Relevant bibliographies by topics / Integrins

Academic literature on the topic 'Integrins'

Author: Grafiati
Published: 4 June 2021
Last updated: 6 July 2024

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Journal articles on the topic "Integrins"

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Díaz-González, F., J. Forsyth, B. Steiner, and M. H. Ginsberg. "Trans-dominant inhibition of integrin function." Molecular Biology of the Cell 7, no. 12 (December 1996): 1939–51. http://dx.doi.org/10.1091/mbc.7.12.1939.

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Occupancy of integrin adhesion receptors can alter the functions of other integrins and cause partition of the ligand-occupied integrin into focal adhesions. Ligand binding also changes the conformation of integrin extracellular domains. To explore the relationship between ligand-induced conformational change and integrin signaling, we examined the effect of ligands specific for integrin alpha IIb beta 3 on the functions of target integrins alpha 5 beta 1 and alpha 2 beta 1. We report that binding of integrin-specific ligands to a suppressive integrin can inhibit the function of other target integrins (trans-dominant inhibition). Trans-dominant inhibition is due to a blockade of integrin signaling. Furthermore, this inhibition involves both a conformational change in the extracellular domain and the presence of the beta cytoplasmic tail in the suppressive integrin. Similarly, ligand-induced recruitment of alpha IIb beta 3 to focal adhesions also involves a conformational rearrangement of its extracellular domain. These findings imply that the ligand-induced conformational changes can propagate from an integrin's extracellular to its intracellular face. Trans-dominant inhibition by integrin ligands may coordinate integrin signaling and can lead to unexpected biological effects of integrin-specific inhibitors.
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Wei, Ying, and Harold Chapman. "Protease Crosstalk with Integrins: the Urokinase Receptor Paradigm." Thrombosis and Haemostasis 86, no. 07 (2001): 124–29. http://dx.doi.org/10.1055/s-0037-1616208.

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SummaryMigratory cells use both adhesion receptors and proteolytic enzymes to regulate their interaction with and response to extracellular matrices. Cooperation between integrins and proteases operates at several levels: integrin signaling induces proteases, proteases co-localize with integrins, and proteases regulate the interface between integrins and the intracellular cytoskeleton. One protease system intimately connected to integrins is the urokinase/urokinase receptor(uPAR)/plasmin system. Recent studies indicate urokinase promotes the ligand-like binding of its receptor to a set of β1 and β2 integrins, this binding in turn affecting integrin signaling and cell migration. The glycolipid anchor of uPAR associates with cholesterol-rich membrane rafts. Binding of uPAR to integrins may enrich integrin clusters with signaling molecules such as src-family kinases that localize to rafts and are important to integrin function. Signals derived from integrin/uPAR complexes promote the function of other integrins. Thus the urokinase/plasmin system coordinates with integrins to regulate cell: matrix interactions.
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Triantafilou, Kathy, Martha Triantafilou, Yoshikazu Takada, and Nelson Fernandez. "Human Parechovirus 1 Utilizes Integrins αvβ3 and αvβ1 as Receptors." Journal of Virology 74, no. 13 (July 1, 2000): 5856–62. http://dx.doi.org/10.1128/jvi.74.13.5856-5862.2000.

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ABSTRACT Human parechovirus 1 (HPEV1) displays an arginine-glycine-aspartic acid (RGD) motif in the VP1 capsid protein, suggesting integrins as candidate receptors for HPEV1. A panel of monoclonal antibodies (MAbs) specific for integrins αvβ3, αvβ1, and αvβ5, which have the ability to recognize the RGD motif, and also a MAb specific for integrin α2β1, an integrin that does not recognize the RGD motif, were tested on A549 cells. Our results showed that integrin αv-specific MAb reduced infectivity by 85%. To specify which αv integrins the virus utilizes, we tested MAbs specific to integrins αvβ3 and αvβ1 which reduced infectivity significantly, while a MAb specific for integrin αvβ5, as well as the MAb specific for α2β1, showed no reduction. When a combination of MAbs specific for integrins αvβ3 and αvβ1 were used, virus infectivity was almost completely inhibited; this shows that integrins αvβ3 and αvβ1 are utilized by the virus. We therefore proceeded to test whether αv integrins' natural ligands fibronectin and vitronectin had an effect on HPEV1 infectivity. We found that vitronectin reduced significantly HPEV1 infectivity, whereas a combination of vitronectin and fibronectin abolished infection. To verify the use of integrins αvβ3 and αvβ1 as HPEV1 receptors, CHO cells transfected and expressing either integrin αvβ3 or integrin αvβ1 were used. It was shown that the virus could successfully infect these cells. However, in immunoprecipitation experiments using HPEV1 virions and allowing the virus to bind to solubilized A549 cell extract, we isolated and confirmed by Western blotting the αvβ3 heterodimer. In conclusion, we found that HPEV1 utilises both integrin αvβ3 and αvβ1 as receptors; however, in cells that express both integrins, HPEV1 may preferentially bind integrin αvβ3.
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Spiess, Matthias, Pablo Hernandez-Varas, Anna Oddone, Helene Olofsson, Hans Blom, Dominic Waithe, John G. Lock, Melike Lakadamyali, and Staffan Strömblad. "Active and inactive β1 integrins segregate into distinct nanoclusters in focal adhesions." Journal of Cell Biology 217, no. 6 (April 9, 2018): 1929–40. http://dx.doi.org/10.1083/jcb.201707075.

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Integrins are the core constituents of cell–matrix adhesion complexes such as focal adhesions (FAs) and play key roles in physiology and disease. Integrins fluctuate between active and inactive conformations, yet whether the activity state influences the spatial organization of integrins within FAs has remained unclear. In this study, we address this question and also ask whether integrin activity may be regulated either independently for each integrin molecule or through locally coordinated mechanisms. We used two distinct superresolution microscopy techniques, stochastic optical reconstruction microscopy (STORM) and stimulated emission depletion microscopy (STED), to visualize active versus inactive β1 integrins. We first reveal a spatial hierarchy of integrin organization with integrin molecules arranged in nanoclusters, which align to form linear substructures that in turn build FAs. Remarkably, within FAs, active and inactive β1 integrins segregate into distinct nanoclusters, with active integrin nanoclusters being more organized. This unexpected segregation indicates synchronization of integrin activities within nanoclusters, implying the existence of a coordinate mechanism of integrin activity regulation.
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Kawakami, Keisuke, Hitoshi Tatsumi, and Masahiro Sokabe. "Dynamics of integrin clustering at focal contacts of endothelial cells studied by multimode imaging microscopy." Journal of Cell Science 114, no. 17 (September 1, 2001): 3125–35. http://dx.doi.org/10.1242/jcs.114.17.3125.

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Human umbilical vein endothelial cells were stained with FITC-labeled anti-β1 integrin antibody and plated on a glass cover slip to elucidate the mechanism of integrin clustering during focal contact formation. The process of integrin clustering was observed by time-lapse total-internal-reflection fluorescence microscopy, which can selectively visualize the labeled integrins at the basal surface of living cells. The clustering of integrins at focal contacts started at 1 hour after plating and individual clusters kept growing for ∼6 hours. Most integrin clusters (∼80%) elongated towards the cell center or along the cell margin at a rate of 0.29±0.24 μm minute−1. Photobleaching and recovery experiments with evanescent illumination revealed that the integrins at the extending tip of the clusters were supplied from the intracellular space. Simultaneous time-lapse imaging of exocytosis of integrin-containing vesicles and elongating focal contacts showed that most exocytosis occurred at or near the focal contacts followed by their elongation. Double staining of F-actins and integrins demonstrated that stress fibers were located near the integrin clusters and that intracellular punctate integrins were associated with these stress fibers. These results suggest that the clustering of integrins is mediated by actin-fiber-dependent translocation of integrins to the extending tip of focal contacts.
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Fasoulakis, Zacharias, Michaela-Zoi Psarommati, Angeliki Papapanagiotou, Vasilios Pergialiotis, Antonios Koutras, Athanasios Douligeris, Anastasia Mortaki, et al. "MicroRNAs Can Influence Ovarian Cancer Progression by Dysregulating Integrin Activity." Cancers 15, no. 18 (September 8, 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 current understanding of integrin-mediated cellular processes in ovarian cancer and the roles of miRNAs in regulating integrins. We also discuss the therapeutic potential of targeting miRNAs that regulate integrins for the treatment of ovarian cancer. Targeting miRNAs that regulate integrins or downstream signaling pathways of integrins may provide novel therapeutic strategies for inhibiting integrin-mediated ovarian cancer progression.
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Shimoda, Michiko, Yoko Takada, Emanual Maverakis, Brunhilde Felding, and Yoshikazu Takada. "CD40L acts as an allosteric activator of integrins for signal transduction independent of inside-out signaling." Journal of Immunology 206, no. 1_Supplement (May 1, 2021): 24.04. http://dx.doi.org/10.4049/jimmunol.206.supp.24.04.

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Abstract CD40L plays a major role in immune response and is a target for inflammatory disease therapy. Besides CD40, CD40L binds to several integrins but their role in signaling is unclear. We showed that integrins αvβ3 and α5β1 bind to the CD40L trimeric interface through classical ligand binding site of integrins (site 1). Several CD40L mutants from HIGM1 (hyper-IgM syndrome type 1) patients were clustered in trimeric interface and defective in integrin binding, and in NF-κB and B cell activation, but still bound CD40 and acted as antagonists of CD40L signaling. Thus, integrins play a critical role in CD40L signaling. Previous studies showed that CX3CL1 and sPLA2-IIA can activate integrins by binding to a recently identified allosteric site (site 2) of integrins. Using cell-free assays, we found that soluble (s)-CD40L activated soluble integrins, α4β1, αvβ3 and α5β1, and induced their binding to known specific ligands independent of inside-out signaling. Also, sCD40L activated cell-surface integrins in CHO cells lacking CD40. Finally, sCD40L bound to a cyclic peptide derived from site 2. These findings indicate that CD40L acts as an allosteric activator of integrins by binding to site 2. Docking simulation predicted that the integrin site 2-binding site of CD40L is located outside of CD40L trimer. Importantly, four HIGM1 mutations are clustered in the predicted site 2-binding site of CD40L. The K143T and G144E mutants were the most defective in integrin activation, indicating that integrin binding occurs around these residues of the predicted site 2-binding site. We propose that allosteric integrin activation by CD40L plays a role in CD40L signaling and that defective integrin site 2-binding may be causal for defective CD40L signaling in HIGM1.
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Takada, Yoko K., Scott I. Simon, and Yoshikazu Takada. "The C-type lectin domain of CD62P (P-selectin) functions as an integrin ligand." Life Science Alliance 6, no. 7 (April 25, 2023): e202201747. http://dx.doi.org/10.26508/lsa.202201747.

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Recognition of integrins by CD62P has not been reported and this motivated a docking simulation using integrin αvβ3 as a target. We predicted that the C-type lectin domain of CD62P functions as a potential integrin ligand and observed that it specifically bound to soluble β3 and β1 integrins. Known inhibitors of the interaction between CD62P–PSGL-1 did not suppress the binding, whereas the disintegrin domain of ADAM-15, a known integrin ligand, suppressed recognition by the lectin domain. Furthermore, an R16E/K17E mutation in the predicted integrin-binding interface located outside of the glycan-binding site within the lectin domain, strongly inhibited CD62P binding to integrins. In contrast, the E88D mutation that strongly disrupts glycan binding only slightly affected CD62P-integrin recognition, indicating that the glycan and integrin-binding sites are distinct. Notably, the lectin domain allosterically activated integrins by binding to the allosteric site 2. We conclude that CD62P-integrin binding may function to promote a diverse set of cell–cell adhesive interactions given that β3 and β1 integrins are more widely expressed than PSGL-1 that is limited to leukocytes.
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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 (August 1, 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 effectors. Integrins increase membrane affinity for Rac, leading to RhoGDI dissociation and effector coupling locally, in the vicinity of activated/bound integrins. Integrin-regulated Rac binding sites are within CEMMs (cholesterol-enriched membrane microdomains). Integrins control Rac signalling by preventing the internalization of its binding sites in CEMMs. Integrin regulation of signalling pathways initiated in CEMMs may be important for the spatial control of cell migration and anchorage dependence of cell growth.
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Miyamoto, S., H. Teramoto, J. S. Gutkind, and K. M. Yamada. "Integrins can collaborate with growth factors for phosphorylation of receptor tyrosine kinases and MAP kinase activation: roles of integrin aggregation and occupancy of receptors." Journal of Cell Biology 135, no. 6 (December 15, 1996): 1633–42. http://dx.doi.org/10.1083/jcb.135.6.1633.

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Integrins mediate cell adhesion, migration, and a variety of signal transduction events. These integrin actions can overlap or even synergize with those of growth factors. We examined for mechanisms of collaboration or synergy between integrins and growth factors involving MAP kinases, which regulate many cellular functions. In cooperation with integrins, the growth factors EGF, PDGF-BB, and basic FGF each produced a marked, transient activation of the ERK (extracellular signal-regulated kinase) class of MAP kinase, but only if the integrins were both aggregated and occupied by ligand. Transmembrane accumulation of total tyrosine-phosphorylated proteins, as well as nonsynergistic MAP kinase activation, could be induced by simple integrin aggregation, whereas enhanced transient accumulation of the EGF-receptor substrate eps8 required integrin aggregation and occupancy, as well as EGF treatment. Each type of growth factor receptor was itself induced to aggregate transiently by integrin ligand-coated beads in a process requiring both aggregation and occupancy of integrin receptors, but not the presence of growth factor ligand. Synergism was also observed between integrins and growth factors for triggering tyrosine phosphorylation of EGF, PDGF, and FGF receptors. This collaborative response also required both integrin aggregation and occupancy. These studies identify mechanisms in the signal transduction response to integrins and growth factors that require various combinations of integrin aggregation and ligands for integrin or growth factor receptors, providing opportunities for collaboration between these major regulatory systems.
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Dissertations / Theses on the topic "Integrins"

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Câmara, Joana. "Integrins and myelination." Thesis, University of Cambridge, 2007. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.613217.

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Mutz, Diana. "Identifizierung von Bindungspartnern des cytosolischen Teils der [alpha]3-Integrin-Untereinheit [Alpha3-Integrin-Untereinheit] und die Aufklärung ihrer Rolle bei der Funktion des [alpha]3[beta]1-Integrins [Alpha3beta1-Integrins]." [S.l. : s.n.], 2004. http://www.diss.fu-berlin.de/2004/214/index.html.

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Bao, Wenjie. "Role of integrin signaling in cell proliferation and survival /." Stockholm, 2005. http://diss.kib.ki.se/2005/91-7140-394-9/.

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Hall, P. E. "Integrins and neural stem cells." Thesis, University of Cambridge, 2007. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.599860.

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Extracellular matrix (ECM)-rich basal laminae are an important component of other stem cell niches and thus are likely to form part of the NSC niche. Interactions with the ECM are mediated manly by cell surface heterodimers called integrins. β1 integrins have been implicated in maintaining human epidermal stem cells, and their elevated expression has allowed the enrichment of human prostate epithelial stem cells from transit amplifying populations. My work has focused on the role of the ECM and its receptors in the mammalian CNS stem cell niche. Initial experiments examined the conditions necessary to grow human NSCs under clonal conditions, before using these findings to demonstrate that these cells express higher levels of integrin α6β1 then progenitor or differential cell types. This led to the question of the role of integrins in NSC behaviour, which was investigated in vitro with human and murine tissue using integrin activating/blocking antibodies together with ECM molecules. Laminin-211, an α6β1 ligand, was found to increase NSC survival in an integrin-dependent manner. However, activation of integrin β1 did not recapitulate these results, indicating that integrin β1 is necessary, but not sufficient, for laminin to increase survival. Finally, in utero injections of the integrin activating/block antibodies into the lateral ventricle of embryonic day 15 (E15) embryos were conducted in order to examine the role of integrins in the in vivo stem cell niche. In conclusion, the findings indicate that integrins are highly expressed by neural stem cells and that integrins function in vitro and in vivo to influence stem cell behaviour.
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Petrie, Timothy Andrew. "Biomimetic integrin-specific surface to direct osteoblastic function and tissue healing." Diss., Atlanta, Ga. : Georgia Institute of Technology, 2009. http://hdl.handle.net/1853/29628.

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Thesis (Ph.D)--Biomedical Engineering, Georgia Institute of Technology, 2010.
Committee Chair: Andres Garcia; Committee Member: Andrew Lyon; Committee Member: Barbara Boyan; Committee Member: Johnna Temenoff; Committee Member: Todd McDevitt. Part of the SMARTech Electronic Thesis and Dissertation Collection.
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Shekaran, Asha. "Beta 1 integrins in bone formation during development and engineering integrin-specific hydrogels for enhanced bone healing." Diss., Georgia Institute of Technology, 2013. http://hdl.handle.net/1853/51720.

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Healing large bone defects remains a clinical challenge. While autografts are the gold standard treatment for large bone defects, they are limited by availability and donor site pain. Growth factor treatments such as BMP therapy provide a promising alternative but are expensive and present clinical safety concerns, primarily due to delivery of BMPs at supraphysiological doses. Integrins are ECM receptors which mediate crucial cell functions such as adhesion and differentiation. Therefore, understanding the role of integrins in bone formation and directing desired interactions may enable modulation of host cell functions for therapeutic applications. In this work, beta 1 integrins were deleted in osteolineage cells of transgenic mice at three different stages of differentiation to elucidate their role in bone development. We also engineered bioartificial PEG-based matrices which target the pro-osteogenic alpha 2 beta 1 integrin to promote bone healing. Conditional deletion of beta 1 integrins in osteochondroprogenitor cells under the Twist 2 promoter resulted in severe pre-natal skeletal mineralization defects and embryonic lethality. Targeted deletion of beta 1 integrins in osterix-expressing osteoprogenitors resulted in growth abnormalities, reduced calvarial mineralization, impaired femur development, and tooth defects. However, mice lacking beta 1 integrins in osteocalcin-expressing osteoblasts and osteocytes displayed only a mild skeletal phenotype, indicating that beta 1 integrins play an important role in early skeletal development, but are not required for mature osteoblast function. PEG hydrogels functionalized with the integrin-specific GFOGER ligand enhanced bone regeneration, induced defect bridging in combination with low doses of rhBMP-2 and stimulated improved bone healing compared collagen sponges, which are the clinical standard delivery vector for BMP-2 therapy. These results suggest that treatment with bioartificial integrin-specific PEG hydrogels may be a promising clinical strategy for bone regeneration in large bone defects.
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Savaris, Ricardo Francalacci. "Níveis de integrina avb3 no endométrio de mulheres usuárias do DIU T200." reponame:Biblioteca Digital de Teses e Dissertações da UFRGS, 1999. http://hdl.handle.net/10183/184861.

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Objetivo: Medir a expressão da integrina av~3 no endométrio de mulheres usuárias do DIUT200. Desenho: Estudo observacional controlado. Local realizado: Centro de saúde secundário e laboratório universitário. Pacientes: Treze mulheres sadias e férteis (controles) e treze usuárias do DIUT200 (casos). lntervençao: Biópsia endometrial realizada entre o 6°-1 0° dia pós-ovulatório do ciclo menstrual. Principal Desfecho Avaliado: A expressão da integrina av~3 através do HSCORE em amostras endometriais criopreservadas. Resultados: O HSCORE das usuárias do DIUT200 foi 0,9 ± 0,7 (média± DP), enquanto que o dos controles foi 2,13 ± 0,7 (média ± DP) (p = 0.001 Teste-t de Student). Todos os controles foram positivos para a expressão da integrina av~3. mas as usuárias do DIUT200 não apresentou positivdade para a integrina av~3 em 38,5% dos casos (p = 0,03 Teste Exato de Fisher). Conclusao: Os resultados apoiam a teoria que o DIUT200 de cobre também tem um mecanismo de ação que interfere diretamente com a receptividade uterina e a implantação.
Objective: To measure the expression of avf33 integrin in the endometrium of IUDT200 users. Design: Observational controlled study Setting: Secondary health care center and University laboratory Patients: Thirteen healthy fertile women (contrais) and thirteen IUDT200 users (cases). lntervention: Endometrial biopsy on postovulatory day 6-1 O of the menstrual cycle. Main Outcome Measure: The expression of avJ33 by HSCORE on cryopreserved endometrial sections. Results: The HSCORE for IUD users was 0.9 ± 0.7 (mean ± SEM), while for contrais was 2.13 ± 0.7 (mean ±SEM) (p < 0.001 Teste-t de Student). Ali contrais were positiva for avJ33, but women with IUD did not express avl33 integrin in 38.5% of the cases (p < 0.03 Fisher's exact test). Conclusion: These results support the theory that copper IUD T200 also has a mechanism of action that is directed at interference with uterine receptivity and implantation.
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Eshghi, Shawdee. "The roll of integrins in hematopoiesis." Thesis, Massachusetts Institute of Technology, 2007. http://hdl.handle.net/1721.1/39905.

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Thesis (Ph. D.)--Massachusetts Institute of Technology, Biological Engineering Division, 2007.
Includes bibliographical references (p. 113-123).
Hematopoietic stem cells (HSCs) hold great promise for the treatment of disease. The rare frequency at which HSCs occur in the bone marrow under homeostatic conditions is a limiting factor in both their study and clinical use. ex vivo expansion of these cells is therefore a necessary step to maximizing their potential. In this thesis I explore the concept that signals from the extracellular matrix can direct differentiation, survival and self-renewal decisions in hematopoietic cells, and thus can provide a foundation for the design of ex vivo expansion strategies. This work is focused on the role integrins, the major class of cell-extracellular matrix adhesion molecules, play in mediating these signals to hematopoietic cells at two developmental stages. In the erythroid lineage, I show that expansion of committed erythroid progenitors is regulated by growth factor and integrin-mediated signals in temporally distinct regimes. I establish a biologically relevant role for [alpha]401 but not [alpha]501 integrins in erythropoiesis and provide evidence that erythroid differentiation and expansion are regulated by separate processes.
(cont.) In the study of uncommitted HSCs, I identify several integrin subunits that are differentially expressed on highly purified HSC populations that correlate with long term repopulating ability. One of these subunits, [alpha]2 integrin, specifically mediates adhesion of HSCs to bone marrow extracellular matrix proteins, thereby providing a potential mechanism for stem cell self-renewal. This work establishes that integrin-mediated interactions between hematopoietic cells and the extracellular matrix are dynamic and provide important developmental cues.
by Shawdee Eshghi.
Ph.D.
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Douglass, Wendy A. "The structure and function of integrins." Thesis, University of Oxford, 1997. http://ora.ox.ac.uk/objects/uuid:cfdfd40c-b350-4500-83e4-2650f9fe455d.

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Integrins are a family of αβ heterodimeric cell surface glycoproteins formed by the noncovalent association of a specific integrin α and β subunit. At present 16 different integrin α subunits and 8 different integrin β subunits have been identified, which can associate in various combinations to produce over 20 different integrin αβ heterodimeric receptors. The leukocyte integrins LFA-1 (αLβ2, CD11a/CD18), Mac-1 (αMβ2, CD11b/CD18) and p150,95 (αXβ2, CD11c/CD18) are formed by the non-covalent association of the αL, αM or αX subunits with the β2 subunit. In order to determine the regions of the β2 subunit which are involved in its heterodimeric interaction with the αL, αM and αX subunits, eight variant β2 subunits were analysed for their ability to form LFA-1, Mac-1 and p150,95 heterodimeric complexes. Three chimeric β2/β1 subunits: β2V1, β2V12 and β2NS1, and three analogous chimeric β2/β7 subunits: β2V7, β2V72 and β2NS7, as well as a soluble and a truncated β2 subunit: β2sol and β2tr, were studied. All of the variant β2 subunits retained the ability to associate with the αL subunit, suggesting that the N-terminal 436 amino acids of the β2 subunit are sufficient to provide the specificity for LFA-1 heterodimer formation. In contrast, all the β2 variants associated inefficiently with the αM and αX subunits, suggesting that the heterodimeric interactions between the α and β subunits in Mac-1 and p150,95 are more extensive, and perhaps more complicated than those in LFA-1. The ability of the modified LFA-1 heterodimers formed with the variant β2 subunits to bind to the LFA-1 ligand ICAM-1 was also studied. All of the modified LFA-1 receptors retained the ability to bind to ICAM-1, suggesting that in LFA-1, the ICAM-1 binding site in the β2 subunit must be located within its N-terminal 436 amino acids. In addition, unlike the wildtype LFA-1 receptor, all of the modified LFA-1 receptors were constitutively active with respect to ICAM-1 binding. It therefore appears that specific interactions between different regions of the β2 subunit are required to constrain the LFA-1 receptor in its inactive, resting state, and that disruption of any one of these intramolecular interactions results in release of the receptor into its high affinity ligand binding conformation. This "constraint model" for the regulation of LFA-1 activity may also be applicable to other integrins. Analysis of a number of mutant β2 subunits carrying leukocyte adhesion deficiency (LAD) mutations, and their ability to form LFA-1, Mac-1 and p150,95 heterodimers, provided results consistent with those obtained with the variant β2 subunits.
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Divekar, Devina. "Integrins in muscle disease and repair." Thesis, University of East Anglia, 2014. https://ueaeprints.uea.ac.uk/54271/.

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Integrin α7β1 plays an important role in maintaining adult skeletal muscle integrity and like dystrophin, provides anchorage and bidirectional signaling as a laminin receptor. The expression of α7β1 integrin was upregulated upon dystrophin deficiency arguing for the molecular compensation and thus considered as potential candidate for treatment of Duchenne Muscular Dystrophy (DMD). The existence of developmentally regulated alternative splice variants makes the α7β1 integrin a complex integrin to study its function in skeletal muscle. In this study we show that increased levels of the adult extracellular variant X2 interfere with muscle integrity, while the presence of embryonic integrin α7 extracellular variant X1 results in normal skeletal muscle architecture. Furthermore, detailed analysis of mdxα7tg mice suggests that overexpression of integrin α7 made no difference on the dystrophic phenotype, in fact mdx α7X2 mice show a more severe phenotype compared to mdx mice. Our study also shed light on the importance of integrin α5 during the development of the skeletal muscle by means of generating conditional knockout (cKO) mice using HSA-Cre and Pax3-Cre promoter systems. Our findings show no obvious difference in the Itga5 cKO when the HSA promoter drives Cre recombinase, however conditional loss under the control of the Pax3 promoter leads perinatal lethality. In addition we investigate the dosage effect of integrin α5 in integrin α7 knockout (KO) mice to understand the cross talk between these two integrins and to correlate with previous data suggesting a gain of function phenotype by that existence of integrin α5 at the myotendinious junction (MTJ) in α7KO muscle (Nawrotzki et al.,2003) From our data we know that gene therapy with integrin α7 is a challenge and is not a suitable alternative to cure dystrophy, at least not in mdx mice, we therefore switch our focus on looking into cell based therapies for DMD by investigating the potential role of perivascular cells (PVCs) using transplantation experiments in mice by artificially inducing muscle damage.
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Books on the topic "Integrins"

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A, Cheresh David, ed. Integrins. Amsterdam: Elsevier, 2007.

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A, Cheresh David, and Mecham Robert P, eds. Integrins: Molecular and biological responses to the extracellular matrix. San Diego: Academic Press, 1994.

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Gullberg, Donald, ed. I Domain Integrins. Dordrecht: Springer Netherlands, 2014. http://dx.doi.org/10.1007/978-94-017-9153-3.

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Becchetti, Andrea, and Annarosa Arcangeli, eds. Integrins and Ion Channels. New York, NY: Springer New York, 2010. http://dx.doi.org/10.1007/978-1-4419-6066-5.

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5

E, Gullberg Donald, ed. I domains in integrins. Georgetown, Tex: Landes Bioscience/Eurekah.com, 2003.

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Gullberg, Donald, and Johannes A. Eble, eds. Integrins in Health and Disease. Cham: Springer International Publishing, 2023. http://dx.doi.org/10.1007/978-3-031-23781-2.

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Yoshikazu, Takada, ed. Integrin: The biological problem. Boca Raton: CRC Press, 1994.

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Leukocyte integrins: Structure, expression, and function. Austin, Tex: R. G. Landes Company, 1996.

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Jewell, Kevin Jeffery. Integrins as transducers of extracellular stimuli. Ottawa: National Library of Canada, 1994.

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Corbí, Angel L. Leukocyte integrins: Structure, expression and function. New York: Springer, 1996.

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Book chapters on the topic "Integrins"

1

Robert, Jacques. "Integrins." In Textbook of Cell Signalling in Cancer, 117–26. Cham: Springer International Publishing, 2014. http://dx.doi.org/10.1007/978-3-319-14340-8_10.

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Miller, David D. "Integrins." In Gene Family Targeted Molecular Design, 85–118. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2008. http://dx.doi.org/10.1002/9780470423936.ch4.

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Salajegheh, Ali. "Integrins." In Angiogenesis in Health, Disease and Malignancy, 169–80. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-28140-7_26.

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Parry, Graham C., Fernando Doñate, Marian L. Plunkett, David E. Shaw, Steven Pirie-Shepherd, and Andrew P. Mazar. "Integrins." In Bone Metastasis, 201–27. Totowa, NJ: Humana Press, 2005. http://dx.doi.org/10.1385/1-59259-892-7:201.

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de Moll, Ellen H., Joanna Dong, Margeaux Oliva, and Yvonne Saenger. "Integrins, Immunology." In Cancer Therapeutic Targets, 285–94. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4419-0717-2_131.

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Dransfield, Ian. "Leukocyte Integrins." In Blood Cell Biochemistry, 307–33. Boston, MA: Springer US, 1993. http://dx.doi.org/10.1007/978-1-4757-9534-9_12.

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de Moll, Ellen H., Joanna Dong, Margeaux Oliva, and Yvonne Saenger. "Integrins, Immunology." In Cancer Therapeutic Targets, 1–9. New York, NY: Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4614-6613-0_131-1.

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de Moll, Ellen H., Joanna Dong, Margeaux Oliva, and Yvonne Saenger. "Integrins, Immunology." In Cancer Therapeutic Targets, 1–10. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4614-6613-0_131-2.

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Kishimoto, Takashi K., Richard S. Larson, Angel L. Corbi, Michael L. Dustin, Donald E. Staunton, and Timothy A. Springer. "Leukocyte Integrins." In Leukocyte Adhesion Molecules, 7–43. New York, NY: Springer New York, 1990. http://dx.doi.org/10.1007/978-1-4612-3234-6_2.

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Mousa, Shaker A., and Paul J. Davis. "Anti-integrins." In Encyclopedia of Molecular Pharmacology, 1–8. Cham: Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-21573-6_81-1.

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Conference papers on the topic "Integrins"

1

Calver, J., C. Joseph, AE John, L. Organ, H. Fainberg, J. Porte, S. Mukhopadhyay, et al. "S31 The novel coronavirus SARS-CoV-2 binds RGD integrins and upregulates avb3 integrins in Covid-19 infected lungs." In British Thoracic Society Winter Meeting, Wednesday 17 to Friday 19 February 2021, Programme and Abstracts. BMJ Publishing Group Ltd and British Thoracic Society, 2021. http://dx.doi.org/10.1136/thorax-2020-btsabstracts.37.

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Gant, V. Alexander, Mustafa H. Chowdury, Gerald A. Meininger, and Gerard L. Cote. "Detection of integrins using surface-enhanced Raman spectroscopy." In Biomedical Optics 2004, edited by Gerard L. Cote and Alexander V. Priezzhev. SPIE, 2004. http://dx.doi.org/10.1117/12.535344.

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Li, Chun. "NIR optical imaging of integrins and matrix metalloproteinases." In Biomedical Topical Meeting. Washington, D.C.: OSA, 2004. http://dx.doi.org/10.1364/bio.2004.tha4.

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Haugh, Matthew G., and Laoise M. McNamara. "The Role of Integrins in Osteocyte Response to Mechanical Stimulus." In ASME 2012 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2012. http://dx.doi.org/10.1115/sbc2012-80126.

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Bone is an exceptional material that is efficiently lightweight, possesses excellent mechanical strength and can also adapt itself in response to changes in physical activity by means of coordinated physiological processes known as modelling and remodelling. The response of bone to mechanical loading is thought to be regulated by mechanosensitive osteocyte cells that can direct the alteration of bone mass, by osteoblasts and osteoclasts, and thereby play an important role in optimizing bone strength. The mechanisms by which osteocytes sense their mechanical environment are not well understood. It has been proposed that integrin-based (αVβ3) attachments to ECM on osteocyte cell processes may facilitate mechanosensation in osteocytes [1,2]. While previous studies have shown that integrin beta;1 plays an important role in response to mechanical stimulus, the role of integrin αVβ3 in osteocyte mechanotransduction has yet to be investigated [3,4].
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Adorno-Cruz, Valery, Xia Liu, and Huiping Liu. "Abstract 5168: Understanding the role of integrins in breast cancer." In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-5168.

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Lian, Eric, Mathieu J. F. Crupi, Jessica G. Cockburn, Simona M. Wagner, Anirudh Goel, and Lois M. Mulligan. "Abstract 4991: RET and integrins cooperate in cell-microenvironment response." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-4991.

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Joshi, Raghav, Wenying Ren, and Paul Mathew. "Abstract 1902: The comparative superiority of a bispecific antibody targeting alpha v and alpha 5 integrins is uniquely characterized by induced degradation of integrins." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.sabcs18-1902.

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Joshi, Raghav, Wenying Ren, and Paul Mathew. "Abstract 1902: The comparative superiority of a bispecific antibody targeting alpha v and alpha 5 integrins is uniquely characterized by induced degradation of integrins." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.am2019-1902.

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Cho, Hongkwan, Abdul Sheikh, and Daria A. Narmoneva. "Non-Specific Endothelial Cell Interactions With the Substrate Result in Cell Activation and Angiogenesis In Vitro." In ASME 2010 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2010. http://dx.doi.org/10.1115/sbc2010-19094.

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Vascularization is critical for success of tissue engineering applications. Previous studies by us and others have shown that self-assembling peptide nanoscaffold RAD16-II promotes de novo capillary formation (angiogenesis) in vitro and neovascularization in vivo, and is a promising material for tissue engineering applications [1, 2]. However, the molecular mechanisms for cell interactions with this material are not known. Angiogenesis is mediated via interactions between integrins, which are expressed on the surface of activated endothelial cells (ECs), and extracellular matrix proteins. Among several integrins, αvβ3 is the most abundant and influential receptor regulating angiogenesis [3]. The αvβ3 integrin binds to its ligands via Arg-Gly-Asp (RGD) biding motif. However, there are no RGD motifs on RAD 16-II peptide. Instead, it contains three RAD motifs. Studies have shown that non-specific binding of αvβ3 with RAD can be retained through R and D sides [4]. The objective of this study, therefore, is to elucidate the underlying molecular mechanisms of RAD16-II nanoscaffold interactions with microvascular endothelial cells. We hypothesize that non-specific interactions between RAD16-II peptide nanoscaffold and αvβ3 integrin result in phosphorylations of β3 cytoplasmic domain, which then activate downstream angiogenic signaling pathways and promote angiogenesis.
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Bayless, Kayla J., and George E. Davis. "AFFINITY OF OSTEOPONTIN FOR LEUKOCYTE INTEGRINS, EXTRACELLULAR MATRICES AND APOPTOTIC CELLS." In 3rd International Conference on Osteopontin and SIBLING (Small Integrin-Binding Ligand, N-linked Glycoprotein) Proteins, 2002. TheScientificWorld Ltd, 2002. http://dx.doi.org/10.1100/tsw.2002.235.

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Reports on the topic "Integrins"

1

Languino, Lucia R. Beta1 and Beta3 Integrins in Prostate Cancer. Fort Belvoir, VA: Defense Technical Information Center, January 2003. http://dx.doi.org/10.21236/ada414864.

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Shimizu, Yoji. Growth Receptors and Integrins in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, November 1999. http://dx.doi.org/10.21236/ada383604.

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Price, Janet. The Role of Integrins in Breast Cancer Metastasis. Fort Belvoir, VA: Defense Technical Information Center, October 1999. http://dx.doi.org/10.21236/ada381790.

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Jongewaard, Ian N. Tumor Cell De-Adhesion by Aberrant, Single Subunit Integrins. Fort Belvoir, VA: Defense Technical Information Center, July 1998. http://dx.doi.org/10.21236/ada378864.

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Shaw, Leslie M., and A. Mercurio. Regulation of Breast Carcinoma Progression by the Alpha-6 Integrins. Fort Belvoir, VA: Defense Technical Information Center, September 2000. http://dx.doi.org/10.21236/ada394030.

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Laouar, A., C. B. H. Chubb, F. Collart, and E. Huberman. Human macrophage differentiation involves an interaction between integrins and fibronectin. Office of Scientific and Technical Information (OSTI), November 1996. http://dx.doi.org/10.2172/495739.

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Shaw, Leslie M., and A. Mercurio. Regulation of Breast Carcinoma Progression by the Alpha-6 Integrins. Fort Belvoir, VA: Defense Technical Information Center, October 2001. http://dx.doi.org/10.21236/ada404843.

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Laouar, A., C. B. H. Chubb, F. Collart, and E. Huberman. Human macrophage differentiation involves an interaction between integrins and fibronectin. Office of Scientific and Technical Information (OSTI), March 1997. http://dx.doi.org/10.2172/515532.

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Shaw, Leslie M. Regulation of Breast Carcinoma Progression by the Alpha-6 Integrins. Fort Belvoir, VA: Defense Technical Information Center, September 1999. http://dx.doi.org/10.21236/ada383962.

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Cardo-Vila, Marina. Isolation of Signaling Molecules Involved in Angiogenic Pathways Mediated Alpha v Integrins. Fort Belvoir, VA: Defense Technical Information Center, May 2004. http://dx.doi.org/10.21236/ada435432.

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