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Angiogenesis and Roles of Adhesion Molecules in Psoriatic Disease
Published in Siba P. Raychaudhuri, Smriti K. Raychaudhuri, Debasis Bagchi, Psoriasis and Psoriatic Arthritis, 2017
Asmita Hazra, Saptarshi Mandal
Integrin αvβ3 also happens to be the main endothelial receptor for VWF. VWF is an integral and unique component of the subendothelial basement membrane and is known to be important in angiogenesis. It may modulate angiogenesis partly through interaction with αvβ3 on the activated endothelial cells. In VWF-deficient endothelial cell αvβ3 levels, function and trafficking are known to be decreased, suggesting that VWF may also regulate αvβ3 activity in various ways. Ang2 has been reported to stimulate the internalization and degradation of αvβ3 and may directly or indirectly regulate a VWF effect on angiogenesis.
The αv Integrins
Published in Yoshikazu Takada, Integrins: The Biological Problems, 2017
Candece L. Gladson, David A. Cheresh
The αv subunit is unique among the integrin α subunits in that it potentially associates with at least five structurally distinct β subunits (β3, β5, β1, β6, and β8).1–16 Two additional β subunits that pair with the αv subunit have been identified (β100K and βS), and it remains to be clarified whether or not they are distinct from the β5 subunit.4,17 The αv subunit and the β1 subunit are the most widely expressed integrin subunits in vitro and in situ. In the αv subfamily, αβ heterodimeric pairing determines ligand specificity, like the large integrin family. However, integrin αvβ3 is unique among the αv subfamily in that it is a promiscuous receptor.1–7 The αv integrins play a role in diverse biologic processes, such as tumor cell invasion, metastasis proliferation,1–3,18–24 retinal neunte outgrowth,25,26 differentiation,26–29 bone resorption,30,31 and the immune response.32–38 The entire integrin family, including the αv integrins, is depicted in Figure 1.
Aptamers and Cancer Nanotechnology
Published in Mansoor M. Amiji, Nanotechnology for Cancer Therapy, 2006
Omid C. Farokhzad, Sangyong Jon, Robert Langer
Alpha-v beta-3 (αvβ3) integrin is a transmembrane glycoprotein that mediates numerous processes, including cell migration, cell growth, tumor growth and metastasis, angiogenesis, and vascular healing. The expression of this protein on the endothelial cells of tumor neovasculature is dramatically increased, making αvβ3 an interesting protein for targeting approaches.55 An 85-base-pair 2’-flouropyrimidine RNA aptamer (Apt-αvβ3) has been shown to bind to the αvβ3 protein on the surface of endothelial cells in vitro and inhibit endothelial cell proliferation and survival.56 The future in vivo use of the Apt-αvβ3 may require post-SELEX optimization, including size minimization to facilitate large-scale synthesis, and enhance the pharmacokinetic properties of this molecule. This aptamer may be utilized for targeted cancer diagnostic and therapeutic applications.
Letrozole promotes the expression of integrin αvβ3 and HOXA10 in endometrium of endometriosis
Published in Systems Biology in Reproductive Medicine, 2022
Jing Zhang, Lihui Wang, Chunyan Li, Hui Zhang, Rui Li, Mingjiang Li
Integrin αvβ3 is a cell-surface receptor for extracellular matrix proteins that play an important role in embryo implantation (Lessey et al. 1992; Lessey, Castelbaum et al. 1994). Its expression shows periodic changes, and the peak time is consistent with the implantation window (Tabibzadeh 1992; Lessey et al. 1994a). The expression of integrin αvβ3 is decreased in women with infertility and endometriosis (Lessey et al. 1994a). Estrogen treatment can down-regulate the expression of integrin αvβ3 (Somkuti et al. 1997). HOXA10, = upstream gene integrin αvβ3 (Zhu et al. 2013), is also highly expressed during the implantation window and is a marker of endometrial receptivity (Gui et al. 1999). Estrogen can stimulate the expression of HOXA10, both in the myometrium and the endometrium (Cermik et al. 2001). In endometriosis, calpain7 can down-regulate the expression of HOXA10 via the PEST sequence, and the expression of integrin αvβ3 is also reduced (Yan et al. 2018). In addition, the expression of HOXA10 is decreased in endometriosis due to promoter methylation (Lu et al. 2013).
A bivalent cyclic RGD–siRNA conjugate enhances the antitumor effect of apatinib via co-inhibiting VEGFR2 in non-small cell lung cancer xenografts
Published in Drug Delivery, 2021
Lumin Liao, Bohong Cen, Guoxian Li, Yuanyi Wei, Zhen Wang, Wen Huang, Shuai He, Yawei Yuan, Aimin Ji
In vivo antitumor pharmacodynamic studies in NSCLC A549 tumor xenograft model, we observed that biRGD–siVEGFR2 treatment groups significantly inhibited tumor growth in the early stage, but the inhibitory effect became weaker in the late stage of tumor development. Moreover, there was no obvious dose-dependent in a small range of dosage we tested. The following possible reasons account for this. (1) Limited number of αvβ3 receptors on the surface of neovascular endothelial cells. As biRGD–siVEGFR2 dosage increased, αvβ3 receptors gradually reached to saturation and the additional biRGD–siVEGFR2 molecules had no extra binding sites for endocytosis. (2) Moreover, lower escape capacity of biRGD–siVEGFR2 molecules in the endosome may be the another key factor for its RNAi activity in cytoplasma, which may be overcome by increasing functional structure to promote the release of biRGD–siVEGFR2 molecules from endosome.
Association of ITGAV polymorphisms and risk of rheumatoid arthritis: evidence from a meta-analysis
Published in Expert Review of Clinical Immunology, 2020
Jun-Ming Huang, Zhi-Ying Pang, Guo-Bin Qi, Zhe Wang, Zheng-Tao Lv
Integrins are a large group of transmembrane proteins that mediate adherence between cells and extracellular matrix (ECM), and the upregulation of integrins and their ligands has been reported in RA [10]. Among a wide variety of Integrins, Integrin αvβ3, also called as the vitronectin receptor, is commonly detected in macrophages, synovial fibroblasts, endothelial cells, and osteoclasts. Integrin αvβ3 plays a major role in osteoclast-mediated bone resorption, angiogenesis, and macrophage dependent inflammation, which are widely recognized as the key features of RA pathogenesis [11,12]. Integrin alpha V (ITGAV), also known as CD51, is a protein-coding gene located in the 2q31 region [13]. ITGAV encodes the chain αv, which is a subunit of integrin αvβ3. Several genetic association studies have been conducted to assess the possible association between ITGAV polymorphisms and risk of RA, however, achieved inconsistent results [14–19]. Due to the relatively small sample size, each individual association study might be inadequate to determine the genetic effects of ITGAV polymorphism on RA risk. To the best of our knowledge, no meta-analysis has been carried out to evaluate the correlation between ITGAV polymorphisms and RA risk. Therefore, the present systematic review and meta-analysis was conducted to assess the correlation between ITGAV SNPs and risk of RA.