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Human Keratinocyte Migration Involves Extracellular Matrix and Soluble Factors
Published in John J. Lemasters, Constance Oliver, Cell Biology of Trauma, 2020
David T. Woodley, John D. Chen, Elizabeth Shim, Janice P. Kim, Jean-Christophe Lapiere, Christina Peavey
To address this question, we placed human keratinocytes on various matrices with and without the presence of monospecific antibodies to the subunits of various integrin receptors. We found that antibodies to the β1 subunit of integrin receptors, inhibited keratinocyte migration on type I collagen, type IV collagen, and fibronectin.10,11 The β1 subunit is the common subunit for collagen and fibronectin receptors, α2β1 and α5β1, respectively. If we used antibodies monospecific to the α2 subunit, keratinocyte migration was inhibited on matrices of type I and IV collagen, but not on fibronectin. Conversely if we use antibodies to the α5 subunit, keratinocyte migration was inhibited on fibronectin but not on the collagen matrices. This set of experiments demonstrated that the integrin receptors for connective tissue matrices were involved in human keratinocyte motility in a very specific manner.10,11
Integrin Expression in Tumor Progression — Role of Signaling Mechanisms
Published in Róza Ádány, Tumor Matrix Biology, 2017
In small cell carcinoma cell lines β1 expression proved to be predominantly associated with the α3 subunit, but at a lower extent αM and α1 subunits can also be found. The α3β1 integrin proved to be involved in laminin adhesion of small cell carcinoma. Interestingly, neither β4 nor α5 and, correspondingly, α5β1 are expressed by these cell lines.166
Signaling to and from T Cell Integrins
Published in Yoshikazu Takada, Integrins: The Biological Problems, 2017
Members of the (VLA proteins) βl integrin subfamily consist of the β 1 chain (also designated CD29) associated with at least six different α chains to form integrins designated α1β1 to α6β1 (Table l).6 Initial studies of T cells identified α1β1 as an antigen that appeared on T cells that had been activated for several weeks in vitro.19 The “VLA” nomenclature signifies this historical designation of α1β1 (VLA-1) as a “very late antigen” on activated T cells. However, subsequent analysis showed that the β chain in α1β1 is identical to the β chain in the classical fibronectin (FN) receptor, α5β1. Thus, it is important to note that: (1) β1 integrins are expressed on a multitude of other cell types besides lymphocytes, and (2) β1 integrins are expressed on resting as well as activated T cells.
The expression of BMP, integrin, ZEB2 in ovarian high-grade serous carcinoma in relation with lymph node metastasis
Published in Growth Factors, 2022
Elham Bahador Zırh, Elif Taşar Kapaklı, Anıl Dolgun, Alp Usubütün, Naciye Dilara Zeybek
In addition to transcription factors, the alterations in integrin expression play a role in the invasion and metastasis of many cancers. In the previous studies on OCs; αvβ6, β1, α5β1, β4 integrin have been shown to play a role in metastasis and invasion (Ganguly et al. 2012). In epithelial OCs, an increase in β1-integrin expression was associated with increased metastasis of cancer cells. In the same study, inhibition of β1 integrin has been shown to reduce cell motility (Chen et al. 2016). In OC cell lines silencing of β1-integrin resulted in an increase in apoptosis and adhesion and migration reduction (Zhang and Zou 2015). Integrin α5β1 has been reported to increase metastasis and invasion (Mitra et al. 2011). In our study, weak immunoreactivity of integrin α5 and β1 in samples with LN metastasis suggests that tumor cells severed the integrin linkages to leave the ovarian tissue and initiate the EMT process. In the LN samples, the strong immunoreactivity may be explained by the fact that the migrating cells are reintroduced to the MET by reintegration through integrins, thus increasing the integrin immunoreactivity.
Disease progression pathways of wet AMD: opportunities for new target discovery
Published in Expert Opinion on Therapeutic Targets, 2022
Amber T. Wolf, Alon Harris, Francesco Oddone, Brent Siesky, Alice Verticchio Vercellin, Thomas A. Ciulla
SF0166 is a αvβ3 antagonist that has been studied for nAMD treatment as topical ocular drug. A double masked Phase 1/2 study 42 in nAMD patients showed biologic effects in nine of the 42 patients. No drug-related serious adverse events were observed in the 28-day study period or in the 28-day follow-up [60]. There are also a number of IVT α5β1 inhibitors, including volociximab (Ophthotech) and JSM6427 (Jerini Ophthalmic, currently Takeda Pharmaceutical Company) that have been studied in Phase 1, open label, dose escalation studies [57]. Wang and colleagues examined the effect of ATN-161, an α5β1 inhibitor, delivered in combination with anti-VEGF monoclonal antibody in rats with laser-induced CNV and found that the dual inhibition of integrin α5β1 and VEGF jointly inhibited angiogenesis [61].
Targeting the TGF-β signaling pathway for fibrosis therapy: a patent review (2015–2020)
Published in Expert Opinion on Therapeutic Patents, 2021
Xuanyi Li, Ziang Ding, Zixuan Wu, Yinqiu Xu, Hequan Yao, Kejiang Lin
Related inhibitors were developed by simulating the ligands of integrin in vivo. The leading compounds are shown in Table 1. Prakash, J. from Universiteit Twente designed ligand peptides mimicking domains 9 and 10 of fibronectin (FN), in which AV-3 has specific affinity for integrin α5β1 and inhibited fibroblast activation in a concentration-dependent manner [28]. There are similar dipeptide sequences, D-pro-L-pro or related sequences in the peptide structure, that have been designed by Kessler et al from Technische Universitaet Muenchen. This sequence induces the conformational transition of peptide to convey specific affinity for integrin αVβ8, which is much higher than that of other integrins [29]. Tang et al. from University of California, Oakland screened a peptide ligand targeting integrin αvβ6 from the fluorobenzoyl one beam one compound (OBOC) peptide library [30].