Examples of using Integrin in English and their translations into Russian
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Colloquial
It also interacts with the integrin dimer VLA-4 also called α4β1.
Integrin, beta 5 has been shown to interact with PTK2, Annexin A5 and PAK4.
This is caused by mutations in integrin α6β4, laminin 322 and BPAG2.
Integrin α2β1 is expressed mainly on epithelial cells and platelets.
TSP-1 has multiple receptors, among which CD36,CD47 and integrins are of particular note.
Multiple integrin heterodimers can bind to the adjacent sites of the virus capsid.
When neural crest cells stop making N-CAM and N-cadherin, andstart displaying integrin receptors, cells separate and migrate.
Implication of integrin α5β1 in human breast carcinoma apoptosis and drug resistance.
At the same time, the activated lymphocytes may penetrate back through the BBB[30] andexpress tropic to the CNS integrins i.e.
Integrins are heterodimers which are formed from one beta and one alpha subunit.
This protein mediates repression of geneactivity through histone deacetylation, and may act as a specific regulator of integrin function.
The cells of this line have integrin receptors[13] affine to RGD sequence, which is present in collagen structure.
Similar to SV40, attachment andbinding with cells triggers clustering and relocation of integrin molecules from lipid rafts to the caveolae-like structures.
Proteases, integrins, pH, and reactive oxygen species are just few of the currently known factors that can activate TGF-β.
This protein interacts with enhancer of zeste 2,the cytoplasmic tail of integrin β7, immunodeficiency virus type 1(HIV-1) MA protein, and histone deacetylase proteins.
Some integrins are on the cell surface in an inactive state, and can be rapidly primed, or put into a state capable of binding their ligands, by cytokines.
Pre-clinical evidence suggests that rituximab could be also used in combination with integrin inhibitors to overcome the resistance to rituximab mediated by stromal cells.
The researchers ablated various parts of the recombinant MyoD sequence and concluded that MyoD used encompassing elements to bind the E-box andthe tetralplex structure of the promoter sequence of the muscle specific gene α7 integrin and sarcomeric sMtCK.
Increasing number of cells expressing these integrins reflects the process of their activation and mobilization in systemic inflammatory reaction characteristic of preeclampsia 21.
Thus, analysis of microRNA influence on signaling pathways of radioresistant andradiosensitive cell lines has shown that inhibitory effect of microRNA on Integrin signaling pathway is reduced in radioresistant cell line.
Our study of microRNA influence on signaling pathways has demonstrated that Integrin signaling pathway inhibition declines after radiation exposure in radioresistant K562 cell line Figure 3(b).
Some integrin antagonists and some systemic immunosuppressive agents have been associated with progressive multifocal leukoencephalopathy(PML), which is a rare and often fatal opportunistic infection caused by the John Cunningham(JC) virus.
It can be explained by the fact that gelatin is collagen denaturation product, and its structure contains RGD sequence,which binds to integrin receptors on fibroblast membranes and by that triggering their proliferation 18.
The contribution of Skoltech and MIT is that we created andprovided lipid nanoparticles with siRNA to beta 1 integrin that blocked the expression of this gene in the hepatocytes in mice, and subsequent observations, over the phenotype of the model obtained, allowed for the identification of choleangiocytes, which are involved in the regeneration of the liver.
Analysis of microRNA influence on signaling pathways of radioresistant andradiosensitive cell lines shows that the inhibitory effect of microRNA on Integrin signaling pathway is reduced and this effect on General transcription by RNA polymerase I is increased in radioresistant K562 cell line.
Reference: Morozevich G.E., Kozlova N.I., Ushakova N.A., Preobrazhenskaya M.E., Berman A.E.,Implication of integrin α5β1 in human breast carcinoma apoptosis and drug resistance, Biomeditsinskaya khimiya, 2011, vol: 57(1), 77-84.
LRP1 plays a key role in intracellular signaling and endocytosis, which thus implicate it in many cellular and biological processes, including lipid and lipoprotein metabolism, protease degradation,platelet derived growth factor receptor regulation, integrin maturation and recycling, regulation of vascular tone, regulation of blood brain barrier permeability, cell growth, cell migration, inflammation, and apoptosis, as well as diseases such as neurodegenerative diseases, atherosclerosis.