superfamily, selectins, and working together with other proteins, such as syndecan. ECM components and integrins bind cell surface, such as laminin fibronectin, vitronectin, and collagen.

Integrin2

Integrin is anaerobic hetero, including a chain of two different called α (alpha) and β (beta) subunit. In mammals, the 8β subunits and 18α, genome of Drosophila encodes a subunit 2β and 5α slightly, nematode C. elegans, have the gene and 1β.Theα of β subunits and two α subunit Whereas yl, and through the plasma membrane, respectively, and has a small cytoplasmic domain and is characterized.

Further, in some embodiments of the subunit-subunit of β-1, 4 kinds exist, for example, is formed by differential splicing. Plasma membrane has been included studies.Integrin number, it depends on the sub-unit of another has a cytoplasmic domain short amino acid of 40-70 degree in general, but the variety and α of the β subunit about 24 unique integrin, which is created through the combination. An exception is a β4 subunit having a cytoplasmic domain of either amino acid number 1088, the most prominent cytoplasmic domains of membrane proteins. Length from the N-terminus of each chain that constitute the ligand-binding domain of the extracellular matrix of 5 nM final cell plasma membrane outside, of approximately 23 nM lying close to each other and of α β chain.

Integrin3

May be different to 160 kDa from the 90 kDa of the molecular weight of the integrin subunit. β subunit, cysteine-rich repeats four. Β subunit binds divalent cations some, Α. The role of divalent cations in the α subunit is unknown, it is possible to stabilize the folding of the protein. cations β subunit is critical: they are involved in the adjustment of at least some of the ligand binding to integrins directly. There are different methods for classifying integrin. For example, a portion of the α-chain, because it has a structure similar to that found in the von Willebrand factor, A-domain protein, called a structure additional elements (“domains”) or (In addition, it also) N-terminal α-domain is called α-I domain. (For example, α2β1 integrin and α1β1) in collagen, or carry or bind this domain, integrin functions as a cell-cell adhesion molecule. The α-I domain is a ligand binding site of integrin thereof. Do not carry this field, also integrins of these, it adds to the domain of the ligand binding site of them, this domain is a β subunit.

Integrin4

In both cases the domain to carry up to binding sites of trivalent cation. It is the presence of a constant at physiological concentrations of divalent cations, one, the major divalent cations in the blood average density 0.8 mm in (magnesium) or magnesium ion, calcium 1.4 mm and (calcium) I carry. For these ligands containing an acidic amino acid in the interaction site of their two positions at the time of binding ligands other, are occupied by cations, at least. The amino acid sequence arginine – glycine – as part of aspartic acid, proteins many ECM, for example, to amino acid functional interactions integrins.

In spite of many years of effort, the difficult proof identification high-resolution structure of integrins: membrane protein is a classic difficult to purify, integrin is complex and large-scale, wood sugar of many (“advanced and is associated with glycosylation “). Resulting GPIIbIIIa, ultracentrifugation Furthermore, low resolution image of the detergent extract data Methods indirect and determine the nature of the solution of the integrin using light scattering, occasional high using integrin electron microscope intact domain or a pair of single molecule model and single integrin chain to be mixed with NMR or crystallographic data resolution was assumed for other chain.

X-ray crystal structure despite extensive efforts described above were obtained for eligible extracellular region integrins, integrin αvβ3 was surprising. It showed a molecular profile inverted bent in a V-shape having a ligand binding site near the cell membrane and potentially. Crystal structure also RGD sequence, more importantly perhaps, obtained the same integrin associated with small ligands, including drug cilengitide. The reason is important for binding of the ligand to the integrin RGD divalent cations (domains), as indicated above, it has been clarified in the end. These sequences, ECM is considered to be the key and influence the behavior of the cell interaction with the integrin.

Structure raises a number of issues with respect to signaling and ligand binding in particular. Ligand-binding site is directed towards C-terminus of the integrin molecule-out area of ​​the cell membrane. It would seem to be closed, if it is found vertically from the ligand binding site of the membrane, usually, a large ECM, integrin ligand is dependent components particularly well. In fact, is known about the angularly dependent membrane proteins on the surface of the film is little, it is a difficult problem to deal with the existing technologies. The default assumption, is that they look like candy smaller, but evidence for this assumption is sweet aware of its absence. May affect general how membrane proteins of works, integrin structure is attracting attention to this problem. It extracellular loop (hereinafter, please refer to “Enable”) seems to be tilted helix through integrins, suggesting that it can not be perpendicular to the surface of the membrane.

It has changed a little surprisingly after binding to the crystal structure cilengitide but, with a change in the shape of the displacement of the ligand binding site is located in a more accessible location from the cell surface integrin function is away, this hypothesis, also occurs this shape change intracellular signaling you have. Body wide biochemical literature and cell biological, supports this goal. Most convincing proof involves the use of antibodies recognizing the integrin only be activated or they are connected to their ligands probably. Since about 3 microns in diameter “mark” that performs antibody binding target range, the resolution of this technique is lower. However, I shows that significant changes in the form integrin occurs on a daily basis is clearly (ligand-induced binding site) antibody so-called LIBS these. However, changes how was detected by an antibody, the structure is still unknown, but it is displayed.

Integrin is a pair of (micro filament especially) non-ECM cytoskeleton of cells. ECM integrin ligand may be coupled with the determination of the integrin α β subunit has been executed. It is a laminin fibronectin, vitronectin, and collagen in the ligand of integrin. The relationship between the ECM and cells, can help cells to withstand the pulling force without being ripped off by the ECM. Capacity of the cells, is essential for ontogeny to create this type of connection.

Mobile phone that is connected to the ECM, is a basic requirement for the development of multicellular organisms. Integrin is not a mere hook, but the cell phone signal, I will give you the important nature of the surroundings. And human and many other signal, from the soluble receptor of the growth factor VEGF, such as this, such as EGF, whether it be differentiated love, movement, death and they, the biological action together I apply the cell solution to what it takes. Therefore cell biological processes underlying many integrin. Adhesion of cells is composed of cytoplasmic proteins and integrins like many paxillin α-actin Tallinn, and vinculin, such complex formation, cell adhesion, passes. By act by regulating the kinase as a Src kinase family member FAK and (focal adhesion kinase), etc. to phosphorylate substrates, they adopted the phosphorus signaling p130CAS adapters such CRK such . Such complexes make the attachment of the actin cytoskeleton. ECM extracellular and intracellular actin Therefore fiber Association, integrin that serves to connect the two networks in the plasma membrane. It binds to the keratin intermediate filament system in epithelial cells: are exceptions Alpha6beta4 integrin.
They After assembly, the focal adhesions is a significant molecular complex obtained after interaction of integrin and ECM.

EPHB6

Ephrin type B-6 receptor is a protein encoded by a gene EPHB6 in humans. And its ligand ephrin receptor, ephrin, many processes of development of the nervous system in particular mediation,. Based on the sequence context and their structure, ephrins are divided into (EFNA) Class ephrin-A, which is fixed to the membrane by (EFNB) Class ephrin-B is a transmembrane protein and glycosylphosphatidylinositol linkage. Eph family of receptors are divided into two groups based on the similarity of their affinity for ephrin ligand binding and ephrin-AB extracellular domain sequence thereof. I comprises a subgroup of the maximum ephrin receptor tyrosine kinase (RTK) family. Lacks kinase activity of the receptor tyrosine kinase most ephrin receptor encoded by this gene, and is connected to the ephrin-B ligands.

EPHB6

And its ligand ephrin receptor, ephrin, many processes of development of the nervous system in particular mediation,. Based on the sequence context and their structure, ephrins are divided into (EFNA) Class ephrin-A, which is fixed to the membrane by (EFNB) Class ephrin-B is a transmembrane protein and glycosylphosphatidylinositol linkage. Eph family of receptors are divided into two groups based on the similarity of their affinity for ephrin ligand binding and ephrin-AB extracellular domain sequence thereof. I comprises a subgroup of the maximum ephrin receptor tyrosine kinase (RTK) family. Lacks kinase activity of the receptor tyrosine kinase most ephrin receptor encoded by this gene, and is connected to the ephrin-B ligands.

Is a family of the largest known receptor tyrosine kinase Eph receptors. First, all of them are identified as orphan receptors Zu known ligands, certain features of which are not well understood. In recent years, the family ligand was identified named ephrins, certain features are identified in the nervous generated accordingly. It is possible to guide the development Eph receptors and ephrins, nerve topographic As it has been implicated as a position tag. They also axon guidance and cell migration, and has been involved in the route selection in the creation of regional model of the nervous system. Ligand is fixed to the cell surface, most of the features found so far, it can be interpreted as an accurate axon guidance or cell migration. This large family of ligands and receptors, there is a potential to contribute significantly to the exact space modeling of cell location and connection of the nervous system.

Was used in order to further express Kaplan-Meier analysis, to examine the predicted relationship between the expression of EFNB3 or EPHB6, EFNB2 TrkA is NB. ; The TrkA and EFNB2; the TrkA and TrkA and EPHB6 of EFNB3: Study groups were divided into groups based on the expression level of the gene combination, the following. ; The high / low EPHB6 TrkA, TrkA / EPHB6 in the low altitude; EPHB6 TrkA of high / low, high TrkA / low EPHB6: For example, there was a combination of TrkA and EPHB6 groups of four. The pattern of the probability distribution of the survival of each of the four groups and patient, I was next examined.

One third of the NB, expressed low low EPHB6 both bets TrkA. Third of another, expressed high TrkA, the high EPHB6 both. The third and the last is TrkA high door of low-TrkA but EPHB6 high NB express, expression who were included low EPHB6. Show the group of positive and negative presence of NB and 3 Group 2, is different by expressing the (or vice versa) of TrkA identification EPHB6 by the expression. Therefore, regardless of the expression of NB TrkA, EPHB6 formula to predict the outcome of the disease. NB individual in the group defined by the combination of these three variables will vary. Together TrkA/EFNB3 combination with TrkA/EFNB2 is obtained, regardless EFNB3 formula data that these EPHB6, EFNB2, Similar results demonstrate that to predict the outcome of the disease from NB expression TrkA.

Incomplete kinase receptor for members of the ephrin-B family. I will bind to ephrin-B2 and ephrin-B1. Regulate the migration and cell adhesion by the effect of both positive and negative upon stimulation by ephrin-B2. Inhibitory activity of JNK, the expression of CD25 and IL-2 secretion induced by T cell receptor stimulation by ephrin-B2

First to evaluate the role of blood pressure Ephb6 (BP) regulation. We its ligand EphB6 Efnb All three have observed that expressed vascular smooth muscle cells in mice (VSMC). We found castrated the shrinkable men Ephb6 gene KO is increased compared to the corresponding WT those small arteries, the activation of RhoA, and shown by ex vivo phosphorylation of constitutive myosin light chain . According to this finding, Ephb6 KO mice presented BP reinforcing castrated compared to castrated WT controls. In experiments in vitro, the Ephb6 reduced VSMC contraction, crosslinking Efnbs is, VSMC that revealed that suggest that it is the responsibility of the phenotypic BP reverse signaling has been observed through Efnbs. Reverse signaling is mediated by GRIP1 adapter protein. As a compensatory mechanism, 24 hours, reduction was shown from Ephb6 KO urinary catecholamine in male mice for feedback to maintain BP within the normal range probably additional experiment. To castration, however, that compensation is canceled in Ephb6 KO mouse, BP is a reason for increase was detected in these animals probably. In addition to regulation of testosterone, which suggests that it is an object nervous / endocrine According VSMC, the catecholamines correction mechanism Ephb6. Extended FNS and method with EPHS and testosterone, can play an important role in the regulation of BP and contraction of the small arteries revealed in our study.

For example, Eph receptors belong to the large class of receptor tyrosine kinases involved in various processes such as angiogenesis rear modeling, and axon guidance. Further These molecules are involved in several cancers, significant work has been done to understand the biological significance of their tumor formation. Eph receptor number and are transferred silence cell, the invasive breast cancer in addition to EphB6 representation of variants of ephrin ligand. In transcriptional silencing of EphB6 due to methylation of the CpG dinucleotide in the gene promoter specific. Gene transcription EphB6 was not detected in MDA-MB-231 cells, transfection of EphB6 expression construction reduces the invasiveness of the in vitro these cells significantly. Perhaps, the yeast two-hybrid system is referred to as reaction EphB6 with intracellular proteins other mediating EphB6 phenotypic expression cells. It was found to affect proteins involved in the metabolism of various or indirectly EphB6 direct comparison proteome analysis of the MDA-MB-231 cells, signal transduction, the expression of energy homeostasis and cytoskeleton.

I have shown that proteome changes seen in cells expressing EphB6 breast cancer may be a direct effect of EphB6 changes in the level of specific proteins. However, most of the change in the level of protein appears to be an indirect effect of EphB6. Major mechanism for these changes, you can include a change of translatable richness of transcript specific, and stability. Of a variety of regulatory molecules that control the expression of genes encoded by the human genome, has emerged as an important class of regulators miRNA. To enhance preventing the transfer and degradation of RNA or small molecule of 21 to 23 nucleotides in length, transcripts and was obtained caused a change in the level of protein in this manner. This is assumed to be a sequence that can be targeted by the miRNA that 2/3rd over gene to be encoded in the human genome are different. diseases appropriate miRNA can be seen from the different levels of these molecules in various types of cancer. The introduction of the miRNA construction of certain tumor cells, inhibiting tumor phenotype miRNA was assigned an important regulatory role thereby is shown. Given a number, miRNA for the purpose intended by the particular miRNA will be able to influence the presence of a large number of proteins and mRNA.

The EphB6 transfection can affect the protein profile due to the abundance of modulating miRNA addition of cells was assumed probably based on proteomic profile was altered EphB6 transfected MDA-MB-231 cells. In response to this opportunity, using nucleic acid locked (LNA) miRCURY platform link between miRNA and cell phenotype, to establish a hybridization array-based strategies. I will provide a link between the biological significance of the change in phenotype of cancer cells and expression status EphB6 MDA-MB-231 cells with the miRNA of here.