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Journal articles on the topic 'Integrin modulation'

Author: Grafiati

Published: 2 November 2024

Last updated: 31 July 2025

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1

Hughes, Paul E., and Martin Pfaff. "Integrin affinity modulation." Trends in Cell Biology 8, no. 9 (1998): 359–64. http://dx.doi.org/10.1016/s0962-8924(98)01339-7.

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2

Martin-Bermudo, Maria D., Olga M. Dunin-Borkowski, and Nicholas H. Brown. "Modulation of Integrin Activity is Vital for Morphogenesis." Journal of Cell Biology 141, no. 4 (1998): 1073–81. http://dx.doi.org/10.1083/jcb.141.4.1073.

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Cells can vary their adhesive properties by modulating the affinity of integrin receptors. The activation and inactivation of integrins by inside-out mechanisms acting on the cytoplasmic domains of the integrin subunits has been demonstrated in platelets, lymphocytes, and keratinocytes. We show that in the embryo, normal morphogenesis requires the α subunit cytoplasmic domain to control integrin adhesion at the right times and places. PS2 integrin (αPS2βPS) adhesion is normally restricted to the muscle termini, where it is required for attaching the muscles to the ends of other muscles and to

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3

Tozer, Eileen Collins, Paul E. Hughes, and Joseph C. Loftus. "Ligand binding and affinity modulation of integrins." Biochemistry and Cell Biology 74, no. 6 (1996): 785–98. http://dx.doi.org/10.1139/o96-085.

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Integrins are cell adhesion receptors that mediate cell–cell and cell–extracellular matrix interactions. The extracellular domains of these receptors possess binding sites for a diverse range of protein ligands. Ligand binding is divalent cation dependent and involves well-defined motifs in the ligand. Integrins can dynamically regulate their affinity for ligands (inside-out signaling). This ability to rapidly modulate their affinity state is key to their involvement in such processes as cell migration and platelet aggregation. This review will focus on two aspects of integrin function: first,

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Li, Yifan, Shantong Peng, Jiatong Xu, Wenjie Liu, and Qi Luo. "Integrin signaling in tumor biology: mechanisms of intercellular crosstalk and emerging targeted therapies." PeerJ 13 (May 7, 2025): e19328. https://doi.org/10.7717/peerj.19328.

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Integrins, a family of transmembrane cell adhesion receptors, mediate intercellular and cell–extracellular matrix crosstalk via outside-in and inside-out signaling pathways. Integrins, categorized into 24 distinct combinations of α and β subunits, exhibit tissue-specific expression and perform unique or overlapping roles in physiological and pathophysiological processes. These roles encompass embryonic angiogenesis, tissue repair, and the modulation of tumor cell angiogenesis, progression, invasion, and metastasis. Notably, integrins are significant contributors to tumor development, offering

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Ashe, Hilary L. "Modulation of BMP signalling by integrins." Biochemical Society Transactions 44, no. 5 (2016): 1465–73. http://dx.doi.org/10.1042/bst20160111.

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The bone morphogenetic protein (BMP) pathway is a major conserved signalling pathway with diverse roles in development and homeostasis. Given that cells exist in three-dimensional environments, one important area is to understand how the BMP pathway operates within such complex cellular environments. The extracellular matrix contains information regarding tissue architecture and its mechanical properties that is transmitted to the cell via integrin receptors. In this review, I describe various examples of modulation of the BMP pathway by integrins. In the case of the Drosophila embryo and some

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Huang, Jing, Lance C. Bridges, and Judith M. White. "Selective Modulation of Integrin-mediated Cell Migration by Distinct ADAM Family Members." Molecular Biology of the Cell 16, no. 10 (2005): 4982–91. http://dx.doi.org/10.1091/mbc.e05-03-0258.

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A disintegrin and a metalloprotease (ADAM) family members have been implicated in many biological processes. Although it is recognized that recombinant ADAM disintegrin domains can interact with integrins, little is known about ADAM-integrin interactions in cellular context. Here, we tested whether ADAMs can selectively regulate integrin-mediated cell migration. ADAMs were expressed in Chinese hamster ovary cells that express defined integrins (α4β1, α5β1, or both), and cell migration on full-length fibronectin or on its α4β1 or α5β1 binding fragments was studied. We found that ADAMs inhibit i

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Sethi, Tariq, Mark H. Ginsberg, Julian Downward, and Paul E. Hughes. "The Small GTP-binding Protein R-Ras Can Influence Integrin Activation by Antagonizing a Ras/Raf-initiated Integrin Suppression Pathway." Molecular Biology of the Cell 10, no. 6 (1999): 1799–809. http://dx.doi.org/10.1091/mbc.10.6.1799.

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The rapid modulation of ligand-binding affinity (“activation”) is a central property of the integrin family of cell adhesion receptors. The small GTP-binding protein Ras and its downstream effector kinase Raf-1 suppress integrin activation. In this study we explored the relationship between Ras and the closely related small GTP-binding protein R-Ras in modulating the integrin affinity state. We found that R-Ras does not seem to be a direct activator of integrins in Chinese hamster ovary cells. However, we observed that GTP-bound R-Ras strongly antagonizes the Ras/Raf-initiated integrin suppres

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Mahabeleshwar, Ganapati H., Juhua Chen, Weiyi Feng, Payaningal R. Somanath, Olga V. Razorenova, and Tatiana V. Byzova. "Integrin affinity modulation in angiogenesis." Cell Cycle 7, no. 3 (2008): 335–47. http://dx.doi.org/10.4161/cc.7.3.5234.

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9

Woods, Anne, and John R. Couchman. "Integrin Modulation by Lateral Association." Journal of Biological Chemistry 275, no. 32 (2000): 24233–36. http://dx.doi.org/10.1074/jbc.r000001200.

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10

Yu, Tao, Xing Wu, Kiran B. Gupta та Dennis F. Kucik. "Affinity, lateral mobility, and clustering contribute independently to β2-integrin-mediated adhesion". American Journal of Physiology-Cell Physiology 299, № 2 (2010): C399—C410. http://dx.doi.org/10.1152/ajpcell.00039.2009.

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Affinity changes and avidity modulation both contribute to activation of β2-integrin-mediated adhesion, an essential, early step in inflammation. Avidity modulation, defined as an increase in adhesiveness independent of integrin conformational changes, might be due to integrin clustering, motion, or both. Increased integrin diffusion upon leukocyte activation has been demonstrated, but whether it is proadhesive in itself, or just constitutes a mechanism for integrin clustering, remains unclear. To understand the proadhesive effects of integrin affinity changes, clustering, and motion, an exper

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11

Anderson, M. J., Z. Q. Shi, and S. L. Zackson. "Proteolytic disruption of laminin-integrin complexes on muscle cells during synapse formation." Molecular and Cellular Biology 16, no. 9 (1996): 4972–84. http://dx.doi.org/10.1128/mcb.16.9.4972.

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To explore whether a neural modulation of muscle integrins' extracellular ligand interactions contributes to synapse induction, we compared the distributions of beta1-integrins and basal lamina proteins on Xenopus myotomal myocytes developing in culture. beta1-Integrins formed numerous organized aggregates scattered over the entire muscle surface, with particularly dense accumulations at specialized sites resembling myotendinous and neuromuscular junctions. Integrin aggregates on muscle cells differed from those on surrounding fibroblasts and epithelial cells, both in their lack of response to

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Berditchevski, Fedor. "Complexes of tetraspanins with integrins: more than meets the eye." Journal of Cell Science 114, no. 23 (2001): 4143–51. http://dx.doi.org/10.1242/jcs.114.23.4143.

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The transmembrane proteins of the tetraspanin superfamily are implicated in a diverse range of biological phenomena, including cell motility, metastasis, cell proliferation and differentiation. The tetraspanins are associated with adhesion receptors of the integrin family and regulate integrin-dependent cell migration. In cells attached to the extracellular matrix, the integrin-tetraspanin adhesion complexes are clustered into a distinct type of adhesion structure at the cell periphery. Various tetraspanins are associated with phosphatidylinositol 4-kinase and protein kinase C isoforms, and th

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Leisner, Tina M., June D. Wencel-Drake, Wei Wang та Stephen C. T. Lam. "Bidirectional Transmembrane Modulation of Integrin αIIbβ3Conformations". Journal of Biological Chemistry 274, № 18 (1999): 12945–49. http://dx.doi.org/10.1074/jbc.274.18.12945.

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Kon, Shigeyuki, Hitomi Kouro та Tadashi Matsuda. "A novel murine α4 integrin splicing variant is a specific receptor for VCAM-1 (61.2)". Journal of Immunology 188, № 1_Supplement (2012): 61.2. http://dx.doi.org/10.4049/jimmunol.188.supp.61.2.

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Abstract Integrins affect multiple cell motility in control of cell survival, growth, or differentiation mediated by cell-cell and cell-extracellular matrix interaction. We previously reported that α9 integrin splicing variant, SFα9, promotes wild type α9 integrin-dependent adhesion. In this report, we introduce a new murine α4 integrin splicing variant mSFα4, which have new short cytoplasmic tail. In inflamed tissues including rheumatoid joint, the expression of mSFa4, as well as wild type α4 integrin, is upregulated. Interestingly, cells expressing mSFα4 bind to VCAM-1 but not other α4 integ

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Wu, Xin, Jon E. Mogford, Steven H. Platts, George E. Davis, Gerald A. Meininger та Michael J. Davis. "Modulation of Calcium Current in Arteriolar Smooth Muscle by αvβ3 and α5β1 Integrin Ligands". Journal of Cell Biology 143, № 1 (1998): 241–52. http://dx.doi.org/10.1083/jcb.143.1.241.

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Vasoactive effects of soluble matrix proteins and integrin-binding peptides on arterioles are mediated by αvβ3 and α5β1 integrins. To examine the underlying mechanisms, we measured L-type Ca2+ channel current in arteriolar smooth muscle cells in response to integrin ligands. Whole-cell, inward Ba2+ currents were inhibited after application of soluble cyclic RGD peptide, vitronectin (VN), fibronectin (FN), either of two anti–β3 integrin antibodies, or monovalent β3 antibody. With VN or β3 antibody coated onto microbeads and presented as an insoluble ligand, current was also inhibited. In contra

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Mana, Giulia, Donatella Valdembri, Janet A. Askari та ін. "The βI domain promotes active β1 integrin clustering into mature adhesion sites". Life Science Alliance 6, № 2 (2022): e202201388. http://dx.doi.org/10.26508/lsa.202201388.

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Modulation of integrin function is required in many physiological and pathological settings, such as angiogenesis and cancer. Integrin allosteric changes, clustering, and trafficking cooperate to regulate cell adhesion and motility on extracellular matrix proteins via mechanisms that are partly defined. By exploiting four monoclonal antibodies recognizing distinct conformational epitopes, we show that in endothelial cells (ECs), the extracellular βI domain, but not the hybrid or I-EGF2 domain of active β1 integrins, promotes their FAK-regulated clustering into tensin 1–containing fibrillar adh

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Vehlow, Anne, та Nils Cordes. "Growth factor receptor and β1 integrin signaling differentially regulate basal clonogenicity and radiation survival of fibroblasts via a modulation of cell cycling". In Vitro Cellular & Developmental Biology - Animal 58, № 2 (2022): 169–78. http://dx.doi.org/10.1007/s11626-022-00656-z.

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AbstractCell adhesion to extracellular matrix proteins mediates resistance to radio- and chemotherapy by activating integrin signaling. In addition, mutual and cooperative interactions between integrin and growth factor receptor signaling contribute to the cellular radiation response. Here, we investigate to which extend the crosstalk between β1 integrins and growth factor receptor signaling determines the cellular radiation response of fibroblasts by assessing clonogenic survival and cell cycling. By utilizing growth factor signaling competent and either β1 integrin wildtype GD25β1A fibroblas

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Kinashi, Tatsuo, Tetsuo Asaoka, Ruri Setoguchi, and Kiyoshi Takatsu. "Affinity Modulation of Very Late Antigen-5 Through Phosphatidylinositol 3-Kinase in Mast Cells." Journal of Immunology 162, no. 5 (1999): 2850–57. http://dx.doi.org/10.4049/jimmunol.162.5.2850.

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Abstract Adhesiveness of integrins is up-regulated rapidly by a number of molecules, including growth factors, cytokines, chemokines, and other cell surface receptors, through a mechanism termed inside-out signaling. The inside-out signaling pathways are thought to alter integrin affinity for ligand, or cell surface distribution of integrin by diffusion/clustering. However, it remains to be clarified whether any physiologically relevant agonists induce a rapid change in the affinity of β1 integrins and how ligand-binding affinity is modulated upon stimulation. In this study, we reported that a

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19

Mousa, Shaker, Faith Davis, and Paul Davis. "Hormone-Integrin Cross Talk and Angiogenesis Modulation." Immunology‚ Endocrine & Metabolic Agents in Medicinal Chemistry 9, no. 2 (2009): 75–83. http://dx.doi.org/10.2174/187152209789000704.

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20

Grinnell, F. "Wound repair, keratinocyte activation and integrin modulation." Journal of Cell Science 101, no. 1 (1992): 1–5. http://dx.doi.org/10.1242/jcs.101.1.1.

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21

Rico, Félix, Calvin Chu, Midhat H. Abdulreda, Yujing Qin, and Vincent T. Moy. "Temperature Modulation of Integrin-Mediated Cell Adhesion." Biophysical Journal 99, no. 5 (2010): 1387–96. http://dx.doi.org/10.1016/j.bpj.2010.06.037.

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22

Wei, Xiaofan, Xiang Wang, Jun Zhan, et al. "Smurf1 inhibits integrin activation by controlling Kindlin-2 ubiquitination and degradation." Journal of Cell Biology 216, no. 5 (2017): 1455–71. http://dx.doi.org/10.1083/jcb.201609073.

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Integrin activation is an indispensable step for various integrin-mediated biological functions. Kindlin-2 is known to coactivate integrins with Talin; however, molecules that restrict integrin activation are elusive. Here, we demonstrate that the E3 ubiquitin ligase Smurf1 controls the amount of Kindlin-2 protein in cells and hinders integrin activation. Smurf1 interacts with and promotes Kindlin-2 ubiquitination and degradation. Smurf1 selectively mediates degradation of Kindlin-2 but not Talin, leading to inhibition of αIIbβ3 integrin activation in Chinese hamster ovary cells and β1 integri

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Thibault, Gaétan, Marie-Josée Lacombe, Lynn M. Schnapp, Alexandre Lacasse, Fatiha Bouzeghrane та Geneviève Lapalme. "Upregulation of α8β1-integrin in cardiac fibroblast by angiotensin II and transforming growth factor-β1". American Journal of Physiology-Cell Physiology 281, № 5 (2001): C1457—C1467. http://dx.doi.org/10.1152/ajpcell.2001.281.5.c1457.

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Using a novel pharmacological tool with125I-echistatin to detect integrins on the cell, we have observed that cardiac fibroblasts harbor five different RGD-binding integrins: α8β1, α3β1, α5β1, αvβ1, and αvβ3. Stimulation of cardiac fibroblasts by angiotensin II (ANG II) or transforming growth factor-β1 (TGF-β1) resulted in an increase of protein and heightening by 50% of the receptor density of α8β1-integrin. The effect of ANG II was blocked by an AT1, but not an AT2, receptor antagonist, or by an anti-TGF-β1 antibody. ANG II and TGF-β1 increased fibronectin secretion, smooth muscle α-actin sy

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Medhora, Meetha M. "Retinoic acid upregulates β1-integrin in vascular smooth muscle cells and alters adhesion to fibronectin". American Journal of Physiology-Heart and Circulatory Physiology 279, № 1 (2000): H382—H387. http://dx.doi.org/10.1152/ajpheart.2000.279.1.h382.

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Retinoic acid has an established physiological role in differentiation, development, and cellular growth. This study investigated the action of all- trans retinoic acid (ATRA) on vascular integrins, cell-surface receptors that control growth and remodeling of blood vessels. The β1-integrin subunit mRNA and protein was induced after treatment with ATRA in two different rat vascular smooth muscle cell lines. To relate this result to the in vivo state, the aortas from adult rats fed with therapeutic doses of ATRA were examined for β1-integrin protein. A significant upregulation of the integrin su

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Huttenlocher, A., M. H. Ginsberg, and A. F. Horwitz. "Modulation of cell migration by integrin-mediated cytoskeletal linkages and ligand-binding affinity." Journal of Cell Biology 134, no. 6 (1996): 1551–62. http://dx.doi.org/10.1083/jcb.134.6.1551.

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Integrin cell surface adhesion receptors play a central role in mediating cell migration. We have developed a model system consisting of CHO cells ectopically expressing the alpha IIb beta 3 integrin to study integrin affinity and cytoskeletal interactions during cell migration. The alpha IIb beta 3 integrins are suited for study of integrin receptors during cell migration because they are well characterized with respect to ligand binding, cytoskeletal interactions, and signal transduction, and mutants with altered receptor function are available. The alpha IIb beta 3 receptor specifically med

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Belkin, Alexey M., S. Francesco Retta, Olga Y. Pletjushkina та ін. "Muscle β1D Integrin Reinforces the Cytoskeleton–Matrix Link: Modulation of Integrin Adhesive Function by Alternative Splicing". Journal of Cell Biology 139, № 6 (1997): 1583–95. http://dx.doi.org/10.1083/jcb.139.6.1583.

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Expression of muscle-specific β1D integrin with an alternatively spliced cytoplasmic domain in CHO and GD25, β1 integrin-minus cells leads to their phenotypic conversion. β1D-transfected nonmuscle cells display rounded morphology, lack of pseudopodial activity, retarded spreading, reduced migration, and significantly enhanced contractility compared with their β1A-expressing counterparts. The transfected β1D is targeted to focal adhesions and efficiently displaces the endogenous β1A and αvβ3 integrins from the sites of cell–matrix contact. This displacement is observed on several types of extra

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Garcı́a, Andrés J., Marı́a D. Vega, and David Boettiger. "Modulation of Cell Proliferation and Differentiation through Substrate-dependent Changes in Fibronectin Conformation." Molecular Biology of the Cell 10, no. 3 (1999): 785–98. http://dx.doi.org/10.1091/mbc.10.3.785.

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Integrin-mediated cell adhesion to extracellular matrices provides signals essential for cell cycle progression and differentiation. We demonstrate that substrate-dependent changes in the conformation of adsorbed fibronectin (Fn) modulated integrin binding and controlled switching between proliferation and differentiation. Adsorption of Fn onto bacterial polystyrene (B), tissue culture polystyrene (T), and collagen (C) resulted in differences in Fn conformation as indicated by antibody binding. Using a biochemical method to quantify bound integrins in cultured cells, we found that differences

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Bloch, Wilhelm, Yun Fan, Ji Han, et al. "Disruption of cytoskeletal integrity impairs Gi-mediated signaling due to displacement of Gi proteins." Journal of Cell Biology 154, no. 4 (2001): 753–62. http://dx.doi.org/10.1083/jcb.200103011.

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β1 integrins play a crucial role as cytoskeletal anchorage proteins. In this study, the coupling of the cytoskeleton and intracellular signaling pathways was investigated in β1 integrin deficient (−/−) embryonic stem cells. Muscarinic inhibition of the L-type Ca2+ current (ICa) and activation of the acetylcholine-activated K+ current (IK,ACh) was found to be absent in β1 integrin−/− cardiomyocytes. Conversely, β adrenoceptor-mediated modulation of ICa was unaffected by the absence of β1 integrins. This defect in muscarinic signaling was due to defective G protein coupling. This was supported b

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Babbitt, Christopher J., Shaw-Yung Shai, Alice E. Harpf, Can G. Pham, and Robert S. Ross. "Modulation of integrins and integrin signaling molecules in the pressure-loaded murine ventricle." Histochemistry and Cell Biology 118, no. 6 (2002): 431–39. http://dx.doi.org/10.1007/s00418-002-0476-1.

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Kertsman, J., E. Cohen, M. Abdellatif та R. Wieder. "Modulation of integrin α5 in head and neck cancer cells by epidermal growth factor and its contribution to the malignant phenotype". Journal of Clinical Oncology 24, № 18_suppl (2006): 15512. http://dx.doi.org/10.1200/jco.2006.24.18_suppl.15512.

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15512 Background: The primary therapy for head and neck cancer consists of combination treatment with radiation and chemotherapy. While this combined modality approach is often curative, a significant fraction of patients have residual viable tumor cells after treatment that can result in progressive disease or relapse. We hypothesize that a significant contribution of cell survival results from interaction of cancer cells with the tumor microenvironment that includes soluble ligands of growth factor receptors and structural ligands of cell surface adhesion molecules. One of the growth factors

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Shattil, S. J., T. O'Toole, M. Eigenthaler, et al. "Beta 3-endonexin, a novel polypeptide that interacts specifically with the cytoplasmic tail of the integrin beta 3 subunit." Journal of Cell Biology 131, no. 3 (1995): 807–16. http://dx.doi.org/10.1083/jcb.131.3.807.

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The adhesive and signaling functions of integrins are regulated through their cytoplasmic domains. We identified a novel 111 residue polypeptide, designated beta 3-endonexin, that interacted with the cytoplasmic tail of the beta 3 integrin subunit in a yeast two-hybrid system. This interaction is structurally specific, since it was reduced by 64% by a point mutation in the beta 3 cytoplasmic tail (S752--&gt;P) that disrupts integrin signaling. Moreover, this interaction is integrin subunit specific since it was not observed with the cytoplasmic tails of the alpha IIb, beta 1, or beta 2 sub

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Cattelino, Anna, Chiara Albertinazzi, Mario Bossi, David R. Critchley, and Ivan de Curtis. "A Cell-free System to Study Regulation of Focal Adhesions and of the Connected Actin Cytoskeleton." Molecular Biology of the Cell 10, no. 2 (1999): 373–91. http://dx.doi.org/10.1091/mbc.10.2.373.

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Assembly and modulation of focal adhesions during dynamic adhesive processes are poorly understood. We describe here the use of ventral plasma membranes from adherent fibroblasts to explore mechanisms regulating integrin distribution and function in a system that preserves the integration of these receptors into the plasma membrane. We find that partial disruption of the cellular organization responsible for the maintenance of organized adhesive sites allows modulation of integrin distribution by divalent cations. High Ca2+ concentrations induce quasi-reversible diffusion of β1 integrins out o

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Goel, Hira Lal, Mara Fornaro, Loredana Moro та ін. "Selective modulation of type 1 insulin-like growth factor receptor signaling and functions by β1 integrins". Journal of Cell Biology 166, № 3 (2004): 407–18. http://dx.doi.org/10.1083/jcb.200403003.

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We show here that β1 integrins selectively modulate insulin-like growth factor type I receptor (IGF-IR) signaling in response to IGF stimulation. The β1A integrin forms a complex with the IGF-IR and insulin receptor substrate-1 (IRS-1); this complex does not promote IGF-I mediated cell adhesion to laminin (LN), although it does support IGF-mediated cell proliferation. In contrast, β1C, an integrin cytoplasmic variant, increases cell adhesion to LN in response to IGF-I and its down-regulation by a ribozyme prevents IGF-mediated adhesion to LN. Moreover, β1C completely prevents IGF-mediated cell

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Kimmins, Sarah, and Leslie A. MacLaren. "Cyclic Modulation of Integrin Expression in Bovine Endometrium1." Biology of Reproduction 61, no. 5 (1999): 1267–74. http://dx.doi.org/10.1095/biolreprod61.5.1267.

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DICKESON, S., T. STRICKER, A. BENTON, Y. PAN та S. SANTORO. "Affinity modulation of the α2 integrin I domain". Matrix Biology 25 (листопад 2006): S52. http://dx.doi.org/10.1016/j.matbio.2006.08.144.

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Zaveri, Toral D., Jamal S. Lewis, Natalia V. Dolgova, Michael J. Clare-Salzler, and Benjamin G. Keselowsky. "Integrin-directed modulation of macrophage responses to biomaterials." Biomaterials 35, no. 11 (2014): 3504–15. http://dx.doi.org/10.1016/j.biomaterials.2014.01.007.

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Ducharme, Lori A., and John H. Weis. "Modulation of integrin expression during mast cell differentiation." European Journal of Immunology 22, no. 10 (1992): 2603–7. http://dx.doi.org/10.1002/eji.1830221020.

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Gout, Stéphanie P., Muriel R. Jacquier-Sarlin, Laurence Rouard-Talbot, Patricia Rousselle та Marc R. Block. "RhoA-dependent Switch between α2β1 and α3β1 Integrins Is Induced by Laminin-5 during Early Stage of HT-29 Cell Differentiation". Molecular Biology of the Cell 12, № 10 (2001): 3268–81. http://dx.doi.org/10.1091/mbc.12.10.3268.

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Integrin-mediated interactions between the basement membrane and epithelial cells control the differentiation of epithelia. We characterized the modulation of adhesive behaviors to basement membrane proteins and of integrin function in the human colon adenocarcinoma HT-29 cell line, which differentiates into enterocytes after the substitution of galactose for glucose in the medium. We demonstrate an increased capability of these cells to adhere to collagen type IV during the early stage of differentiation. This effect occurs without any changes in integrin cell surface expression but rather re

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Bosquetti, Bruna, Aline Aparecida Santana, Paulo Cézar Gregório та ін. "The Role of α3β1 Integrin Modulation on Fabry Disease Podocyte Injury and Kidney Impairment". Toxins 15, № 12 (2023): 700. http://dx.doi.org/10.3390/toxins15120700.

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Podocyte dysfunction plays a crucial role in renal injury and is identified as a key contributor to proteinuria in Fabry disease (FD), primarily impacting glomerular filtration function (GFF). The α3β1 integrins are important for podocyte adhesion to the glomerular basement membrane, and disturbances in these integrins can lead to podocyte injury. Therefore, this study aimed to assess the effects of chloroquine (CQ) on podocytes, as this drug can be used to obtain an in vitro condition analogous to the FD. Murine podocytes were employed in our experiments. The results revealed a dose-dependent

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Mana, Giulia, Donatella Valdembri, and Guido Serini. "Conformationally active integrin endocytosis and traffic: why, where, when and how?" Biochemical Society Transactions 48, no. 1 (2020): 83–93. http://dx.doi.org/10.1042/bst20190309.

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Spatiotemporal control of integrin-mediated cell adhesion to the extracellular matrix (ECM) is critical for physiological and pathological events in multicellular organisms, such as embryonic development, angiogenesis, platelet aggregation, leukocytes extravasation, and cancer cell metastatic dissemination. Regulation of integrin adhesive function and signaling relies on the modulation of both conformation and traffic. Indeed, integrins exist in a dynamic equilibrium between a bent/closed (inactive) and an extended/open (active) conformation, respectively endowed with low and high affinity for

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Shewchuk, Lee J., Sean Bryan, Marina Ulanova та Neelam Khaper. "Integrin β3 prevents apoptosis of HL-1 cardiomyocytes under conditions of oxidative stressThis article is one of a selection of papers published in a Special Issue on Oxidative Stress in Health and Disease." Canadian Journal of Physiology and Pharmacology 88, № 3 (2010): 324–30. http://dx.doi.org/10.1139/y09-131.

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Integrin receptors are essential in the regulation of vital cardiac functions, and impaired integrin activity has been associated with cardiac remodeling. Oxidative stress is known to be involved in apoptosis and cardiac remodeling and thus may profoundly influence cardiac function via integrin modulation. The aim of this study was to determine the expression pattern and functional role of integrins in HL-1 cardiomyocytes under conditions of oxidative stress. Gene expression was studied by end-point and real-time PCR; surface protein expression was studied by flow cytometry; integrin knockdown

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Hato, Takaaki, Nisar Pampori та Sanford J. Shattil. "Complementary Roles for Receptor Clustering and Conformational Change in the Adhesive and Signaling Functions of Integrin αIIbβ3". Journal of Cell Biology 141, № 7 (1998): 1685–95. http://dx.doi.org/10.1083/jcb.141.7.1685.

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Integrin αIIbβ3 mediates platelet aggregation and “outside-in” signaling. It is regulated by changes in receptor conformation and affinity and/or by lateral diffusion and receptor clustering. To document the relative contributions of conformation and clustering to αIIbβ3 function, αIIb was fused at its cytoplasmic tail to one or two FKBP12 repeats (FKBP). These modified αIIb subunits were expressed with β3 in CHO cells, and the heterodimers could be clustered into morphologically detectable oligomers upon addition of AP1510, a membrane-permeable, bivalent FKBP ligand. Integrin clustering by AP

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AlJamal-Naylor, Rehab, Linda Wilson, Susan McIntyre, et al. "Allosteric Modulation of Beta1 Integrin Function Induces Lung Tissue Repair." Advances in Pharmacological Sciences 2012 (2012): 1–16. http://dx.doi.org/10.1155/2012/768720.

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The cellular cytoskeleton, adhesion receptors, extracellular matrix composition, and their spatial distribution are together fundamental in a cell's balanced mechanical sensing of its environment. We show that, in lung injury, extracellular matrix-integrin interactions are altered and this leads to signalling alteration and mechanical missensing. The missensing, secondary to matrix alteration and cell surface receptor alterations, leads to increased cellular stiffness, injury, and death. We have identified a monoclonal antibody against β1 integrin which caused matrix remodelling and enhancemen

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Davis-Lunn, Mathew, Benjamin T. Goult, and Melissa R. Andrews. "Clutching at Guidance Cues: The Integrin–FAK Axis Steers Axon Outgrowth." Biology 12, no. 7 (2023): 954. http://dx.doi.org/10.3390/biology12070954.

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Integrin receptors are essential contributors to neurite outgrowth and axon elongation. Activated integrins engage components of the extracellular matrix, enabling the growth cone to form point contacts, which connect the extracellular substrate to dynamic intracellular protein complexes. These adhesion complexes facilitate efficient growth cone migration and neurite extension. Major signalling pathways mediated by the adhesion complex are instigated by focal adhesion kinase (FAK), whilst axonal guidance molecules present in vivo promote growth cone turning or retraction by local modulation of

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Hangan-Steinman, Dolores, Wai-chi Ho, Priti Shenoy, Bosco MC Chan та Vincent L. Morris. "Differences in phosphatase modulation of α4 β1 and α5 β1 integrin-mediated adhesion and migration of B16F1 cells". Biochemistry and Cell Biology 77, № 5 (1999): 409–20. http://dx.doi.org/10.1139/o99-050.

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It is well established that a biphasic relationship exists between the adhesive strength of β1 integrins and their ability to mediate cell movement. Thus, cell movement increases progressively with adhesive strength, but beyond a certain point of optimal interaction, cell movement is reduced with further increases in adhesive function. The interplay between the various kinase and phosphatase activities provides the balance in β1 integrin-mediated cell adhesion and migration. In the present study, the significance of protein tyrosine phosphatases (PTP) and ser/thr protein phosphatases (PP) in α

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Dimitrov, Stoyan I., Luciana Besedovsky, Anja Tatiana Ramstedt Jensen, et al. "G-alpha-s-coupled receptor signaling controls circadian rhythm in integrin-mediated cell adhesion of virus-specific human CD8+ T cells." Journal of Immunology 196, no. 1_Supplement (2016): 119.17. http://dx.doi.org/10.4049/jimmunol.196.supp.119.17.

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Abstract Beta2-integrin activation in response to inside-out signaling by chemokines plays a major role in T-cell adhesion to the endothelium and the following extravasation into the inflamed tissue. We and others have previously shown that daytime increase in G-alpha-s-coupled receptor (GαsPCR) signaling, such as via beta2-adrenergic receptors counteracts integrin activation and promotes mobilization of effector CD8+ T cells from the marginal pool into the recirculation. In T cells, integrin activation is also rapidly induced by stimulation of antigen-specific T-cell receptors (TCR), resultin

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Pal, Sekhar, Kirat Kumar Ganguly, Shuvojit Moulik та Amitava Chatterjee. "Modulation of MMPs by Cell Surface Integrin Receptor α5β1". Anti-Cancer Agents in Medicinal Chemistry 12, № 7 (2012): 726–32. http://dx.doi.org/10.2174/187152012802650183.

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Kinashi, Tatsuo, Ruri Wada, Masayo Inaba, Tetsuo Asaoka, and Kiyoshi Takatsu. "Mechanisms of avidity modulation of integrin in mast cells." Ensho 16, no. 3 (1996): 163–69. http://dx.doi.org/10.2492/jsir1981.16.163.

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Rose, David M., Ronen Alon, and Mark H. Ginsberg. "Integrin modulation and signaling in leukocyte adhesion and migration." Immunological Reviews 218, no. 1 (2007): 126–34. http://dx.doi.org/10.1111/j.1600-065x.2007.00536.x.

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Zheng, Duo-Qi, Mara Fornaro, Cindy J. M. Bofetiado, Giovanni Tallini, Silvano Bosari, and Lucia R. Languino. "Modulation of cell proliferation by the integrin cytoplasmic domain." Kidney International 51, no. 5 (1997): 1434–40. http://dx.doi.org/10.1038/ki.1997.196.

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