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.
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.