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Journal articles on the topic 'Integrin-targeting'

Author: Grafiati

Published: 3 June 2025

Last updated: 31 July 2025

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1

Boettner, Benjamin. "Targeting fibrotic integrin." Science-Business eXchange 6, no. 46 (2013): 1308. http://dx.doi.org/10.1038/scibx.2013.1308.

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Estevez, Brian, Bo Shen, and Xiaoping Du. "Targeting Integrin and Integrin Signaling in Treating Thrombosis." Arteriosclerosis, Thrombosis, and Vascular Biology 35, no. 1 (2015): 24–29. http://dx.doi.org/10.1161/atvbaha.114.303411.

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Färber, Stefanie Felicitas, Alexander Wurzer, Florian Reichart та ін. "Therapeutic Radiopharmaceuticals Targeting Integrin αvβ6". ACS Omega 3, № 2 (2018): 2428–36. http://dx.doi.org/10.1021/acsomega.8b00035.

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4

Egorova, Elena A., and Maxim P. Nikitin. "Delivery of Theranostic Nanoparticles to Various Cancers by Means of Integrin-Binding Peptides." International Journal of Molecular Sciences 23, no. 22 (2022): 13735. http://dx.doi.org/10.3390/ijms232213735.

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Active targeting of tumors is believed to be the key to efficient cancer therapy and accurate, early-stage diagnostics. Active targeting implies minimized off-targeting and associated cytotoxicity towards healthy tissue. One way to acquire active targeting is to employ conjugates of therapeutic agents with ligands known to bind receptors overexpressed onto cancer cells. The integrin receptor family has been studied as a target for cancer treatment for almost fifty years. However, systematic knowledge on their effects on cancer cells, is yet lacking, especially when utilized as an active target

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Ye, Yunpeng, and Xiaoyuan Chen. "Integrin Targeting for Tumor Optical Imaging." Theranostics 1 (2011): 102–26. http://dx.doi.org/10.7150/thno/v01p0102.

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Burkhart, David J., Brian T. Kalet, Michael P. Coleman, Glen C. Post та Tad H. Koch. "Doxorubicin-formaldehyde conjugates targeting αvβ3 integrin". Molecular Cancer Therapeutics 3, № 12 (2004): 1593–604. http://dx.doi.org/10.1158/1535-7163.1593.3.12.

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Abstract We have reported the synthesis and biological evaluation of a prodrug to a doxorubicin active metabolite. Under physiologic conditions, release of the active metabolite, a conjugate of doxorubicin with formaldehyde, occurs with a half-life of 1 hour. To direct this prodrug to tumor, we designed two conjugates of the prodrug, doxsaliform, with the αvβ3-targeting peptides, CDCRGDCFC (RGD-4C) and cyclic-(N-Me-VRGDf) (Cilengitide). We now report the synthesis of these doxsaliform-peptide conjugates and their evaluation using MDA-MB-435 cancer cells. A hydroxylamine ether tether was used t

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Cai, Weibo, Sanjiv Sam Gambhir та Xiaoyuan Chen. "Multimodality tumor imaging targeting integrin αvβ3". BioTechniques 39, № 6S (2005): S14—S25. http://dx.doi.org/10.2144/000112091.

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E. Hagemeyer, Christoph, and Karlheinz Peter. "Targeting the Platelet Integrin GPIIb/IIIa." Current Pharmaceutical Design 16, no. 37 (2010): 4119–33. http://dx.doi.org/10.2174/138161210794519255.

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Cheng, Tsai-Mu, Wong-Jin Chang, Hsiu-Yi Chu та ін. "Nano-Strategies Targeting the Integrin αvβ3 Network for Cancer Therapy". Cells 10, № 7 (2021): 1684. http://dx.doi.org/10.3390/cells10071684.

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Integrin αvβ3, a cell surface receptor, participates in signaling transduction pathways in cancer cell proliferation and metastasis. Several ligands bind to integrin αvβ3 to regulate proliferation and metastasis in cancer cells. Crosstalk between the integrin and other signal transduction pathways also plays an important role in modulating cancer proliferation. Carcinoembryonic antigen cell adhesion molecule 6 (CEACAM6) activates the downstream integrin FAK to stimulate biological activities including cancer proliferation and metastasis. Blockage of signals related to integrin αvβ3 was shown t

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Jiang, Yaqun, Yu Long, Hao Ji та ін. "Development and Evaluation of a Peptide Heterodimeric Tracer Targeting CXCR4 and Integrin αvβ3 for Pancreatic Cancer Imaging". Pharmaceutics 14, № 9 (2022): 1791. http://dx.doi.org/10.3390/pharmaceutics14091791.

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Nowadays, pancreatic cancer is still a formidable disease to diagnose. The CXC chemokine receptor 4 (CXCR4) and integrin αvβ3 play important roles in tumor development, progression, invasion, and metastasis, which are overexpressed in many types of human cancers. In this study, we developed a heterodimeric tracer 68Ga-yG5-RGD targeting both CXCR4 and integrin αvβ3, and evaluated its feasibility and utility in PET imaging of pancreatic cancer. The 68Ga-yG5-RGD could accumulate in CXCR4/integrin αvβ3 positive BxPC3 tumors in a high concentration and was much higher than that of 68Ga-yG5 (p <

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López Rivas, Paula, Christoph Müller, Christian Breunig та ін. "β-Glucuronidase triggers extracellular MMAE release from an integrin-targeted conjugate". Organic & Biomolecular Chemistry 17, № 19 (2019): 4705–10. http://dx.doi.org/10.1039/c9ob00617f.

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Hakanpaa, Laura, Elina A. Kiss, Guillaume Jacquemet та ін. "Targeting β1-integrin inhibits vascular leakage in endotoxemia". Proceedings of the National Academy of Sciences 115, № 28 (2018): E6467—E6476. http://dx.doi.org/10.1073/pnas.1722317115.

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Loss of endothelial integrity promotes capillary leakage in numerous diseases, including sepsis, but there are no effective therapies for preserving endothelial barrier function. Angiopoietin-2 (ANGPT2) is a context-dependent regulator of vascular leakage that signals via both endothelial TEK receptor tyrosine kinase (TIE2) and integrins. Here, we show that antibodies against β1-integrin decrease LPS-induced vascular leakage in murine endotoxemia, as either a preventative or an intervention therapy. β1-integrin inhibiting antibodies bound to the vascular endothelium in vivo improved the integr

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Sawada, Kenjiro, Chifumi Ohyagi-Hara, Tadashi Kimura, and Ken-ichirou Morishige. "Integrin Inhibitors as a Therapeutic Agent for Ovarian Cancer." Journal of Oncology 2012 (2012): 1–6. http://dx.doi.org/10.1155/2012/915140.

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Ovarian cancer is a deadly disease, with a cure rate of only 30%. Despite aggressive treatments, relapse remains almost inevitable in patients with advanced-stage disease. In recent years, great progress has been made towards targeting integrins in cancer treatment, and clinical studies with various integrin inhibitors have demonstrated their effectiveness in blocking cancer progression. Given that the initial critical step of ovarian cancer metastasis is the attachment of cancer cells onto the peritoneum or omentum, in addition to the proven positive clinical results of anti-angiogenic therap

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Dobson, Hannah E., Shasha Ruan, Alfred E. Chang, Max S. Wicha та Qiao Li. "Targeting cancer stem cells via integrin β4". Oncotarget 12, № 18 (2021): 1850–58. http://dx.doi.org/10.18632/oncotarget.27977.

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15

Nam, Jin-Min, Yoonsun Chung, Howard C. Hsu та Catherine C. Park. "β1 integrin targeting to enhance radiation therapy". International Journal of Radiation Biology 85, № 11 (2009): 923–28. http://dx.doi.org/10.3109/09553000903232876.

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16

Shallal, Hassan M., Il Minn, Sangeeta R. Banerjee, Ala Lisok, Ronnie C. Mease та Martin G. Pomper. "Heterobivalent Agents Targeting PSMA and Integrin-αvβ3". Bioconjugate Chemistry 25, № 2 (2014): 393–405. http://dx.doi.org/10.1021/bc4005377.

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Vicente-Manzanares, Miguel, and Francisco Sánchez-Madrid. "Targeting the integrin interactome in human disease." Current Opinion in Cell Biology 55 (December 2018): 17–23. http://dx.doi.org/10.1016/j.ceb.2018.05.010.

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18

Nemerow, Glen R. "Integrin-Targeting Strategies for Adenovirus Gene Therapy." Viruses 16, no. 5 (2024): 770. http://dx.doi.org/10.3390/v16050770.

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Numerous human adenovirus (AdV) types are endowed with arginine–glycine–aspartic acid (RGD) sequences that enable them to recognize vitronectin-binding (αv) integrins. These RGD-binding cell receptors mediate AdV entry into host cells, a crucial early step in virus infection. Integrin interactions with adenoviruses not only initiate receptor-mediated endocytosis but also facilitate AdV capsid disassembly, a prerequisite for membrane penetration by AdV protein VI. This review discusses fundamental aspects of AdV–host interactions mediated by integrins. Recent efforts to re-engineer AdV vectors

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Shlamkovich, Tomer, Lidan Aharon, Dana Koslawsky, Yulia Einav та Niv Papo. "Targeting the Tie2–αvβ3 integrin axis with bi-specific reagents for the inhibition of angiogenesis". BMC Biology 16, № 1 (2018): 92. https://doi.org/10.1186/s12915-018-0557-9.

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<strong>Background: </strong>Increased activity of the receptor tyrosine kinase Tie2 has been implicated in the promotion of pathological angiogenesis. This activity is mainly mediated through angiopoietin (Ang)1- and Ang2-dependent activation of integrins by Tie2, rendering the Ang/Tie2/integrin axis an attractive putative target for cancer therapeutics.<strong>Results: </strong>To target this axis, we developed single domain, non-immunoglobulin high-affinity bi-specific protein inhibitors against both Tie2 and α<sub>v</sub>β<sub>3</sub> integrin. We have previously engineered the Ang2-bindin

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Yu, Chi, Wei Jiang, Bin Li, Yong Hu, and Dan Liu. "The Role of Integrins for Mediating Nanodrugs to Improve Performance in Tumor Diagnosis and Treatment." Nanomaterials 13, no. 11 (2023): 1721. http://dx.doi.org/10.3390/nano13111721.

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Integrins are heterodimeric transmembrane proteins that mediate adhesive connections between cells and their surroundings, including surrounding cells and the extracellular matrix (ECM). They modulate tissue mechanics and regulate intracellular signaling, including cell generation, survival, proliferation, and differentiation, and the up-regulation of integrins in tumor cells has been confirmed to be associated with tumor development, invasion, angiogenesis, metastasis, and therapeutic resistance. Thus, integrins are expected to be an effective target to improve the efficacy of tumor therapy.

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Artz, Annette, Stefan Butz та Dietmar Vestweber. "GDF-15 inhibits integrin activation and mouse neutrophil recruitment through the ALK-5/TGF-βRII heterodimer". Blood 128, № 4 (2016): 529–41. http://dx.doi.org/10.1182/blood-2016-01-696617.

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Key Points A classical TGF-β receptor pair counteracts extravasation of myeloid cells by rapidly interfering with integrin activation. GDF-15 and TGF-β1 inhibit leukocyte integrin activation by targeting the Rap-1 GTPase exchange factor CalDAG-GEF1.

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Alday-Parejo, Stupp, and Rüegg. "Are Integrins Still Practicable Targets for Anti-Cancer Therapy?" Cancers 11, no. 7 (2019): 978. http://dx.doi.org/10.3390/cancers11070978.

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Correlative clinical evidence and experimental observations indicate that integrin adhesion receptors, in particular those of the αV family, are relevant to cancer cell features, including proliferation, survival, migration, invasion, and metastasis. In addition, integrins promote events in the tumor microenvironment that are critical for tumor progression and metastasis, including tumor angiogenesis, matrix remodeling, and the recruitment of immune and inflammatory cells. In spite of compelling preclinical results demonstrating that the inhibition of integrin αVβ3/αVβ5 and α5β1 has therapeuti

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Masoumi, Katarzyna Chmielarska, Xiaoli Huang, Wondossen Sime та ін. "Integrin α10-Antibodies Reduce Glioblastoma Tumor Growth and Cell Migration". Cancers 13, № 5 (2021): 1184. http://dx.doi.org/10.3390/cancers13051184.

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Glioblastoma (GB) is the most common and the most aggressive form of brain tumor in adults, which currently lacks efficient treatment strategies. In this study, we investigated the therapeutic effect of function-blocking antibodies targeting integrin α10β1 on patient-derived-GB cell lines in vitro and in vivo. The in vitro studies demonstrated significant inhibiting effects of the integrin α10 antibodies on the adhesion, migration, proliferation, and sphere formation of GB cells. In a xenograft mouse model, the effect of the antibodies on tumor growth was investigated in luciferase-labeled and

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Elsharif, Amal A., Laurence H. Patterson, Steven D. Shnyder та Helen M. Sheldrake. "K562 Chronic Myeloid Leukemia Cells as a Dual β3-Expressing Functional Cell Line Model to Investigate the Effects of Combined αIIbβ3 and αvβ3 Antagonism". Methods and Protocols 8, № 4 (2025): 73. https://doi.org/10.3390/mps8040073.

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Several of the integrin family of cell adhesion receptors have been popular targets for the development of anticancer agents, but with little clinical success to date. Cancer cells usually express multiple redundant integrins; one hypothesis for the lack of efficacy of current antagonists is their high selectivity for a single integrin. To address this, we developed a functional dual-β3-expressing cell model to investigate the effects of combined αIIbβ3/αvβ3 antagonism. We established that treating K562 chronic myeloid leukemia cells with 0.04 μM phorbol 12-myristate 13-acetate (PMA) for 40 h

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Kossatz, Susanne, Ambros Johannes Beer та Johannes Notni. "It’s Time to Shift the Paradigm: Translation and Clinical Application of Non-αvβ3 Integrin Targeting Radiopharmaceuticals". Cancers 13, № 23 (2021): 5958. http://dx.doi.org/10.3390/cancers13235958.

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For almost the entire period of the last two decades, translational research in the area of integrin-targeting radiopharmaceuticals was strongly focused on the subtype αvβ3, owing to its expression on endothelial cells and its well-established role as a biomarker for, and promoter of, angiogenesis. Despite a large number of translated tracers and clinical studies, a clinical value of αvβ3-integrin imaging could not be defined yet. The focus of research has, thus, been moving slowly but steadily towards other integrin subtypes which are involved in a large variety of tumorigenic pathways. Pepti

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Chakraborty, Indira, Anirban Roy та Aniruddha Banerji. "The Role of All-trans Retinoic Acid (ATRA) As A Potential Downregulator of Integrin α5β1 Mediated Signalling in Melanomas". South Asian Journal of Experimental Biology 14, № 6 (2025): 282–93. https://doi.org/10.38150/sajeb.14(6).p282-293.

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Integrin α5β1 plays an important role in promoting tumour metastasis in melanomas which have the highest mortality rate among all dermatological cancers. Interactions of fibronectin with integrin α5β1 activates cellular signalling through phosphatidylinositol 3’ kinase (PI3K) and extracellular signal regulated kinase (ERK) pathways. Synthetic inhibitors have been used for targeting integrins and integrin mediated signalling pathways but such therapies are often hindered by toxicity or by a lack of efficacy. In our present study, the effects of the phytochemical all-trans retinoic acid (ATRA) o

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Matsuura, Shinobu, Siyang Long, Iris Karkempetzaki, et al. "Targeting the JAK2V617F Hematopoietic Stem Cell through Beta1 Integrin." Blood 142, Supplement 1 (2023): 4517. http://dx.doi.org/10.1182/blood-2023-186090.

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The major barrier to progress in treatment of primary myelofibrosis (PMF) is the lack of effective therapies targeting the malignant JAK2 V617F hematopoietic stem cell (HSC), the source of disease progression and relapse. Expression of JAK2 V617F induces abnormal proliferation and differentiation of HSC, affecting all blood lineages but most prominently the erythro-megakaryocytic lineage, leading to clonal megakaryocyte proliferation, erythrocytosis and thrombocytosis. In our previously published work ( Matsuura et al, Blood 2020) we identified elevated expression of the α5 subunit of the α5β1

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Yau, Enoch, Melissa Lim, Zoya Qaiyum, et al. "Effect of Integrin Blockade on Experimental Spondyloarthritis." Biomolecules 14, no. 11 (2024): 1386. http://dx.doi.org/10.3390/biom14111386.

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Spondyloarthritis (SpA) describes a group of diseases characterized by chronic inflammation in the spine and peripheral joints. While pathogenesis is still unclear, proinflammatory gut-derived immune cells have been identified in the joints of SpA patients. We previously identified an enriched population of integrin-expressing cells in the joints of SpA patients. Entry of gut-derived cells into joints may be mediated by these integrins. In the current study, we used the SKG murine model of SpA to study the impact of integrin blockade. Mice were injected with antibodies against the integrin α4β

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Alahmari, Bader, Jaebok Choi, Matthew L. Cooper, Kiran R. Vij, Julie Ritchey, and John F. DiPersio. "Targeting Alpha 4 Integrin (CD49d) to Reduce GvHD." Blood 126, no. 23 (2015): 4283. http://dx.doi.org/10.1182/blood.v126.23.4283.4283.

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Abstract Acute graft versus host disease (aGvHD) is a life-threatening condition that complicates allogeneic hematopoietic cell transplantation (allo-HCT). Donor T cells recognize the recipientÕs tissues as foreign causing GvHD, however, these same donor T cells are also responsible for the beneficial graft versus leukemia (GVL). Distinguishing between GvHD and GvL is crucial for the development of safe and effective therapies following allogeneic bone marrow transplantation. We have recently reported that the disruption of alloreactive donor T cell trafficking to the GvHD target organs signif

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Carney, Randy P., Sidhartha Hazari, Tatu Rojalin, et al. "Targeting Tumor-Associated Exosomes with Integrin-Binding Peptides." Advanced Biosystems 1, no. 5 (2017): 1600038. http://dx.doi.org/10.1002/adbi.201600038.

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Dhavalikar, Prachi, Andrew Robinson, Ziyang Lan, et al. "Review of Integrin‐Targeting Biomaterials in Tissue Engineering." Advanced Healthcare Materials 9, no. 23 (2020): 2000795. http://dx.doi.org/10.1002/adhm.202000795.

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Bogdanović, Bojana, Daniel Fagret, Catherine Ghezzi, and Christopher Montemagno. "Integrin Targeting and Beyond: Enhancing Cancer Treatment with Dual-Targeting RGD (Arginine–Glycine–Aspartate) Strategies." Pharmaceuticals 17, no. 11 (2024): 1556. http://dx.doi.org/10.3390/ph17111556.

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Integrins, an important superfamily of cell adhesion receptors, play an essential role in cancer progression, metastasis, and angiogenesis, establishing them as prime targets for both diagnostic and therapeutic applications. Despite their significant potential, integrin-targeted therapies have faced substantial challenges in clinical trials, including variable efficacy and unmet high expectations. Nevertheless, the consistent expression of integrins on tumor and stromal cells underscores their ongoing relevance and potential. Traditional RGD-based imaging and therapeutic agents have faced limi

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Fasoulakis, Zacharias, Michaela-Zoi Psarommati, Angeliki Papapanagiotou, et al. "MicroRNAs Can Influence Ovarian Cancer Progression by Dysregulating Integrin Activity." Cancers 15, no. 18 (2023): 4449. http://dx.doi.org/10.3390/cancers15184449.

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Ovarian cancer is a deadly disease that affects thousands of women worldwide. Integrins, transmembrane receptors that mediate cell adhesion and signaling, play important roles in ovarian cancer progression, metastasis, and drug resistance. Dysregulated expression of integrins is implicated in various cellular processes, such as cell migration, invasion, and proliferation. Emerging evidence suggests that microRNAs (miRNAs) can regulate integrin expression and function, thus affecting various physiological and pathological processes, including ovarian cancer. In this article, we review the curre

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Wang, Feng, Ying Xin, James J. Moon, Alfred E. Chang, Max Wicha та Qiao Li. "Abstract 2788: Immunological targeting of integrin β1high/β3high melanoma". Cancer Research 84, № 6_Supplement (2024): 2788. http://dx.doi.org/10.1158/1538-7445.am2024-2788.

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Abstract We previously reported two integrin β4 (ITGB4)-targeted immunologic strategies, e.g., ITGB4 protein-pulsed dendritic cells (ITGB4-DC) for vaccination and adoptive transfer of anti-CD3/anti-ITGB4 bispecific antibody (ITGB4 BiAb)-armed tumor draining lymph node (TDLN) T cells. Both immunotherapies significantly demonstrated efficacy in inhibiting local tumor growth and lung metastases. We found these therapeutic efficacies were closely associated with the T cell as well as humoral anti-integrin β4high cancer stem cells (CSCs) in breast (4T1) and head and neck squamous cell carcinoma (SC

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Song, Fei, Kevin Do, Daniel E. C. Fein, Narges Jahanseir, Raghav Joshi та Paul Mathew. "Dual targeting of αv and α5β1 integrins in triple-negative breast cancer (TNBC)." Journal of Clinical Oncology 42, № 16_suppl (2024): e15073-e15073. http://dx.doi.org/10.1200/jco.2024.42.16_suppl.e15073.

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e15073 Background: Integrin αv has been implicated in a stem-phenotype of breast cancer (1) and is cross-regulated by fibronectin-binding integrin α5β1 in tumor cells (2). We hypothesized that these integrins are expressed in TNBC cells and dual targeting of αv and α5β1 integrins by a bispecific antibody (BsAbαv/α5β1) will be superior to monospecific integrin antibodies (MsAbs) alone or in combination. Methods: A representative panel of basal-subtype TNBC lines was assembled: MDA-MB-231 (P53 mutated, KRAS mutated), MDA-MB-468 (P53 mutated, PTEN deleted, EGFR amplified) and BT-20 (P53 and PIK3C

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Grande-García, A., A. Echarri, and M. A. Del Pozo. "Integrin regulation of membrane domain trafficking and Rac targeting." Biochemical Society Transactions 33, no. 4 (2005): 609–13. http://dx.doi.org/10.1042/bst0330609.

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Integrins are crucial regulators of essential cellular processes such as gene expression, cell proliferation and migration. Alteration of these processes is central to tumourigenesis. Integrin signals mediate anchorage dependence of cell growth, while growth of cancer cells is anchorage-independent. Integrins critically regulate Rho family GTPases, that are also involved in cell-cycle progression and oncogenesis. In addition to their effect on GTP loading, integrins independently control the translocation of GTP-bound Rac to the plasma membrane. This step is essential for Rac binding to effect

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Sutherland, Mark, Andrew Gordon, Fatemah O. F. O. Al-Shammari та ін. "Synthesis and Biological Evaluation of Cyclobutane-Based β3 Integrin Antagonists: A Novel Approach to Targeting Integrins for Cancer Therapy". Cancers 15, № 16 (2023): 4023. http://dx.doi.org/10.3390/cancers15164023.

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The Arg-Gly-Asp (RGD)-binding family of integrin receptors, and notably the β3 subfamily, are key to multiple physiological processes involved in tissue development, cancer proliferation, and metastatic dissemination. While there is compelling preclinical evidence that both αvβ3 and αIIbβ3 are important anticancer targets, most integrin antagonists developed to target the β3 integrins are highly selective for αvβ3 or αIIbβ3. We report the design, synthesis, and biological evaluation of a new structural class of ligand-mimetic β3 integrin antagonist. These new antagonists combine a high activit

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Chae, Young Chan, Kyung Lock Kim, Sang Hoon Ha, Jaeyoon Kim, Pann-Ghill Suh та Sung Ho Ryu. "Protein Kinase Cδ-Mediated Phosphorylation of Phospholipase D Controls Integrin-Mediated Cell Spreading". Molecular and Cellular Biology 30, № 21 (2010): 5086–98. http://dx.doi.org/10.1128/mcb.00443-10.

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ABSTRACT Integrin signaling plays critical roles in cell adhesion, spreading, and migration, and it is generally accepted that to regulate these integrin functions accurately, localized actin remodeling is required. However, the molecular mechanisms that control the targeting of actin regulation molecules to the proper sites are unknown. We previously demonstrated that integrin-mediated cell spreading and migration on fibronectin are dependent on the localized activation of phospholipase D (PLD). However, the mechanism underlying PLD activation by integrin is largely unknown. Here we demonstra

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Nam, Arin, Shashi Jain, Alejandro Campos та ін. "Abstract 3066: Lung cancer cells overcome nutrient stress by upregulating an integrin αvβ3/AMPK/OXPHOS axis". Cancer Research 84, № 6_Supplement (2024): 3066. http://dx.doi.org/10.1158/1538-7445.am2024-3066.

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Abstract Tumor cells are exposed to various forms of stress within the tumor microenvironment, and those cells that adapt often gain stem-like properties that facilitate tumor initiation and metastasis. Here, we show that lung cancer cells exposed to nutrient stress adapt and survive by converting their metabolism from glycolytic to oxidative phosphorylation (OXPHOS). This is based on the cell’s ability to upregulate expression of integrin αvβ3, a driver of tumor initiation, progression, and drug resistance. Mechanistically, integrin αvβ3 recruits and activates c-Src, promoting sustained AMPK

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40

Yue, Xiling, Alma R. Morales, Grace W. Githaiga, et al. "RGD-conjugated two-photon absorbing near-IR emitting fluorescent probes for tumor vasculature imaging." Organic & Biomolecular Chemistry 13, no. 43 (2015): 10716–25. http://dx.doi.org/10.1039/c5ob01536g.

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Dhanesha, Nirav, Manasa K. Nayak, Prakash Doddapattar та ін. "Targeting myeloid-cell specific integrin α9β1 inhibits arterial thrombosis in mice". Blood 135, № 11 (2020): 857–61. http://dx.doi.org/10.1182/blood.2019002846.

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Abstract Evidence suggests that neutrophils contribute to thrombosis via several mechanisms, including neutrophil extracellular traps (NETs) formation. Integrin α9β1 is highly expressed on neutrophils when compared with monocytes. It undergoes affinity upregulation on neutrophil activation, and stabilizes adhesion to the activated endothelium. The role of integrin α9 in arterial thrombosis remains unexplored. We generated novel myeloid cell-specific integrin α9−/− mice (α9fl/flLysMCre+) to study the role of integrin α9 in arterial thrombosis. α9fl/fl littermates were used as controls. We repor

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Dhanesha, Nirav, Manasa K. Nayak, Prakash Doddapattar та Anil K. Chauhan. "Targeting Myeloid-Cell Specific Integrin α9β1 Inhibits Arterial Thrombosis in Mice". Blood 134, Supplement_1 (2019): 3581. http://dx.doi.org/10.1182/blood-2019-127006.

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Background: Coordinated interactions between neutrophils, platelets and endothelial cells contribute towards the development of arterial thrombosis. Neutrophils along with platelets are the first immune cells that are recruited at the site of endothelial activation/injury or infection. Recent studies have suggested that neutrophils modulate thrombosis via several mechanisms, including NETosis (formation of neutrophil extracellular traps). The integrin α9 is highly expressed on neutrophils while platelets do not express it. The integrin α9 up-regulated upon neutrophil activation and is implicat

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Hiu, Takeshi, Ayaka Matsuo, Mariko Kamiya, et al. "10065- ET-6 MRNA-ENCAPSULATED LIPID NANOPARTICLES FOR MALIGNANT GLIOMA." Neuro-Oncology Advances 6, Supplement_4 (2024): iv5. http://dx.doi.org/10.1093/noajnl/vdae173.017.

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Abstract Nucleic acid therapeutics hold promise for cancer treatment but have yet to be effectively applied to malignant glioma due to challenges in stability and delivery. We explored the intracerebral delivery of lipid nanoparticles (LNPs) encapsulating siRNA as a drug delivery carrier. Our goal was to develop an siRNA therapy selectively targeting malignant glioma cells by combining LNPs with Fc-domain-binding peptide lipids (FcBPs), a modification system that allows antibody orientation control. Intracerebral Delivery of mRNA-Encapsulated Lipid Nanoparticles: We aimed to deliver mRNA-encap

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Song, Eun Kyung, Jimin Jeon, Dong Gil Jang, et al. "ITGBL1 modulates integrin activity to promote cartilage formation and protect against arthritis." Science Translational Medicine 10, no. 462 (2018): eaam7486. http://dx.doi.org/10.1126/scitranslmed.aam7486.

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Developing and mature chondrocytes constantly interact with and remodel the surrounding extracellular matrix (ECM). Recent research indicates that integrin-ECM interaction is differentially regulated during cartilage formation (chondrogenesis). Integrin signaling is also a key source of the catabolic reactions responsible for joint destruction in both rheumatoid arthritis and osteoarthritis. However, we do not understand how chondrocytes dynamically regulate integrin signaling in such an ECM-rich environment. Here, we found that developing chondrocytes express integrin-β–like 1 (Itgbl1) at spe

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Zhou, Jian, Rui Li, Jinhang Zhang та ін. "Targeting Interstitial Myofibroblast-Expressed Integrin αvβ3 Alleviates Renal Fibrosis". Molecular Pharmaceutics 18, № 3 (2021): 1373–85. http://dx.doi.org/10.1021/acs.molpharmaceut.0c01182.

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Chen, Yan-Jun, Hsu-Yuan Wang, Feng-Ting Huang, and Chiun-Wei Huang. "Integrin‐targeting ferritin for drug delivery and tumor imaging." FASEB Journal 34, S1 (2020): 1. http://dx.doi.org/10.1096/fasebj.2020.34.s1.02827.

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Weigel-Kelley, Kirsten A., Mervin C. Yoder, Linyuan Chen, and Arun Srivastava. "Role of Integrin Cross-Regulation in Parvovirus B19 Targeting." Human Gene Therapy 17, no. 9 (2006): 909–20. http://dx.doi.org/10.1089/hum.2006.17.909.

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Giancotti, Filippo G. "Targeting integrin β4 for cancer and anti-angiogenic therapy". Trends in Pharmacological Sciences 28, № 10 (2007): 506–11. http://dx.doi.org/10.1016/j.tips.2007.08.004.

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Sadeghi, Mehran M., та Jeffrey R. Bender. "Activated αvβ3 Integrin Targeting in Injury-Induced Vascular Remodeling". Trends in Cardiovascular Medicine 17, № 1 (2007): 5–10. http://dx.doi.org/10.1016/j.tcm.2006.07.003.

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Leonhardt, F., M. Behe, R. Dumont та ін. "Integrin αV Inhibition Reduces GvHD by Targeting inflammatory Neovascularization". Biology of Blood and Marrow Transplantation 17, № 2 (2011): S336. http://dx.doi.org/10.1016/j.bbmt.2010.12.548.

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