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Human Integrin beta 2 Protein expressed in HEK-293 Cells - ABIN2713476
De Franceschi, Peuhu, Parsons, Rissanen, Vattulainen, Salmi, Ivaska, Pouwels: Mutually Exclusive Roles of SHARPIN in Integrin Inactivation and NF-κB Signaling. in PLoS ONE 2015
These results indicate complementary role for LFA-1 and CD28 in the regulation and putative coupling of TCR micro-clusters to actin.
A novel mutation of the ITGB2 gene in a Chinese Zhuang minority patient with leukocyte adhesion deficiency type 1 and glucose-6-phosphate dehydrogenase deficiency.
this study shows that LFA-1 engagement enhances IFN-gamma production by invariant NKT cells
Complement receptor 3 (Integrin alpha-M beta-2)-mediated phagocytosis of Francisella due to increased ras GTPase-activating protein (RasGAP) activity.
After blocking the beta-glucan receptor (CR3) or inhibiting downstream kinase (SYK) in neutrophils, the killing percent to C. albicans (regardless of endemic and non-endemic strains) and the ratio of LC3B-II/I of neutrophils were significantly decreased.
Post-LFA-1 activation, MK2 inducibly associates with both hnRNPC and HuR, resulting in the dissociation of HuR from hnRNPs C, H1 and K. Freed from the three hnRNPs, HuR translocates from the nucleus to the cytoplasm, and mediates the stabilization of labile cytokine transcripts. Modulation of T cell cytokine mRNA half-life is an intricate process that is negatively regulated by hnRNPs C, H1 and K and requires MK2.
CD18-mediated adhesion of extracellular vesicles is a prerequisite for their proinflammatory activity.
The LFA-1-ICAM-1 orientation described here with ICAM-1 pointing anti-parallel to the LFA-1 beta-subunit leg is the same orientation that would be stabilized by tensile force transmitted between the ligand and the actin cytoskeleton and is consistent with the cytoskeletal force model of integrin activation.
LncRNA ITGB2-AS1 could promote the migration and invasion of breast cancer cells by up-regulating ITGB2.
Data show that integrin alphaLbeta2 (LFA-1) is oriented relative to actin retrograde flow.
Overexpression of ITGB2 was not correlated with ITGB2 promoter hypomethylation in systemic sclerosis.
actin engagement produces tension within the beta2 subunit to induce and stabilize an active integrin conformational state and that this requires intact talin and kindlin motifs.
on tumour-infiltrating T-lymphocytes, galectin prevents the formation of a functional secretory synapse by preventing optimal LFA-1 triggering
exploration of the underlying mechanism demonstrated that ICAM3 not only binds to LFA-1 with its extracellular domain and structure protein ERM but also to lamellipodia with its intracellular domain which causes a tension that pulls cells apart (metastasis).
vesicle-associated RhoB is a regulator of the Rab11-mediated recycling of LFA-1 to the cell surface, an event that is necessary for T lymphocyte motility.
alphaMbeta2 uses its alphaI domain to bind iC3b at the thioester domain and simultaneously interacts through a region near the alphaM beta-propeller and beta2 betaI domain with a region of the C3c moiety near the C345C domain.
The ITGB2 variant rs2230531 was examined in an independent cohort of Tasmanian patients with hematologic malignancies (HM) to see if its presence correlated with chronic lymphocytic leukemia. The variant was found in several lymphoid and myeloid HMs, so if contributes to the risk of HM, it does so broadly across HM subtypes in this population.
Data suggest that the residue volume at phenylalanine (Phe) in alpha1-helix is critical for alpha(L)/beta(2) integrin (CD49a/CD18) activation and binding with soluble/immobilized ICAM1 (intercellular cell adhesion molecule 1).
an integrated strategy of whole genome and transcriptome analysis enabled identification of LB-ITGB2-1 as HLA-B*15:01-restricted MiHAs encoded by an alternative transcript. The alternative ITGB2 transcript was shown to be expressed in leukemic cells of different origins.
Neutrophil rolling over E-selectin at precise shear stress transmits tension and catch-bond formation with L-selectin via sLe(x), resulting in focal clusters that deliver a distinct signal to upshift beta2-integrins to a high-affinity state. Rivipansel effectively blocked formation of selectin catch-bonds, revealing a novel mechanotransduction circuit
Findings identify Crk proteins as key intermediates coupling LFA-1 signals to actin remodeling and provide mechanistic insights into how T cells sense and respond to substrate stiffness.
this study shows that CD18 regulates monocyte hematopoiesis and promotes resistance to experimental schistosomiasis
findings identified cross-talk between JAK2-V617F and integrin activation promoting pathologic thrombosis and abnormal trafficking of leukocytes to the spleen.
Neutrophil CD11b/CD18 limits pathology in influenza-induced, T cell-mediated disease.
We show that during T cell migration within lymphatic organs the contributions of the integrin LFA-1 and the chemokine receptor CCR7 are complementary rather than positioned in a linear pathway, as they are during leukocyte extravasation from the blood vasculature
LFA-1 dominates polymorphonuclear leukocyte (PMN) adhesion on ICAM-1 and ICAM-2, while Mac-1 mediates PMN adhesion on RAGE, JAM-A, and JAM-C
CD18(-/-) leukocytes extravasated later than WT leukocytes. However, once extravasated, CD18(-/-) leukocytes transmigrated more rapidly than their WT counterparts. These results suggest that, although CD18 facilitates efficient extravasation, outside of the vessel CD18 interaction with the extracellular matrix, it reduced transmigration velocity.
A modulatory role for the tumor beta2 subunit of the LFA-1 integrin in the metastatic progression of colorectal cancer to the liver by impaired activation of liver endothelium.
Data show CD18 is selectively required for T helper 2, but not T helper 1, homing and has a minimal influence on T-effector development.
Adhesive properties of the leukocyte integrin Mac-1 are not required for macrophage accumulation in adipose tissue. Instead, Mac-1 modulates inflammatory gene expression in macrophages.
in T cells, PI3Kdelta attenuates the activation of Rac1, but sustains the activation of Rap1.
An intracellular pool of LFA-1 in naive CD8(+) T cells plays a key role in T cell activation and differentiation.
Extracellular ISG15 signals cytokine secretion through the LFA-1 integrin receptor (CD11a/CD18) in natural killer cells.
CD18 deficiency curbs methionine-choline-deficient-mediated liver injury by limiting the activation of innate immune cells in the liver without compromising intrahepatic cytokine activation
results identify a role for Caveolin (Cav)1in membrane organization and beta2 integrin Lfa1 function in primary CD8 T cells.
Coro1A represents an important novel player in integrin biology, with key functions in polymorphonuclear neutrophils trafficking during innate immunity.
The data disclose a previously unknown function for alpha(1,3)-fucose, in which this structure negatively regulates the integrin activation step in leukocyte recruitment.
These results identify CD47 as an important regulator of LFA-1 and VLA-4 integrin-adhesive functions in T cell proliferation.
both GDF-15 and TGF-beta1 counteract chemokine-induced integrin activation on neutrophils via the ALK-5/TGF-betaRII heterodimer.
missense variants in the CD18 signal peptide affect Leukotoxin binding.
Identification of numerous variations in exonic and intronic regions within the ITGB2 gene in Bos taurus and indicus screened for bovine leukocyte adhesion deficiency.
intramammarily administered lipopolysaccharides seem to play an important role in modulating L-selectin and beta2 integrin expression on circulating bovine polymorphonuclear leukocytes
A delay in apoptosis was demonstrated in CD18-deficient bovine neutrophils and this appeared to be closely associated with lowered signalling via [Ca2+]i, diminished annexin V expression on the cell surface, and decreased caspase 3 activity in lysates
The I-EGF-3 domain of bovine CD18 (amino acid residues 541-581) is critical for conferring species-specific susceptibility to Mannheimia haemolytica leukotoxin.
These results clearly indicate that the bovine CD18 subunit of beta(2)-integrins is the functional receptor for M. haemolytica Lkt.[ruminant-specific leukotoxin]
study provides evidence that the expression of CD18 was downregulated by the plasma glycoforms of alpha-1 acid glycoprotein and inhibited the chemotaxis of monocytes
Loss of CD18 is associated with bovine leukocyte adhesion deficiency.
Intact signal peptide of CD18, the beta-subunit of beta2-integrins, renders ruminants susceptible to Mannheimia haemolytica leukotoxin.
CR3 plays a cardinal role in beta-glucan signalling in porcine neutrophils, while macrophages use a more diverse receptor array to detect and respond towards beta-glucans.
The expression of zona pellucida glycoprotein 3 and integrin beta-2 in oocytes after brilliant cresyl blue staining is reported.
early CD18 downregulation is profitable for the host in a situation with an intense LPS stimulus
It is concluded that porcine CD18 is necessary to mediate A. pleuropneumoniae ApxIIIA toxin-induced leukolysis.
Integrin CD11c/CD18 alpha-chain phosphorylation is functionally important.
The product of this gene belongs to the integrin beta chain family of proteins. Integrins are integral cell-surface proteins composed of an alpha chain and a beta chain. This gene encodes the integrin beta chain beta 2. A given chain may combine with multiple partners resulting in different integrins. For example, beta 2 combines with the alpha L chain to form the integrin LFA-1, and combines with the alpha M chain to form the integrin Mac-1. Integrins are known to participate in cell adhesion as well as cell-surface mediated signalling. Defects in this gene are the cause of leukocyte adhesion deficiency type I (LAD1). Two transcript variants encoding the same protein have been identified for this gene.
cell surface adhesion glycoprotein LFA-1/CR3/P150,959 beta subunit precursor)
, cell surface adhesion glycoproteins LFA-1/CR3/p150,95 subunit beta
, complement receptor C3 beta-subunit
, complement receptor C3 subunit beta
, integrin beta chain, beta 2
, integrin beta-2
, leukocyte cell adhesion molecule CD18
, leukocyte-associated antigens CD18/11A, CD18/11B, CD18/11C
, Mac-1 beta
, lymphocyte function associated antigen 1
, macrophage antigen-1 beta
, CD18 subunit
, Leu-CAM receptor
, integrin, beta 2 (antigen CD18 subunit (p95), lymphocyte function-associated antigen 1, integrin B2)
, integrin beta 2 subunit
, CD18 leukocyte adhesion molecule
, antigen CD18
, integrin beta-2 chain
, integrin beta 2
, integrin, beta 2 (antigen CD18 (p95), lymphocyte function-associated antigen 1
, integrin, beta 2 (antigen CD18 (p95), lymphocyte function-associated antigen 1; macrophage antigen 1 (mac-1) beta subunit)
, macrophage antigen 1 (mac-1) beta subunit)
, Cell surface adhesion glycoproteins LFA-1/CR3/p150,95 subunit beta
, Complement receptor C3 subunit beta
, Integrin beta-2
, integrin beta-2 subunit
, integrin subunit beta 2 S homeolog
, integrin, beta 2 (complement component 3 receptor 3 and 4 subunit)