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Relevant bibliographies by topics / Fibronectin; Integrins

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Academic literature on the topic 'Fibronectin; Integrins'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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Journal articles on the topic "Fibronectin; Integrins"

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Pankov, Roumen, Edna Cukierman, Ben-Zion Katz, Kazue Matsumoto, Diane C. Lin, Shin Lin, Cornelia Hahn, and Kenneth M. Yamada. "Integrin Dynamics and Matrix Assembly." Journal of Cell Biology 148, no. 5 (March 6, 2000): 1075–90. http://dx.doi.org/10.1083/jcb.148.5.1075.

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Fibronectin matrix assembly is a multistep, integrin-dependent process. To investigate the role of integrin dynamics in fibronectin fibrillogenesis, we developed an antibody-chasing technique for simultaneous tracking of two integrin populations by different antibodies. We established that whereas the vitronectin receptor αvβ3 remains within focal contacts, the fibronectin receptor α5β1 translocates from focal contacts into and along extracellular matrix (ECM) contacts. This escalator-like translocation occurs relative to the focal contacts at 6.5 ± 0.7 μm/h and is independent of cell migration. It is induced by ligation of α5β1 integrins and depends on interactions with a functional actin cytoskeleton and vitronectin receptor ligation. During cell spreading, translocation of ligand-occupied α5β1 integrins away from focal contacts and along bundles of actin filaments generates ECM contacts. Tensin is a primary cytoskeletal component of these ECM contacts, and a novel dominant-negative inhibitor of tensin blocked ECM contact formation, integrin translocation, and fibronectin fibrillogenesis without affecting focal contacts. We propose that translocating α5β1 integrins induce initial fibronectin fibrillogenesis by transmitting cytoskeleton-generated tension to extracellular fibronectin molecules. Blocking this integrin translocation by a variety of treatments prevents the formation of ECM contacts and fibronectin fibrillogenesis. These studies identify a localized, directional, integrin translocation mechanism for matrix assembly.

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Balasubramanian, Lavanya, Abu Ahmed, Chun-Min Lo, James S. K. Sham, and Kay-Pong Yip. "Integrin-mediated mechanotransduction in renal vascular smooth muscle cells: activation of calcium sparks." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 293, no. 4 (October 2007): R1586—R1594. http://dx.doi.org/10.1152/ajpregu.00025.2007.

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Integrins are transmembrane heterodimeric proteins that link extracellular matrix (ECM) to cytoskeleton and have been shown to function as mechanotransducers in nonmuscle cells. Synthetic integrin-binding peptide triggers Ca2+ mobilization and contraction in vascular smooth muscle cells (VSMCs) of rat afferent arteriole, indicating that interactions between the ECM and integrins modulate vascular tone. To examine whether integrins transduce extracellular mechanical stress into intracellular Ca2+ signaling events in VSMCs, unidirectional mechanical force was applied to freshly isolated renal VSMCs through paramagnetic beads coated with fibronectin (natural ligand of α5β1-integrin in VSMCs). Pulling of fibronectin-coated beads with an electromagnet triggered Ca2+ sparks, followed by global Ca2+ mobilization. Paramagnetic beads coated with low-density lipoprotein, whose receptors are not linked to cytoskeleton, were minimally effective in triggering Ca2+ sparks and global Ca2+ mobilization. Preincubation with ryanodine, cytochalasin-D, or colchicine substantially reduced the occurrence of Ca2+ sparks triggered by fibronectin-coated beads. Binding of VSMCs with antibodies specific to the extracellular domains of α5- and β1-integrins triggered Ca2+ sparks simulating the effects of fibronectin-coated beads. Preincubation of microperfused afferent arterioles with ryanodine or integrin-specific binding peptide inhibited pressure-induced myogenic constriction. In conclusion, integrins transduce mechanical force into intracellular Ca2+ signaling events in renal VSMCs. Integrin-mediated mechanotransduction is probably involved in myogenic response of afferent arterioles.

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Kim, H. J., D. H. Ingbar, and C. A. Henke. "Integrin mediation of type II cell adherence to provisional matrix proteins." American Journal of Physiology-Lung Cellular and Molecular Physiology 271, no. 2 (August 1, 1996): L277—L286. http://dx.doi.org/10.1152/ajplung.1996.271.2.l277.

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Lung injury causes alveolar type I epithelial cell death, basement membrane denudation, and alveolar flooding with serum fibronectin and fibrinogen. For successful restoration of normal architecture, the epithelium must be regenerated from progenitor type II alveolar cells. Using adhesion assays, we examined whether type II alveolar cells adhere to the provisional matrix proteins fibronectin, fibrinogen, and fibrin, and whether integrins mediate this adherence. Rat type II cells adhered to fibronectin, vitronectin, fibrinogen, and fibrin. Synthetic RGD (arginine-glycine-aspartic acid) peptide blocked this adhesion. Flow cytometry and Western analysis indicated that type II cells expressed beta 1- and alpha v beta 3-integrins. Anti-beta 1-and anti-alpha v beta 3-integrin antibodies blocked type II cell adhesion to fibronectin and to fibronectin and fibrinogen, respectively. In summary, type II cells adhered to fibronectin, fibrinogen, and fibrin, and adhesion was partially mediated by integrins. This study provides the first evidence of type II cell adhesion to fibrin gels and vitronectin, beta 1- and alpha v beta 3-integrin mediation of type II cell adhesion, and the presence of the alpha v beta 3-integrin on type II epithelial cells.

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Akimov, Sergey S., Dmitry Krylov, Laurie F. Fleischman, and Alexey M. Belkin. "Tissue Transglutaminase Is an Integrin-Binding Adhesion Coreceptor for Fibronectin." Journal of Cell Biology 148, no. 4 (February 21, 2000): 825–38. http://dx.doi.org/10.1083/jcb.148.4.825.

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The protein cross-linking enzyme tissue transglutaminase binds in vitro with high affinity to fibronectin via its 42-kD gelatin-binding domain. Here we report that cell surface transglutaminase mediates adhesion and spreading of cells on the 42-kD fibronectin fragment, which lacks integrin-binding motifs. Overexpression of tissue transglutaminase increases its amount on the cell surface, enhances adhesion and spreading on fibronectin and its 42-kD fragment, enlarges focal adhesions, and amplifies adhesion-dependent phosphorylation of focal adhesion kinase. These effects are specific for tissue transglutaminase and are not shared by its functional homologue, a catalytic subunit of factor XIII. Adhesive function of tissue transglutaminase does not require its cross-linking activity but depends on its stable noncovalent association with integrins. Transglutaminase interacts directly with multiple integrins of β1 and β3 subfamilies, but not with β2 integrins. Complexes of transglutaminase with integrins are formed inside the cell during biosynthesis and accumulate on the surface and in focal adhesions. Together our results demonstrate that tissue transglutaminase mediates the interaction of integrins with fibronectin, thereby acting as an integrin-associated coreceptor to promote cell adhesion and spreading.

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Orr, A. Wayne, Mark H. Ginsberg, Sanford J. Shattil, Hans Deckmyn, and Martin A. Schwartz. "Matrix-specific Suppression of Integrin Activation in Shear Stress Signaling." Molecular Biology of the Cell 17, no. 11 (November 2006): 4686–97. http://dx.doi.org/10.1091/mbc.e06-04-0289.

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Atherosclerotic plaque develops at sites of disturbed flow. We previously showed that flow activates endothelial cell integrins, which then bind to the subendothelial extracellular matrix (ECM), and, in cells on fibronectin or fibrinogen, trigger nuclear factor-κB activation. Additionally, fibronectin and fibrinogen are deposited into the subendothelial ECM at atherosclerosis-prone sites at early times. We now show that flow activates ECM-specific signals that establish patterns of integrin dominance. Flow induced α2β1 activation in cells on collagen, but not on fibronectin or fibrinogen. Conversely, α5β1 and αvβ3 are activated on fibronectin and fibrinogen, but not collagen. Failure of these integrins to be activated on nonpermissive ECM is because of active suppression by the integrins that are ligated. Protein kinase A is activated specifically on collagen and suppresses flow-induced αvβ3 activation. Alternatively, protein kinase Cα is activated on fibronectin and mediates α2β1 suppression. Thus, integrins actively cross-inhibit through specific kinase pathways. These mechanisms may determine cellular responses to complex extracellular matrices.

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Wu, C., A. E. Chung, and J. A. McDonald. "A novel role for alpha 3 beta 1 integrins in extracellular matrix assembly." Journal of Cell Science 108, no. 6 (June 1, 1995): 2511–23. http://dx.doi.org/10.1242/jcs.108.6.2511.

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To study the biological role of alpha 3 beta 1 integrins in cell adhesion, migration, and in the deposition of extracellular matrix, we stably expressed the human alpha 3 integrin subunit in the alpha 4, alpha 5 integrin deficient CHO cell line B2. The expression of alpha 3 beta 1 integrins enhanced cell adhesion on entactin (also known as nidogen), but not on fibronectin. Using recombinant GST-fusion proteins that span the entire length of the entactin molecule, we located cell adhesive activity to the G2 domain of entactin. These results suggest that the alpha 3 beta 1 integrin functions as an adhesion receptor interacting with the G2 domain of entactin. On the other hand, the expression of alpha 3 beta 1 integrins did not confer the ability to migrate on entactin. Strikingly, the expression of alpha 3 beta 1 dramatically increased the deposition of entactin and fibronectin into the pericellular matrix. This was accompanied by increased binding activity of the 29 kDa amino-terminal domain of fibronectin. Thus, similar to alpha 5 beta 1 integrins, alpha 3 beta 1 integrins can play an important role in modulating the assembly of pericellular matrices. However, unlike fibronectin deposition supported by alpha 5 beta 1, alpha 3 beta 1 supported fibronectin deposition into pericellular matrix was not inhibited by antibodies binding to the RGD containing cell adhesion domain of fibronectin, demonstrating that the two processes are mechanistically distinct. The role of alpha 3 beta 1 in pericellular matrix assembly potentially implicates this receptor in the assembly and/or recognition of entactin-containing pericellular matrices, an observation consistent with its apparent role in the renal glomerulus of the mammalian kidney.

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Watt, F. M., M. D. Kubler, N. A. Hotchin, L. J. Nicholson, and J. C. Adams. "Regulation of keratinocyte terminal differentiation by integrin-extracellular matrix interactions." Journal of Cell Science 106, no. 1 (September 1, 1993): 175–82. http://dx.doi.org/10.1242/jcs.106.1.175.

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Suspension-induced terminal differentiation of human epidermal keratinocytes can be inhibited by fibronectin through binding to the alpha 5 beta 1 integrin. We have investigated the effect of fibronectin on expression of integrins and proteins of the actin cytoskeleton and have explored the nature of the differentiation stimulus by testing different combinations of anti-integrin monoclonal antibodies or extracellular matrix proteins in the suspension assay. Fibronectin prolonged cell surface expression of beta 1 integrins but did not overcome the inhibition of intracellular transport of integrins that occurs when keratinocytes are placed in suspension. Fibronectin did not prevent the suspension-induced decline in the level of mRNAs encoding the beta 1 integrin subunit, actin, filamin and alpha-actinin; furthermore, the inhibition of terminal differentiation did not depend on the state of assembly of microfilaments or microtubules. Terminal differentiation could be partially inhibited by an adhesion-blocking monoclonal antibody to the beta 1 integrin subunit or by a combination of adhesion blocking antibodies recognising the alpha subunits that associate with beta 1 (alpha 2, alpha 3 and alpha 5). Although laminin and type IV collagen do not inhibit terminal differentiation individually, they were inhibitory when added to cells in combination with a low concentration of fibronectin. We conclude that the proportion of keratinocyte beta 1 integrins occupied by ligand can regulate the initiation of terminal differentiation independently of the state of assembly of the actin cytoskeleton.

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Sottile, J., D. C. Hocking, and K. J. Langenbach. "Fibronectin polymerization stimulates cell growth by RGD-dependent and -independent mechanisms." Journal of Cell Science 113, no. 23 (December 1, 2000): 4287–99. http://dx.doi.org/10.1242/jcs.113.23.4287.

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Many aspects of cell behavior are regulated by cell-extracellular matrix interactions, including cell migration and cell growth. We previously showed that the addition of soluble fibronectin to collagen-adherent fibronectin-null cells enhances cell growth. This growth-promoting effect of fibronectin depended upon the deposition of fibronectin into the extracellular matrix; occupancy and clustering of fibronectin-binding integrins was not sufficient to trigger enhanced cell growth. To determine whether the binding of integrins to fibronectin's RGD site is required for fibronectin-enhanced cell growth, the ability of fibronectin lacking the integrin-binding RGD site (FN(Delta)RGD) to promote cell growth was tested. FN(Delta)RGD promoted cell growth when used as an adhesive substrate or when added in solution to collagen-adherent fibronectin-null cells. Addition of FN(Delta)RGD to collagen-adherent fibronectin-null cells resulted in a 1.6-1.8x increase in cell growth in comparison with cells grown in the absence of fibronectin. The growth-promoting effects of FN(Delta)RGD and wild-type fibronectin were blocked by inhibitors of fibronectin polymerization, including the anti-fibronectin antibody, L8. In addition, FN(Delta)RGD-induced cell growth was completely inhibited by the addition of heparin, and was partially blocked by either heparitinase-treatment or by addition of recombinant fibronectin heparin-binding domain. Heparin and heparitinase-treatment also partially blocked the growth-promoting effects of wild-type fibronectin, as well as the deposition of wild-type fibronectin into the extracellular matrix. These data suggest that cell surface heparan-sulfate proteoglycans contribute to the growth-promoting effects of FN(Delta)RGD and wild-type fibronectin. Addition of heparin, treatment with heparitinase, or incubation with monoclonal antibody L8 all inhibited the formation of short linear FN(Delta)RGD fibrils on the cell surface. Inhibitory (beta)1 integrin antibodies had no effect on FN(Delta)RGD fibril formation, FN(Delta)RGD-induced cell growth, or cell adhesion on FN(Delta)RGD-coated substrates. These data suggest that fibronectin fibril formation can promote cell growth by a novel mechanism that is independent of RGD-integrin binding, and that involves cell surface proteoglycans.

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Guan, J. L., J. E. Trevithick, and R. O. Hynes. "Fibronectin/integrin interaction induces tyrosine phosphorylation of a 120-kDa protein." Cell Regulation 2, no. 11 (November 1991): 951–64. http://dx.doi.org/10.1091/mbc.2.11.951.

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We describe a 120-kDa protein (pp120) that is phosphorylated on tyrosine in cells attached to fibronectin-coated surfaces. The protein appears to be located in focal contacts where it codistributes with beta 1 integrins. pp120 is distinct from the beta 1 subunit of integrins and from vinculin and alpha-actinin. pp120 is rapidly dephosphorylated in cells suspended by trypsinization but becomes rapidly phosphorylated in cells attaching and spreading on fibronectin. Attachment of cells to RGD-containing peptides, polylysine, or concanavalin A is not sufficient to induce phosphorylation of pp120. The 120-kDa cell-binding domain of fibronectin can induce some phosphorylation of pp120, but further phosphorylation occurs in the presence also of the heparin-binding domain of fibronectin. Phosphorylation of pp120 precedes, but is correlated with, subsequent cell spreading. Phosphorylation of pp120 can also be triggered by attachment of cells to anti-integrin antibodies, and this requires the cytoplasmic domain of the integrin beta 1 subunit. Thus interaction of beta 1 integrins with extracellular ligands (fibronectin or antibodies) triggers phosphorylation of an intracellular 120-kDa protein, pp120, that may be involved in the responses of cells to attachment.

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TANI, Patricia H., Joseph C. LOFTUS, and Ron D. BOWDITCH. "In vitro selection of fibronectin gain-of-function mutations." Biochemical Journal 365, no. 1 (July 1, 2002): 287–94. http://dx.doi.org/10.1042/bj20020067.

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Directed protein evolution, which employs a combination of random mutagenesis, phage display, and in vitro selection, was used to identify second-site suppressors of the fibronectin (Fn) cell binding domain mutation Asp1495Ala (RGA). The mutations in the Fn 9th (3fn9) and 10th (3fn10) type III repeats obtained after selection on purified integrins αIIbβ3(D119Y) and α5β1 are reported. The 3fn9–10(D1495A) phage with substitution mutations at Asp1418, which is located within the linker region between 3fn9 and 3fn10, enhanced binding to the integrins αIIbβ3 and α5β1, but not αvβ3. The substitution mutations identified at residue Asp1418 were introduced into the native recombinant 3fn9–10 sequence and found to augment binding to αIIbβ3, demonstrating that the observed gain-of-function phenotype was independent of the multivalent character of the phage. These results support the following conclusions. First, regions of Fn in addition to the RGD loop are in close proximity to αIIbβ3 and α5β1 and are capable of participating in the binding to these integrins. Secondly, the conformational relationship between the 3fn9 and 3fn10 modules may be an important factor in the binding of Fn to these two integrins. Thirdly, other altered properties of Fn-integrin interactions, such as integrin specificity, may also be selected. This is the first description of Fn mutations that augment binding to integrins. The ability to select for particular phenotypes in vitro and the subsequent characterization of these mutations should further our understanding of the molecular details involved in the association of integrins and their ligands. Additionally, these higher-affinity 3fn9–10 ligands provide a starting point for further in vitro evolution and engineering of integrin-specific modules.

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Dissertations / Theses on the topic "Fibronectin; Integrins"

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Yee, Karen O. "Smooth muscle cell interaction with fibrin-A possible mechanism for vessel narrowing during atherosclerosis /." Thesis, Connect to this title online; UW restricted, 1998. http://hdl.handle.net/1773/5049.

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Phan, Isabelle Q. H. "Structural studies of modular proteins by NMR and molecular modelling." Thesis, University of Oxford, 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.294330.

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Atieh, Youmna Marie Lyne. "Interplay between cancer cells and cancer-associated fibroblasts in tumor invasion and metastasis formation." Thesis, Paris 6, 2017. http://www.theses.fr/2017PA066140/document.

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Les carcinomes sont des cancers touchant plusieurs organes du corps humain, notamment les seins, le pancréas, les poumons, l'intestin… et sont issus de la transformation de cellules épithéliales en cellules tumorales. Au cours du développement d'une tumeur, les cellules cancéreuses, contrairement aux cellules normales, acquièrent la capacité de se déplacer dans le corps humain, jusqu'à coloniser des organes voisins. Ces colonies sont appelées métastases. Le processus métastatique est responsable de 90% des décès dans le cadre des carcinomes. Ce processus n'est pas dû à l'action isolée des cellules cancéreuses mais est aussi le résultat d'une coopération entre la tumeur et son voisinage – le microenvironnement tumoral – favorisant la survie et la migration des cellules cancéreuses. Les fibroblastes sont une population cellulaire du microenvironnement tumoral. Il a été démontré que les fibroblastes sont activés à proximité des cellules cancéreuses ; on les qualifie de fibroblastes associés au cancer ou CAFs. Dans des tissus de patients, les tumeurs les plus agressives corrèlent avec un enrichissement en fibroblastes et une matrice plus dense. Mon projet de thèse illustre un nouveau mécanisme de coopération entre CAFs et cellules cancéreuses. Cibler l’action des fibroblastes pourrait ralentir la progression tumorale, voire bloquer la formation de métastases
Cancer-associated fibroblasts (CAFs) are the most abundant cells of the tumor stroma. Their capacity to contract the matrix and induce invasion of cancer cells has been well-documented. However, it is not clear if CAFs remodel the matrix by other means (degradation, matrix deposition or stiffening). This project demonstrates that CAFs induce cancer cell invasion through assembly of FN into the matrix. CAFs assembled fibronectin (FN) mainly via integrin α5 but integrin αvβ3 was necessary for initial mechanosensing and fibrillar adhesion formation. In the absence of FN, contractility of the matrix by CAFs is preserved. When degradation is impaired, CAFs retain the capacity to induce invasion in a FN-dependent manner. In all cases, the levels of expression of integrin β3 and the amount of assembled FN was directly proportional to the invasion induced by fibroblast populations. Our results highlight FN assembly and integrin β3 as new hallmarks of CAFs. We also noticed that cancer cells migrate towards CAFs suggesting a possible chemotactic response. Using Dunn’s chemotaxis chamber, we found that cancer cells migrate along a gradient of CAF-conditioned media and a gradient of fibronectin. Finally, orthotopic injections of cancer cells and CAFs in the colon wall of mice revealed that CAFs stimulate metastasis of cancer cells to the liver. In conclusion, our data show that CAFs promote cancer cell invasion by depositing fibronectin that can guide cancer cells favoring metastasis formation

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Altroff, Harri. "The role of FIII domains of human fibronectin in cell adhesion." Thesis, University of Oxford, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.343279.

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Baneyx, Gretchen W. "The role of mechanical tension in fibronectin matrix assembly /." Thesis, Connect to this title online; UW restricted, 2001. http://hdl.handle.net/1773/8059.

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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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Kong, Fang. "Interaction of integrin α₅β₁and fibronectin under force." Diss., Georgia Institute of Technology, 2008. http://hdl.handle.net/1853/31705.

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Integrins are heterodimers that mediate cell adhesion in many physiological processes. Binding of integrins to ligands provides anchorage and signals for the cell. However, how force regulates integrin/ligand dissociation is unclear. Atomic force microscopy was used to measure the force dependence of lifetimes of single bonds between a FN fragment and integrin α₅β₁. First, lifetime-force relationships demonstrated that force prolonged bond lifetimes in the 10-30 pN range, a behavior called catch bonds. Changing divalent cations from Ca²⁺/Mg²⁺ to Mg²⁺/EGTA and to Mn²⁺ caused more pronounced catch bonds. A truncated α₅β₁ construct containing the headpiece but not the legs (trα₅β₁-Fc) formed much longer-lived catch bonds in the same force range. Bindings of two activating mAbs, 12G10 and TS2/16, left shift the catch bond and converted catch bonds to slip bonds, respectively. Catch bonds may provide a mechanical mechanism for the cell to regulate adhesion by applying different forces. Second, FNIII₇₋₁₀/α₅β₁-Fc/GG-7 bond was stretched to ~ 30 pN and then relaxed to ~ 7 pN at which the bond's lifetime was measured. The strong bond state induced by the 30 pN stretching stayed stable even after the force was reduced to 7 pN. In other words, lower the force would not weaken FNIII₇₋₁₀/α₅β₁-Fc bond once it had been stretched. Similar behaviors were observed for FNIII₇₋₁₀/trα₅β₁-Fc and FNIII₇₋₁₀/mα₅β₁interactions. In addition, the efficiency of the force to induce such a strong bond state for FNIII₇₋₁₀/α₅β₁-Fc interaction in 2 mM Mg²⁺/EGTA condition was characterized. The probability of force to induce the strong bond state increased as force increased and when the force reached 26 pN, all bonds were transit to the strong state. Moreover, reversible unbending of α₅β₁binding with FNIII₇₋₁₀ under mechanical force were observed, which proved that integrin bending and unbending was dynamic. Importantly, integrin could restore bent conformation even when engaged with its ligand, providing a mechanism for mechanotransduction. Third, structural changes of α₅β₁under force were observed. The structural changes did not change the trend of lifetime-force relationships of FNIII₇₋₁₀/α₅β₁/GG-7 bond. Moreover, the lifetime for the structural changes to occur and molecular length changes caused by them were characterized.

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Stupack, Dwayne G. P. "Utilization and regulation of integrins by lymphoid cells to adhere to fibronectin and collagen." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1996. http://www.collectionscanada.ca/obj/s4/f2/dsk3/ftp04/nq23671.pdf.

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Owen, Caroline Ann. "Monocyte adherence to fibronectin : role of CD11/CD18 integrins and relationship to other monocyte functions." Thesis, University of Birmingham, 1993. http://etheses.bham.ac.uk//id/eprint/36/.

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Regulated adherence of monocytes to extracellular matrix macromolecules is a prerequisite for their accumulation at sites of pulmonary infection and inflammation. To begin to assess the pathobiological importance of alterations in monocyte adherence to extracellular matrix in inflammatory lung diseases, the adherence properties of monocytes from patients with an inflammatory lung disease (bronchiectasis) and healthy subjects to a representative matrix component (fibronectin) were compared. Spontaneous adherence of monocytes from the control subjects was 20 to 25%, whereas that of the patients' cells was 2 to 3-fold higher and correlated with the severity of airway inflammation. Endotoxin (LPS) and cytokines from areas of airway disease are likely to be responsible for the observed monocyte activation since: 1) LPS was detected in plasma from all of the patients but none of the control subjects; and 2) LPS and cytokines produced dose-related increases in the adherence of normal monocytes in vitro. Monocyte adherence to fibronectin was substantially mediated by CD11/CD18 integrins, via both RGD-dependent and RGD-independent mechanisms. These data indicate that signals arising from foci of pulmonary inflammation are likely determinants of the accumulation of monocytes in the lungs of patients with chronic inflammatory lung diseases. There was a striking relationship between the adherence properties of monocytes and functions that are of biological importance at sites of inflammation. Spontaneously adherent monocytes had an "inflammatory effector" phenotype, non-adherent cells had an "immune modulatory" phenotype and monocytes that could stimulated to adhere by LPS (LPS-adherent cells) had an intermediate phenotype. In addition, only the adherent monocyte subpopulations were replete with HLE and these cells contained a substantial (10 to 11-fold) molar excess of HLE compared with the physiological inhibitor of this enzyme (a1-antitrypsin). Maturation in vitro increased the accumulation of a1-antitrypsin by all of the monocyte subpopulations. In contrast, proinflammatory mediators up-regulated a1-antitrypsin accumulation by only the spontaneously adherent cells, probably by translational or post-translational mechanisms. In conclusion, these data indicate that monocytes are heterogeneous in their ability to accumulate at sites of infection and inflammation. In addition, the capacity of monocytes to adhere to fibronectin is related to monocyte functions that are of biological importance at sites of infection and inflammation. Furthermore, LPS released from foci of infection, may induce the accumulation of monocytes with an inflammatory effector phenotype, and may thereby promote resolution of tissue infection. Alternatively, LPS may promote the recruitment of monocytes with capacity to contribute to HLE-mediated tissue injury.

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Reyes, Catherine Diane. "Collagen- and Fibronectin-Mimetic Integrin-Specific Surfaces That Promote Osseointegration." Diss., Georgia Institute of Technology, 2006. http://hdl.handle.net/1853/11599.

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Cell adhesion to the extracellular matrix through cell-surface integrin receptors is essential to development, wound healing, and tissue remodeling and therefore represents a central theme in the design of bioactive surfaces that successfully interface with the body. This is especially significant in the areas of integrative implant coatings since adhesion triggers signals that regulate cell cycle progression and differentiation in multiple cellular systems. The interactions of osteoblasts with their surrounding extracellular matrix are essential for skeletal development and homeostasis and the maintenance of the mature osteoblastic phenotype. Our objective was to engineer integrin-specific bioactive surfaces that support osteoblastic differentiation and promote osseointegration by mimicking these interactions. We target two specific integrins essential to osteoblast differentiation the type I collagen receptor alpha2beta1 and the fibronectin receptor alpha5beta1. The central hypothesis of this project was that the controlled presentation of type I collagen and fibronectin binding domains onto well-defined substrates would result in integrin-specific bioadhesive surfaces that support osteoblastic differentiation, matrix mineralization, and osseointegration. We have demonstrated that these biomimetic peptides enhance bone formation and mechanical osseointegration on titanium implants in a rat tibia cortical bone model. We have also shown that the presentation of multiple integrin-binding ligands synergize to enhance intracellular signaling and proliferation. Finally, we demonstrate the advantage of the short biomimetic peptides over the native ECM proteins. This research is significant because it addresses current orthopaedic implant limitations by specifically targeting cellular responses that are critical to osteoblastic differentiation and bone formation. This biomolecular approach provides a versatile and robust strategy for developing bioactive surfaces that enhance bone repair and osseointegration of orthopaedic implants.

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Books on the topic "Fibronectin; Integrins"

1

Owen, Caroline A. Monocyte adherence to fibronectin: Role of CD11/CD18 integrins and relationship to other monocyte functions. Birmingham: University of Birmingham, 1992.

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2

Strooper, B. De. Biosynthesis and Expression of the Human A5B1-integrin Fibronectin Receptor. Leuven University Press, 1991.

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Book chapters on the topic "Fibronectin; Integrins"

1

Huynh, Khon, Phong Le, Thao Nguyen, Hiep Nguyen, and Volker Stoldt. "Characterization of Fibronectin Assembly by Adherent Platelets Under Flow Conditions: Effect of Shear Stress and Role of β3 Integrins." In 6th International Conference on the Development of Biomedical Engineering in Vietnam (BME6), 779–82. Singapore: Springer Singapore, 2017. http://dx.doi.org/10.1007/978-981-10-4361-1_132.

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Aota, Shin-Ichi, and Kenneth M. Yamada. "Fibronectin and Cell Adhesion: Specificity of Integrin-Ligand Interaction." In Advances in Enzymology - and Related Areas of Molecular Biology, 1–21. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2006. http://dx.doi.org/10.1002/9780470123164.ch1.

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Humphries, Martin J., Joe Sheridan, A. Paul Mould, and Peter Newham. "Mechanisms of VCAM-1 and Fibronectin Binding to Integrin α4β1: Implications for Integrin Function and Rational Drug Design." In Ciba Foundation Symposium 189 - Cell Adhesion and Human Disease, 177–99. Chichester, UK: John Wiley & Sons, Ltd., 2007. http://dx.doi.org/10.1002/9780470514719.ch13.

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DeSimone, Douglas W., Jim C. Smith, James E. Howard, David G. Ransom, and Karen Symes. "The Expression of Fibronectins and Integrins During Mesodermal Induction and Gastrulation in Xenopus." In Gastrulation, 185–98. Boston, MA: Springer US, 1991. http://dx.doi.org/10.1007/978-1-4684-6027-8_11.

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Saba, Thomas M. "Kinetics of Plasma Fibronectin: Relationship to Phagocytic Function and Lung Vascular Integrity." In Fibronection, 395–439. Elsevier, 1989. http://dx.doi.org/10.1016/b978-0-12-508470-3.50020-1.

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"Fibronectin: Role in Phagocytic Host Defense and Lung Vascular Integrity." In Fibronectin in Health and Disease, edited by Thomas M. Saba, 49–68. CRC Press, 2018. http://dx.doi.org/10.1201/9781351072038-4.

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Ruoslahti, Erkki. "Fibronectin and Its Integrin Receptors in Cancer." In Advances in Cancer Research, 1–20. Elsevier, 1999. http://dx.doi.org/10.1016/s0065-230x(08)60772-1.

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Conference papers on the topic "Fibronectin; Integrins"

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Butler, Peter J., Amit Bhatnagar, and Michael Ferko. "Multiscale Stress Analysis of Sheared and Focally-Adhered Endothelial Cells: Role of Subcellular Matrix Moduli in Focal Adhesion-Mediated Signaling." In ASME 2007 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2007. http://dx.doi.org/10.1115/sbc2007-176604.

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Focal adhesions (FAs) and their associated integrins are thought to act as mechanosensors and transducers of shear stress into intracellular biochemical signals. However, to date there exists no quantification of the magnitude of forces generated at integrin molecules in response to apically-applied fluid shear stress. Thus, we used finite element analysis of fluid dynamics and cellular stresses to compute FA stresses from solid models of focally-adhered endothelial cells. These models were developed from quantitative 3-D microscopy and total internal reflection fluorescence (TIRF) microscopy of calcein-stained endothelial cells. Extrusion coupling variables mapped stresses from the macroscale cell model to individual microscale 3-D models of FAs determined from quantitative TIRF. Included in the microscale FA model were moduli for subcellular matrix (SCM) (e.g. hyaluronan, hyaluronaic acid and other glycocalyx constituents) and extracellular matrix (ECM) (e.g. collagen, fibronectin). Integrin forces were estimated from assumed bonds densities and computed FA stresses. Maximal bond tension obtained from the simulation for a single integrin-extracellular matrix (ECM) bond was .1pN. Thus, it is unlikely that integrin-ECM bonds or chemical activities are appreciably affected by shear stress. The computational model, however, supports an alternative model of activation in and reorganization of FAs in which shear stress-induced forces cause the membrane to bend toward and away from the ECM immediately upstream and downstream of the FA, respectively. The simulation also suggests that the elasticity of the SCM plays an important role in modulating shear-induced FA reorganization. These results support a new model of endothelial cell activation by shear stress in which integrins and FAs participate in the directional biasing of force-induce signaling but do not initiate it.

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Gallant, Nathan D., and Kranthi Kumar Elineni. "Regulation of Adhesion Strength by Focal Adhesion Position and Cell Shape." In ASME 2012 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2012. http://dx.doi.org/10.1115/sbc2012-80832.

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Cell adhesion to extracellular matrices is critical to numerous cellular functions and is primarily mediated by integrin receptors. Binding and aggregation of integrins leads to the formation of focal adhesions (FA) which connect the cytoskeleton to the extracellular matrix in order to reinforce adhesion and transmit signals [1]. Preliminary observations indicated preferential recruitment of FAs to the periphery of the cell spreading area on both uniformly coated and micropatterned fibronectin surfaces (Fig. 1). The current study investigates the biophysical regulation of cell adhesion strength based on the size and position of FA with the central hypothesis that peripheral FAs stabilize adhesion strength. The hypothesis was tested by delineating the cell spreading area from the total cell adhesive area by employing microcontact printing to pattern substrates with a series of circular and annular adhesive islands which control cell shape (Fig. 2). A well characterized hydrodynamic shear assay known as the spinning disk device was used to quantify the adhesion strength of cells adhered to the micropatterns [2].

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Phillips, David R., Laurence A. Fitzgerald, Leslie V. Parise, and Israel F. Charo. "The Platelet Membrane Glycoprotein IIb-III a Complex: Member of a Superfamily of Adhesive Protein Receptors." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643727.

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The glycoprotein (GP) IIb-IIIa complex isthe receptor for fibrinogen,fibronectin and von Willebrand factor on the surface of activated platelets that mediates platelet aggregation.The GP IIb-IIIa complex contains two subunits; an a subunit, GP IIb, and a smaller 8 subunit, GP IIIa. To identify the subunits of GP IIb-IIIa responsible for fibrinogen binding, we examined the ability of purified subunitsto bind to immobilized fibrinogen. Both the GP IIb and the GP III a subunits have fibrinogen binding activity, suggesting that fibrinogen binds to multiple sites onthe GP I Ib-IIIa complex.A GP Ilb-IIIa-like complex has been identified on endothelial cells which is immunoreactive with antibodies raised against platelet GP IIb-III a. This complex binds a similar broadspectrum of adhesive proteins as plateletGP IIb-IIIa and appears to mediate the attachment of endothelial cells to the extracellular matrix. We have established, however, that while GP Ilia in endothelial cells is the same primary translation product as platelet GP Ilia, the endothelialcell "GP lib" is a different, but closely related, protein from platelet GP lib. This close relationship of the receptors on these two cells is reflective of recent observations in several laboratories which have shown that a wide variety of cells contain surface glycoproteins which have structural and functionalsimilarities to the GP IIb-IIIa complexinplatelets and the "GP IIb-IIIa-like" complex in endothelial cells.These glycoproteins, which have been termed "integrins" or "cytoadhesins", are complexes of highly homologous a and 8 subunits, mediate cell-cell or cel 1-substrata interactions, and may also bind the RGD sequence on adhesive proteins. Although in vertebrates this family includes at least ten receptor complexes, there are only three known 8 subunits, each of which defines a subset of receptors. One is GP IIIa, the 8 subunit for GP IIb-IIIa and the vitronectin receptor; another is the 8 subunit for the fibronectin receptors and the very late antigens on lymphocytes; the third is the 8subunit of the Mac-1, LFA-1, and P150/95 antigens on leukocytes. These three 6 subunits have been cloned and sequenced. Each contains 746-777 amino acids, a singletransmembrane domain near the carboxy terminus, 56 cysteines in identical positionsof the proteins, 31 of which are clustered into four repeats, and an overall identity in 45-47% of their amino acids. The asubunits are more diverse in size but appear to have a similar degree of homology.The available sequence information indicates that they contain a single transmembrane domain near their carbody terminii and four tandem repeats near their amino terminii which include sequences indicativeof four Ca2+-binding sites. These may account for the known Ca2+-binding properties of GP IIb. GP I Ib-IIIa and the other adhesive protein receptors therefore appear to have two membrane insertion sites, one on each subunit,with short cytoplasmic domains derived from the carboxy terminii of the two subunits. The amino terminii along with most ofthe mass of these proteins is extracellular. It can be anticipated that the highlyhomologous sequences between GP IIb-IIIa and the other adhesive protein receptors will help identify the functional domainswhich have been conserved since their evolutionary divergences.

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Mahan, Anne, Yao Chen, and Margaret A. Schwarz. "Alpha5Beta1 Integrin / Fibronectin Interactions Mediate Type 2 Pneumocyte Adhesion." In American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a1853.

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Schwarz, Margaret A., Susan K. Legan, Haiming Xu, and Ramsey Foty. "Pulmonary Epithelial Lumen Formation Requires α5β1 Integrin Regulated Fibronectin Deposition." In American Thoracic Society 2012 International Conference, May 18-23, 2012 • San Francisco, California. American Thoracic Society, 2012. http://dx.doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a5554.

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Regis, Shawn, Manisha Jassal, Sina Youssefian, Nima Rahbar, and Sankha Bhowmick. "Quantitative Studies of Fibronectin Adsorption on Submicron Scaffolds." In ASME 2012 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2012. http://dx.doi.org/10.1115/sbc2012-80633.

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Fibronectin plays a crucial role in adhesion of several cell types, mainly due to the fact that it is recognized by at least ten different integrin receptors. Since most cell types can bind to fibronectin, it becomes involved in many various biological processes. The interaction of cells with ECM proteins such as fibronectin provides the signals affecting morphology, motility, gene expression, and survival of cells [1]. Fibronectin exists in both soluble and insoluble forms; soluble fibronectin is secreted by cells and exits in cell media or body fluids, whereas insoluble fibronectin exists in tissues or the extracellular matrix of cultured cells [2]. The ability to control adsorption of fibronectin on tissue engineering scaffolds would therefore play a huge role in controlling cell attachment and survival in vivo. This can be achieved through surface functionalization of the scaffolds. The goal of these studies is to use molecular dynamics (MD) simulations to mechanistically understand how fibronectin adsorption is enhanced by surface functionalization of submicron scaffolds.

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Modugno, Francesca Di, Sheila Spada, Belinda Palermo, Paolo Visca, Pierluigi Iapicca, Anna Di Carlo, Barbara Antoniani, et al. "Abstract 5224: hMENA isoforms impact NSCLC patient outcome through fibronectin/β1 integrin axis." 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.am2018-5224.

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Huang, Chi-Ruei, Chung-Ta Lee, Kwang-Yu Chang, Wen-Chang Chang, and Ben-Kuen Chen. "Abstract 523: Decrease of ARNT promotes cancer metastasis by activating the fibronectin/integrin β1/FAK axis." 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.am2015-523.

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Lee, Shinhee, Huiwen Cheng, and Shiyong Wu. "Abstract 4344: Ionizing radiation induces adhesion of breast cancer cells to fibronectin through upregulation of integrin alpha5beta1." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-4344.

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Curnis, Flavio, Angela Sacchi, Renato Longhi, and Angelo Corti. "Abstract 426: The molecular microenvironment critically affects the formation of isoDGR-dependent integrin binding sites in fibronectin." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-426.

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Reports on the topic "Fibronectin; Integrins"

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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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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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