Disease relevance of ITGAV

• We studied 23 renal cell carcinomas and two normal kidney tissues by immunohistochemistry using monoclonal antibodies against subunits of the VLA integrins (VLA-1 to VLA-6) and CD51 [1].
• Expression of CD51 in the distal airways correlated with the degree of airway obstruction (r = -0.57, P = .001) [2].
• CONCLUSIONS: In Emergency Department patients with unstable angina, early eptifibatide rapidly and profoundly inhibits platelet aggregation and reduces GP IIb/IIIa activity and the expression of CD51/61 and CD 42b; the latter two effects may also contribute to the drug's anti-thrombotic effect [3].
• A novel integrin beta subunit is associated with the vitronectin receptor alpha subunit (alpha v) in a human osteosarcoma cell line and is a substrate for protein kinase C [4].
• DcR3-differentiated cells exhibit characteristics unique for osteoclasts, including polynuclear giant morphology, bone resorption, TRAP, CD51/61, and MMP-9 expression [5].

High impact information on ITGAV

• These cells were shown to have vitronectin beta-receptors using a specific monoclonal antibody, i.e., 23C6 (CD51), which reacts with osteoclasts in human bone biopsy samples [6].
• Intact P. falciparum-infected erythrocytes can bind directly to CD36 and indirectly to CD51 [7].
• Anti-integrin alphavbeta3 MoAb (CD51/CD61; 23C6) only slightly inhibited colony size (P < .05) [8].
• High surface expression of CD49e, CD51, and CD61 along with kit was apparent by 4 weeks of culture, whereas expression of each at day 0 was low to undetectable [9].
• Human mast cells derived from fetal liver cells cultured with stem cell factor express a functional CD51/CD61 (alpha v beta 3) integrin [9].

Biological context of ITGAV

• Cloning and characterisation of ITGAV, the genomic sequence for human cell adhesion protein (vitronectin) receptor alpha subunit, CD51 [10].
• The human locus for the av gene (VNRA) was previously mapped to the long arm of chromosome 2 by DNA analysis of somatic cell hybrids [11].
• Other genes are implicated in signal transduction (ITGAV) or tumorigenesis (AF1q) [12].
• The amino acid sequence of the vitronectin receptor alpha subunit deduced from cDNA is presented [13].
• Could coenzyme Q10 affect hemostasis by inhibiting platelet vitronectin (CD51/CD61) receptor [14]?

Anatomical context of ITGAV

• The 7-kilobase vitronectin receptor alpha subunit mRNA was found to be expressed in all cell lines examined, including endothelial cells, K562 and HEL leukemia cells, and osteosarcoma cells [13].
• Interaction of human Thy-1 (CD 90) with the integrin alphavbeta3 (CD51/CD61): an important mechanism mediating melanoma cell adhesion to activated endothelium [15].
• Human skin mast cells adhere to vitronectin via the alphavbeta3 integrin receptor (CD51/CD61) [16].
• In vitro, monocyte to macrophage transformation occurs in the presence of serum and can be followed by the expression of the maturation-associated antigens gp65-MAX.1, gp68-MAX.3, and CD51 [17].
• It is proposed that either the decrease in the expression of collagen integrin receptor alpha2 (CD 49b), an increase in the expression of the vitronectin receptor alpha(v) (CD 51), or a combination of both is responsible for disruption of collagen fibroblast interactions [18].

Associations of ITGAV with chemical compounds

• The human cDNA for alpha-V integrin (ITGAV) consists of a 5,717-bp transcript with a coding sequence (CDS) of 3,146 bp encoding a 150-kDa mature peptide [10].
• Dietary coenzyme Q10 supplementation alters platelet size and inhibits human vitronectin (CD51/CD61) receptor expression [19].
• PAC-1 (GP IIb/IIIa activity), CD 51/61 (vitronectin receptor) and CD 42b (GP Ib) were inhibited by eptifibatide (p <.05) [3].
• All 18 cysteine residues occur at positions conserved in human GPIIb and the vitronectin receptor alpha subunit VNR alpha [20].
• The Arg-Gly-Asp sequence (RGD), is recognized by many integrins, including integrin alphavbeta3 (CD51/61) [21].

Regulatory relationships of ITGAV

• RA SF presented more cell surface integrins, and monoclonal antibodies against CD51 inhibited the adhesion to COMP by 80% [22].
• CD51 is only weakly expressed by malpighian epithelial cells and does not colocalize with TSP [23].

Other interactions of ITGAV

• Adhesion occurred in part through the CD61/CD51 receptor [9].
• By contrast, CD51, CD54, and CD61 expressions were negligible [24].
• Biochemical analyses show expression of TSP-1 in human cartilage, but its cellular source as well as the presence of its main surface receptors CD36 and CD51 in normal and osteoarthritic cartilage remain unknown [25].
• Localization of thrombospondin, CD36 and CD51 during prenatal development of the human mammary gland [23].
• Immunohistochemistry allowed us to confirm overexpression of the ITGAV and CTSB genes at the protein level and showed a marked relocation of the CTSB protein [12].

Analytical, diagnostic and therapeutic context of ITGAV

• The expression of intracellular galectin-3, or cell surface CD29, CD51, and CD61 was determined by flow cytometry before and after adhesion [22].
• Immunohistologic and Western blot analysis of patient scar fibroblasts showed (1) more a smooth muscle actin within stress fibers, (2) increased expression of the vitronectin integrin receptor alpha(v) (CD 51), and (3) reduced expression of the collagen integrin receptor alpha2 (CD 49b) [18].
• We performed a quantitative evaluation of CD51 receptors on the surface of HeLa cells, a common cell line utilized in many receptor-based studies, and compared them to other similar and dissimilar cell types [26].
• Additionally, PDGF-B producing cells were identified as macrophages in sections taken from an additional patient with CSA DGO by double immunofluorescence labeling of the CD51 membrane marker for macrophages and intracellular PDGF-B [27].

References