Fibronectin Interactions
Published by Anonymous on 2007/9/29 (2834 reads)
1: J Investig Dermatol Symp Proc. 2006 Sep;11(1):73-8.
Modulation of cell-fibronectin matrix interactions during tissue repair.
Midwood KS, Mao Y, Hsia HC, Valenick LV, Schwarzbauer JE.
Department of Molecular Biology, Princeton University, Princeton, New Jersey 08544-1014, USA.
Environmental signals from the extracellular matrix (ECM) are transmitted by cell surface receptors that connect to the actin cytoskeleton and to multiple intracellular signaling pathways. To dissect how the ECM regulates cell functions, we are using a three-dimensional (3D) fibrin-fibronectin matrix, resembling the wound provisional matrix. Fibroblasts adhere to fibronectin in this matrix via concomitant engagement of alpha 5 beta 1 integrin receptors and syndecan-4, a transmembrane proteoglycan. An adhesive phenotype is developed with actin stress fibers and activation of focal adhesion kinase (FAK) and Rho GTPase. Lack of syndecan-4 engagement, as occurs in the presence of the ECM protein tenascin-C, promotes a motile phenotype; FAK and Rho signaling are downregulated and filopodia are extended. Fibronectin matrices have distinct effects on two other receptors: alpha 4 beta 1 and beta v beta 3 integrins. Although alpha 4 beta 1 does not naturally support strong cell interactions with a fibrin-fibronectin matrix, binding is dramatically enhanced by proteolytic cleavage of fibronectin. Conversely, activity of alpha v beta 3 is stimulated by multimeric fibronectin fibrils showing that the organization of fibronectin differentially affects integrin functions. Thus, deposition of additional ECM components, expression of co-receptors for ECM, cleavage of adhesive proteins, and the architecture of the ECM microenvironment are different mechanisms for modulating cell responses to fibronectin matrix.
Publication Types:
Research Support, N.I.H., Extramural
Review
PMID: 17069013 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
2: Acta Haematol. 2003;109(1):1-10.
Substance p-fibronectin-cytokine interactions in myeloproliferative disorders with bone marrow fibrosis.
Rameshwar P, Oh HS, Yook C, Gascon P, Chang VT.
Department of Medicine, UMDNJ New Jersey Medical School, Newark, N.J. 07103, USA. rameshwa@umdnj.edu
Bone marrow (BM) fibrosis could occur secondarily to several clinical disorders: hematological and nonhematological. Clinical presentation of fibrosis could occur in myeloproliferative diseases, lymphoma, myelodysplastic syndrome and myeloma. The pathophysiology underlying BM fibrosis remains unclear despite intensive study, with a corresponding lack of specific therapy. This review discusses new insights in the role of substance P, cytokines and fibronectin in the development of BM fibrosis. Substance P is a neuropeptide that possesses pleiotropic properties, e.g. neurotransmission and immune/hematopoietic modulation and is linked to BM fibrosis. Cytokines and growth factors, in particular those associated with fibrogenic properties, e.g. TGF-beta, IL-1 and platelet-derived growth factor, are linked to BM fibrosis. Extracellular matrix proteins are increased in patients with BM fibrosis. Fibronectin in the sera of patients with BM fibrosis is complexed to substance P. Fibronectin appears to protect substance P from degradation by endogenous peptidases. This review describes the preliminary findings on the colocalization of substance P and fibronectin in the BM of patients with fibrosis. These data are reviewed in the context of published reports with particular focus on the relevant cytokines. A more detailed understanding of intra- and intercellular mechanisms in BM fibrosis may lead to effective therapy. Copyright 2003 S. Karger AG, Basel
Publication Types:
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 12486316 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
3: Parasitol Int. 2002 Sep;51(3):285-92.
The complex fibronectin--Trichomonas vaginalis interactions and Trichomonosis.
Alderete JF, Benchimol M, Lehker MW, Crouch ML.
Department of Microbiology, University of Texas Health Science Center at San Antonio, MC 7758, 7703 Floyd Curl Dr, San Antonio, TX 78229-3900, USA. alderete@uthscsa.edu
Trichomonosis is the vaginitis caused by Trichomonas vaginalis. This sexually transmitted agent achieves successful host parasitism through various means including: (1). acquisition of nutrients through specific receptors; (2). recognition and binding to mucin followed by cytoadherence mediated by adhesins that resemble metabolic enzymes; (3). evasion of immune responses through (i). masking of organisms by host proteins, (ii). shedding of trichomonad proteins into the secretions and (iii). secretions of cysteine proteinases that degrade all immunoglobulin subclasses and complement; (4). alternating surface expression of at least two antigen repertoires; and (5) alternate and coordinate expression of virulence genes in response to host environmental factors. The fact that the parasite survives long term in the varying and adverse environment of the vagina attests to the highly evolved nature of this protist. An understanding of the non-self-limiting nature of this infection may come from recent findings illustrating the complexity of Trichomonas vaginalis-fibronectin (FN) interactions. The parasite readily attaches to surfaces with immobilized FN and binds to FN in a highly specific receptor-mediated fashion. The amount and affinity of bound FN by live organisms is influenced by concentrations in medium of both iron and calcium. De novo protein synthesis is required for optimal FN acquisition in the presence of calcium. Furthermore, the parasites bind with differing affinities to the N-terminal domain (NTD), the cell-binding domain (CBD) and the gelatin-binding domain (GBD) of FN. Iron modulates binding of NTD similar to that of FN. This minireview summarizes recent findings on the T. vaginalis-FN associations.
Publication Types:
Research Support, U.S. Gov't, Non-P.H.S.
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 12243782 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
4: Ann N Y Acad Sci. 1999 Apr 30;872:109-13; discussion 113-4.
Retroviral-fibronectin interactions in transduction of mammalian cells.
Williams DA.
Section of Pediatric Hematology/Oncology, Herman B Wells Center for Pediatric Research, Riley Hospital for Children, Howard Hughes Medical Institute, Indiana University School of Medicine, Indianapolis 46202, USA. dwilliam@iupui.edu
Hematopoiesis occurs in a complex environment in the medullary cavity in close proximity to stromal cells, fibroblasts, endothelial cells and matrix molecules. Hematopoietic cell interactions in this environment appear to involve both integrin and proteoglycan-mediated cell-cell and cell-matrix interactions. Genetic transduction of hematopoietic stem cells via retroviral vectors has been hampered by low efficiency of gene transfer. Recently, hematopoietic stem cell adhesion to the extracellular matrix molecule fibronectin has been shown to increase transduction of these target cells using retrovirus vectors. The mechanism of increased transduction appears to involve colocalization of virus particles and target cells. These data are reviewed in this paper.
Publication Types:
Review
PMID: 10372115 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
5: Front Biosci. 1997 Mar 1;2:d126-46.
Fibronectin-integrin interactions.
Johansson S, Svineng G, Wennerberg K, Armulik A, Lohikangas L.
Department of Medical and Physiological Chemistry, The Biomedical Center, Box 575, S-751 23 Uppsala, Sweden. staffan.johansson@bmc.uu.se
Fibronectin is recognized by at least ten cell surface receptors of the integrin family. Most cell types in the body can adhere to fibronectin via these receptors, and thereby fibronectin becomes involved in many different biological processes. Three areas related to fibronectin and its receptors which have developed rapidly during the last few years are summarized in this review: the mechanisms of interactions between fibronectin and integrins, fibronectin polymerization, and in vivo functions of the proteins as studied by gene targeting in mice.
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 9159220 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
6: J Investig Med. 1996 Oct;44(8):429-41.
Fibronectin and integrins interactions.
Mohri H.
First Department of Internal Medicine, Yokohama City University School of Medicine, Japan.
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 8952223 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
7: Cell Adhes Commun. 1994 Jul;2(3):269-73.
Functional interactions of fibronectin and TNF alpha: a paradigm of physiological linkage between cytokines and extracellular matrix moieties.
Cahalon L, Hershkoviz R, Gilat D, Miller A, Akiyama SK, Yamada KM, Lider O.
Department Cell Biology, Weizmann Institute of Science, Rehovot, Israel.
Publication Types:
Review
PMID: 7827964 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
8: In Vivo. 1991 Sep-Oct;5(5):489-92.
Cellular interactions with fibronectin as a model for redundant binding of cells to other extracellular matrix proteins.
Argraves WS, Gehlsen KR.
American Red Cross, Biochemistry Laboratory, Rockville, Maryland 20855.
Perhaps the most studied property of fibronectin (Fn) is its ability to bind to cells. Interestingly, there are multiple mechanisms by which cells can bind Fn involving as many as ten different cell surface molecules and perhaps six distinct sites within Fn. This apparent redundant binding system is not only restricted to Fn since cells bind other extracellular matrix proteins such as laminin, vitronectin and fibrinogen in a similar manner. The many binding interactions between cells and Fn may serve as a model for understanding redundant binding between cells and other matrix proteins.
Publication Types:
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 1768799 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
9: Zentralbl Bakteriol. 1990 Dec;274(3):342-9.
Fibronectin-staphylococcal interactions in endovascular infections.
Proctor RA.
Department of Medical Microbiology and Immunology, University of Wisconsin, Madison 53706.
Fibronectin is a large molecular weight protein that is found coating the surfaces of sites where endovascular damage has occurred. These are also the sites most commonly infected by bacteremic strains of staphylococci. Epidemiologic studies show a correlation between expression of fibronectin receptors and development of invasive infections. In vitro studies using cultured cells, artificial matrices containing fibronectin, blood clots, natural inflammatory matrices, and anti-fibronectin antibodies implicate fibronectin as an important ligand for staphylococcal attachment to host tissues and prosthetic devices. In the rat endocarditis model, S. aureus strains that lack the fibronectin receptor due to site-directed mutagenesis were unable to colonize the traumatized heart valves. These data suggest that the fibronectin receptor on staphylococci is important in the pathogenesis of endovascular infections. Because the fibronectin receptor is widely expressed on pathogenic of staphylococci, a broadly protective vaccine against S. aureus might be possible.
Publication Types:
Review
PMID: 2090149 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
10: J Invest Dermatol. 1990 Jun;94(6 Suppl):7S-14S.
Fibronectin-cell interactions.
Couchman JR, Austria MR, Woods A.
Department of Cell Biology & Anatomy, University of Alabama, Birmingham 35294.
Fibronectins are widespread extracellular matrix and body fluid glycoproteins, capable of multiple interactions with cell surfaces and other matrix components. Their structure at a molecular level has been resolved, yet there are still many unanswered questions regarding their biologic activity in vivo. Much data suggests that fibronectins may promote extracellular matrix assembly, and cell adhesion to those matrices. However, one outstanding enigma is that fibronectins may, under different circumstances, promote both cell migration and anchorage. An analysis of the interaction of fibroblasts with proteolytically derived and purified domains of plasma fibronectin revealed that the type of adhesion and the correlated cytoskeletal organization depended on multiple interactions of fibronectin domains with the cell surface. Human dermal fibroblasts were capable of interacting with the integrin-binding domain and both heparin-binding domains of the plasma fibronectin molecule and their interactions determined the type of adhesion. The same principle was seen in a study of the ability of plasma fibronectin to promote basement membrane assembly in an endodermal cell line, PF-HR9. There also, interactions of both heparin- and integrin-binding domains combined to promote the deposition of a proteoglycan, laminin, and type IV collagen-containing basement membrane matrix. The underlying conclusion from our studies is, therefore, that fibronectins may, through their different isotypes, multiple receptors, and varying interaction of one or more domains with those receptors, result in a spectrum of responses in different cell types. The molecular details of this array of biologic activities is not resolved but is the target of much current research.
Publication Types:
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 2191056 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
11: Rev Infect Dis. 1987 Jul-Aug;9 Suppl 4:S351-9.
Interactions of fibronectin with streptococci: the role of fibronectin as a receptor for Streptococcus pyogenes.
Simpson WA, Courtney HS, Ofek I.
Veterans Administration Medical Center, Memphis, Tennessee 38104.
Current evidence suggests that lipoteichoic acid (LTA) on the surface of Streptococcus pyogenes is centrally involved in the adherence of these bacteria to the oral mucosa. The major receptor on the surface of buccal mucosal cells for S. pyogenes is fibronectin. Fibronectin is a complex glycoprotein found in blood, extracellular matrices, and saliva. Many species of streptococci bind to fibronectin, although the characteristics of these interactions are different. Furthermore, whereas LTA is an efficient inhibitor of the binding of fibronectin to group A streptococci, it has little ability to inhibit the binding of fibronectin to Streptococcus pneumoniae or Staphylococcus aureus. Studies conducted with fibronectin show that different bacteria bind to different sites. The ability of various bacteria to interact with different domains on the fibronectin molecule may play an important role in bacterial adherence and tissue tropism.
Publication Types:
Research Support, U.S. Gov't, Non-P.H.S.
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 3326132 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
12: Rev Infect Dis. 1987 Jul-Aug;9 Suppl 4:S322-34.
Fibronectin-cell surface interactions.
McKeown-Longo PJ.
Department of Biological Sciences, State University of New York, Albany.
Fibronectins are a group of closely related proteins that are found in body fluids and tissue extracellular matrices. Fibronectins play important roles in the maintenance of hemostasis and in the organization of developing tissues. The interaction of cells with fibronectin probably involves specific cell-surface molecules. Two distinct receptors for fibronectin have been postulated. One receptor, a 140-kilodalton complex, has been identified in a variety of cell types and is believed to mediate the attachment of cells to fibronectin-coated substrata. The existence of a second receptor has been proposed but it has not been identified. This receptor may function in the assembly of soluble fibronectin into the extracellular matrix. In this paper some of the recent developments in the identification and characterization of fibronectin-binding molecules on the surfaces of eukaryotic cells are outlined.
Publication Types:
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 2964076 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
13: Vutr Boles. 1987;26(5):12-5.
[Fibronectin--its clinical importance, chemical structure and biological interactions]
[Article in Bulgarian]
Ivanov V, Chernev K, Shipkov T.
Publication Types:
Review
PMID: 3324485 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
14: Prog Clin Biol Res. 1986;226:127-39.
Interactions of migrating neural crest cells with fibronectin.
Duband JL, Rocher S, Yamada KM, Thiery JP.
Publication Types:
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 2949329 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
15: C R Seances Soc Biol Fil. 1986;180(2):142-50.
[Fibronectin and its role in cell-matrix interactions]
[Article in French]
Labat-Robert J.
Publication Types:
Review
PMID: 2946363 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
16: Prog Clin Biol Res. 1984;151:1-15.
Fibronectin and interactions at the cell surface.
Yamada KM, Hasegawa T, Hasegawa E, Kennedy DW, Hirano H, Hayashi M, Akiyama SK, Olden K.
Publication Types:
Comparative Study
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 6382271 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
17: Med Biol. 1983;61(6):283-95.
Fibronectin: multiple interactions assigned to structural domains.
Vartio T.
Characteristic features of fibronectin are its various molecular and biological interactions and a wide distribution in vivo. Structural studies of the protein have indicated that the functions correspond to specific interactive domains in the molecule and have revealed unique, internally homologous sequences in the primary structure. Fibronectin is easily degraded by proteinases and many of its biological effects are shared by the proteolytic fragments which also seem to have effects of their own.
Publication Types:
Review
PMID: 6374309 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
18: Cesk Fysiol. 1981;30(5):397-406.
[Fibronectin and its role in cell interactions with extracellular matrices]
[Article in Czech]
Deyl Z, Svojtková E.
Publication Types:
Review
PMID: 7028281 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
19: Experientia. 1980 May 15;36(5):505-7.
Fibroblast cell-substratum interactions: role of cold insoluble globulin (plasma fibronectin).
Grinnel F.
Publication Types:
Review
PMID: 6991273 [PubMed - indexed for MEDLINE]
Modulation of cell-fibronectin matrix interactions during tissue repair.
Midwood KS, Mao Y, Hsia HC, Valenick LV, Schwarzbauer JE.
Department of Molecular Biology, Princeton University, Princeton, New Jersey 08544-1014, USA.
Environmental signals from the extracellular matrix (ECM) are transmitted by cell surface receptors that connect to the actin cytoskeleton and to multiple intracellular signaling pathways. To dissect how the ECM regulates cell functions, we are using a three-dimensional (3D) fibrin-fibronectin matrix, resembling the wound provisional matrix. Fibroblasts adhere to fibronectin in this matrix via concomitant engagement of alpha 5 beta 1 integrin receptors and syndecan-4, a transmembrane proteoglycan. An adhesive phenotype is developed with actin stress fibers and activation of focal adhesion kinase (FAK) and Rho GTPase. Lack of syndecan-4 engagement, as occurs in the presence of the ECM protein tenascin-C, promotes a motile phenotype; FAK and Rho signaling are downregulated and filopodia are extended. Fibronectin matrices have distinct effects on two other receptors: alpha 4 beta 1 and beta v beta 3 integrins. Although alpha 4 beta 1 does not naturally support strong cell interactions with a fibrin-fibronectin matrix, binding is dramatically enhanced by proteolytic cleavage of fibronectin. Conversely, activity of alpha v beta 3 is stimulated by multimeric fibronectin fibrils showing that the organization of fibronectin differentially affects integrin functions. Thus, deposition of additional ECM components, expression of co-receptors for ECM, cleavage of adhesive proteins, and the architecture of the ECM microenvironment are different mechanisms for modulating cell responses to fibronectin matrix.
Publication Types:
Research Support, N.I.H., Extramural
Review
PMID: 17069013 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
2: Acta Haematol. 2003;109(1):1-10.
Substance p-fibronectin-cytokine interactions in myeloproliferative disorders with bone marrow fibrosis.
Rameshwar P, Oh HS, Yook C, Gascon P, Chang VT.
Department of Medicine, UMDNJ New Jersey Medical School, Newark, N.J. 07103, USA. rameshwa@umdnj.edu
Bone marrow (BM) fibrosis could occur secondarily to several clinical disorders: hematological and nonhematological. Clinical presentation of fibrosis could occur in myeloproliferative diseases, lymphoma, myelodysplastic syndrome and myeloma. The pathophysiology underlying BM fibrosis remains unclear despite intensive study, with a corresponding lack of specific therapy. This review discusses new insights in the role of substance P, cytokines and fibronectin in the development of BM fibrosis. Substance P is a neuropeptide that possesses pleiotropic properties, e.g. neurotransmission and immune/hematopoietic modulation and is linked to BM fibrosis. Cytokines and growth factors, in particular those associated with fibrogenic properties, e.g. TGF-beta, IL-1 and platelet-derived growth factor, are linked to BM fibrosis. Extracellular matrix proteins are increased in patients with BM fibrosis. Fibronectin in the sera of patients with BM fibrosis is complexed to substance P. Fibronectin appears to protect substance P from degradation by endogenous peptidases. This review describes the preliminary findings on the colocalization of substance P and fibronectin in the BM of patients with fibrosis. These data are reviewed in the context of published reports with particular focus on the relevant cytokines. A more detailed understanding of intra- and intercellular mechanisms in BM fibrosis may lead to effective therapy. Copyright 2003 S. Karger AG, Basel
Publication Types:
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 12486316 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
3: Parasitol Int. 2002 Sep;51(3):285-92.
The complex fibronectin--Trichomonas vaginalis interactions and Trichomonosis.
Alderete JF, Benchimol M, Lehker MW, Crouch ML.
Department of Microbiology, University of Texas Health Science Center at San Antonio, MC 7758, 7703 Floyd Curl Dr, San Antonio, TX 78229-3900, USA. alderete@uthscsa.edu
Trichomonosis is the vaginitis caused by Trichomonas vaginalis. This sexually transmitted agent achieves successful host parasitism through various means including: (1). acquisition of nutrients through specific receptors; (2). recognition and binding to mucin followed by cytoadherence mediated by adhesins that resemble metabolic enzymes; (3). evasion of immune responses through (i). masking of organisms by host proteins, (ii). shedding of trichomonad proteins into the secretions and (iii). secretions of cysteine proteinases that degrade all immunoglobulin subclasses and complement; (4). alternating surface expression of at least two antigen repertoires; and (5) alternate and coordinate expression of virulence genes in response to host environmental factors. The fact that the parasite survives long term in the varying and adverse environment of the vagina attests to the highly evolved nature of this protist. An understanding of the non-self-limiting nature of this infection may come from recent findings illustrating the complexity of Trichomonas vaginalis-fibronectin (FN) interactions. The parasite readily attaches to surfaces with immobilized FN and binds to FN in a highly specific receptor-mediated fashion. The amount and affinity of bound FN by live organisms is influenced by concentrations in medium of both iron and calcium. De novo protein synthesis is required for optimal FN acquisition in the presence of calcium. Furthermore, the parasites bind with differing affinities to the N-terminal domain (NTD), the cell-binding domain (CBD) and the gelatin-binding domain (GBD) of FN. Iron modulates binding of NTD similar to that of FN. This minireview summarizes recent findings on the T. vaginalis-FN associations.
Publication Types:
Research Support, U.S. Gov't, Non-P.H.S.
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 12243782 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
4: Ann N Y Acad Sci. 1999 Apr 30;872:109-13; discussion 113-4.
Retroviral-fibronectin interactions in transduction of mammalian cells.
Williams DA.
Section of Pediatric Hematology/Oncology, Herman B Wells Center for Pediatric Research, Riley Hospital for Children, Howard Hughes Medical Institute, Indiana University School of Medicine, Indianapolis 46202, USA. dwilliam@iupui.edu
Hematopoiesis occurs in a complex environment in the medullary cavity in close proximity to stromal cells, fibroblasts, endothelial cells and matrix molecules. Hematopoietic cell interactions in this environment appear to involve both integrin and proteoglycan-mediated cell-cell and cell-matrix interactions. Genetic transduction of hematopoietic stem cells via retroviral vectors has been hampered by low efficiency of gene transfer. Recently, hematopoietic stem cell adhesion to the extracellular matrix molecule fibronectin has been shown to increase transduction of these target cells using retrovirus vectors. The mechanism of increased transduction appears to involve colocalization of virus particles and target cells. These data are reviewed in this paper.
Publication Types:
Review
PMID: 10372115 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
5: Front Biosci. 1997 Mar 1;2:d126-46.
Fibronectin-integrin interactions.
Johansson S, Svineng G, Wennerberg K, Armulik A, Lohikangas L.
Department of Medical and Physiological Chemistry, The Biomedical Center, Box 575, S-751 23 Uppsala, Sweden. staffan.johansson@bmc.uu.se
Fibronectin is recognized by at least ten cell surface receptors of the integrin family. Most cell types in the body can adhere to fibronectin via these receptors, and thereby fibronectin becomes involved in many different biological processes. Three areas related to fibronectin and its receptors which have developed rapidly during the last few years are summarized in this review: the mechanisms of interactions between fibronectin and integrins, fibronectin polymerization, and in vivo functions of the proteins as studied by gene targeting in mice.
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 9159220 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
6: J Investig Med. 1996 Oct;44(8):429-41.
Fibronectin and integrins interactions.
Mohri H.
First Department of Internal Medicine, Yokohama City University School of Medicine, Japan.
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 8952223 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
7: Cell Adhes Commun. 1994 Jul;2(3):269-73.
Functional interactions of fibronectin and TNF alpha: a paradigm of physiological linkage between cytokines and extracellular matrix moieties.
Cahalon L, Hershkoviz R, Gilat D, Miller A, Akiyama SK, Yamada KM, Lider O.
Department Cell Biology, Weizmann Institute of Science, Rehovot, Israel.
Publication Types:
Review
PMID: 7827964 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
8: In Vivo. 1991 Sep-Oct;5(5):489-92.
Cellular interactions with fibronectin as a model for redundant binding of cells to other extracellular matrix proteins.
Argraves WS, Gehlsen KR.
American Red Cross, Biochemistry Laboratory, Rockville, Maryland 20855.
Perhaps the most studied property of fibronectin (Fn) is its ability to bind to cells. Interestingly, there are multiple mechanisms by which cells can bind Fn involving as many as ten different cell surface molecules and perhaps six distinct sites within Fn. This apparent redundant binding system is not only restricted to Fn since cells bind other extracellular matrix proteins such as laminin, vitronectin and fibrinogen in a similar manner. The many binding interactions between cells and Fn may serve as a model for understanding redundant binding between cells and other matrix proteins.
Publication Types:
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 1768799 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
9: Zentralbl Bakteriol. 1990 Dec;274(3):342-9.
Fibronectin-staphylococcal interactions in endovascular infections.
Proctor RA.
Department of Medical Microbiology and Immunology, University of Wisconsin, Madison 53706.
Fibronectin is a large molecular weight protein that is found coating the surfaces of sites where endovascular damage has occurred. These are also the sites most commonly infected by bacteremic strains of staphylococci. Epidemiologic studies show a correlation between expression of fibronectin receptors and development of invasive infections. In vitro studies using cultured cells, artificial matrices containing fibronectin, blood clots, natural inflammatory matrices, and anti-fibronectin antibodies implicate fibronectin as an important ligand for staphylococcal attachment to host tissues and prosthetic devices. In the rat endocarditis model, S. aureus strains that lack the fibronectin receptor due to site-directed mutagenesis were unable to colonize the traumatized heart valves. These data suggest that the fibronectin receptor on staphylococci is important in the pathogenesis of endovascular infections. Because the fibronectin receptor is widely expressed on pathogenic of staphylococci, a broadly protective vaccine against S. aureus might be possible.
Publication Types:
Review
PMID: 2090149 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
10: J Invest Dermatol. 1990 Jun;94(6 Suppl):7S-14S.
Fibronectin-cell interactions.
Couchman JR, Austria MR, Woods A.
Department of Cell Biology & Anatomy, University of Alabama, Birmingham 35294.
Fibronectins are widespread extracellular matrix and body fluid glycoproteins, capable of multiple interactions with cell surfaces and other matrix components. Their structure at a molecular level has been resolved, yet there are still many unanswered questions regarding their biologic activity in vivo. Much data suggests that fibronectins may promote extracellular matrix assembly, and cell adhesion to those matrices. However, one outstanding enigma is that fibronectins may, under different circumstances, promote both cell migration and anchorage. An analysis of the interaction of fibroblasts with proteolytically derived and purified domains of plasma fibronectin revealed that the type of adhesion and the correlated cytoskeletal organization depended on multiple interactions of fibronectin domains with the cell surface. Human dermal fibroblasts were capable of interacting with the integrin-binding domain and both heparin-binding domains of the plasma fibronectin molecule and their interactions determined the type of adhesion. The same principle was seen in a study of the ability of plasma fibronectin to promote basement membrane assembly in an endodermal cell line, PF-HR9. There also, interactions of both heparin- and integrin-binding domains combined to promote the deposition of a proteoglycan, laminin, and type IV collagen-containing basement membrane matrix. The underlying conclusion from our studies is, therefore, that fibronectins may, through their different isotypes, multiple receptors, and varying interaction of one or more domains with those receptors, result in a spectrum of responses in different cell types. The molecular details of this array of biologic activities is not resolved but is the target of much current research.
Publication Types:
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 2191056 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
11: Rev Infect Dis. 1987 Jul-Aug;9 Suppl 4:S351-9.
Interactions of fibronectin with streptococci: the role of fibronectin as a receptor for Streptococcus pyogenes.
Simpson WA, Courtney HS, Ofek I.
Veterans Administration Medical Center, Memphis, Tennessee 38104.
Current evidence suggests that lipoteichoic acid (LTA) on the surface of Streptococcus pyogenes is centrally involved in the adherence of these bacteria to the oral mucosa. The major receptor on the surface of buccal mucosal cells for S. pyogenes is fibronectin. Fibronectin is a complex glycoprotein found in blood, extracellular matrices, and saliva. Many species of streptococci bind to fibronectin, although the characteristics of these interactions are different. Furthermore, whereas LTA is an efficient inhibitor of the binding of fibronectin to group A streptococci, it has little ability to inhibit the binding of fibronectin to Streptococcus pneumoniae or Staphylococcus aureus. Studies conducted with fibronectin show that different bacteria bind to different sites. The ability of various bacteria to interact with different domains on the fibronectin molecule may play an important role in bacterial adherence and tissue tropism.
Publication Types:
Research Support, U.S. Gov't, Non-P.H.S.
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 3326132 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
12: Rev Infect Dis. 1987 Jul-Aug;9 Suppl 4:S322-34.
Fibronectin-cell surface interactions.
McKeown-Longo PJ.
Department of Biological Sciences, State University of New York, Albany.
Fibronectins are a group of closely related proteins that are found in body fluids and tissue extracellular matrices. Fibronectins play important roles in the maintenance of hemostasis and in the organization of developing tissues. The interaction of cells with fibronectin probably involves specific cell-surface molecules. Two distinct receptors for fibronectin have been postulated. One receptor, a 140-kilodalton complex, has been identified in a variety of cell types and is believed to mediate the attachment of cells to fibronectin-coated substrata. The existence of a second receptor has been proposed but it has not been identified. This receptor may function in the assembly of soluble fibronectin into the extracellular matrix. In this paper some of the recent developments in the identification and characterization of fibronectin-binding molecules on the surfaces of eukaryotic cells are outlined.
Publication Types:
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 2964076 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
13: Vutr Boles. 1987;26(5):12-5.
[Fibronectin--its clinical importance, chemical structure and biological interactions]
[Article in Bulgarian]
Ivanov V, Chernev K, Shipkov T.
Publication Types:
Review
PMID: 3324485 [PubMed - indexed for MEDLINE]
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14: Prog Clin Biol Res. 1986;226:127-39.
Interactions of migrating neural crest cells with fibronectin.
Duband JL, Rocher S, Yamada KM, Thiery JP.
Publication Types:
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 2949329 [PubMed - indexed for MEDLINE]
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15: C R Seances Soc Biol Fil. 1986;180(2):142-50.
[Fibronectin and its role in cell-matrix interactions]
[Article in French]
Labat-Robert J.
Publication Types:
Review
PMID: 2946363 [PubMed - indexed for MEDLINE]
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16: Prog Clin Biol Res. 1984;151:1-15.
Fibronectin and interactions at the cell surface.
Yamada KM, Hasegawa T, Hasegawa E, Kennedy DW, Hirano H, Hayashi M, Akiyama SK, Olden K.
Publication Types:
Comparative Study
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 6382271 [PubMed - indexed for MEDLINE]
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17: Med Biol. 1983;61(6):283-95.
Fibronectin: multiple interactions assigned to structural domains.
Vartio T.
Characteristic features of fibronectin are its various molecular and biological interactions and a wide distribution in vivo. Structural studies of the protein have indicated that the functions correspond to specific interactive domains in the molecule and have revealed unique, internally homologous sequences in the primary structure. Fibronectin is easily degraded by proteinases and many of its biological effects are shared by the proteolytic fragments which also seem to have effects of their own.
Publication Types:
Review
PMID: 6374309 [PubMed - indexed for MEDLINE]
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18: Cesk Fysiol. 1981;30(5):397-406.
[Fibronectin and its role in cell interactions with extracellular matrices]
[Article in Czech]
Deyl Z, Svojtková E.
Publication Types:
Review
PMID: 7028281 [PubMed - indexed for MEDLINE]
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19: Experientia. 1980 May 15;36(5):505-7.
Fibroblast cell-substratum interactions: role of cold insoluble globulin (plasma fibronectin).
Grinnel F.
Publication Types:
Review
PMID: 6991273 [PubMed - indexed for MEDLINE]
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