[27] Arginine-glycine-aspartic acid adhesion receptors

Pytela, Robert; Pierschbacher, Michael D.; Argraves, Scott; Suzuki, Shintaro; Ruoslahti, Erkki

doi:10.1016/0076-6879(87)44196-7

Cited by 256 publications

(143 citation statements)

References 28 publications

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“…The adherence of the 110-75 fimbriae to solidphase intact FN or to the 30-kDa and 120-140-kDa fragments of FN was not inhibited by the tetrapeptides Arg-Gly-Asp-Ser (the cellattachment sequence of FN [6]) or Val-Ala-AlaPhe (a test control), both tested at 5 mM (not shown). This concentration of the Arg-Gly-AspSer peptide is enough to inhibit adhesion of normal rat kidney cells to immobilized intact FN [6].…”

Section: Resultsmentioning

confidence: 94%

“…This concentration of the Arg-Gly-AspSer peptide is enough to inhibit adhesion of normal rat kidney cells to immobilized intact FN [6].…”

Section: Resultsmentioning

confidence: 96%

“…P fimbriae are thought to increase the virulence of E. coli by mediating bacterial adherence to epithelial glycoconjugates, thus giving resistance to mechanical clearance by the flow of urine. The receptor structure recognized by Pfimbriated E. coli is the disaccharide moiety ot-DGal-(1-4)-~-D-Gal of the P-blood-group antigens [31. Fibronectin (FN) is a 450-kDa dimeric glycoprotein found in a soluble form in body fluids, such as blood plasma, and as an insoluble protein in the Correspondence address: B. Westerlund, University of Helsinki, Department of General Microbiology, Mannerheimintie 172, SF-00300, Helsinki, Finland extracellular matrix and in association with basement membranes [4][5][6]. One of the main biological functions of FN is to promote attachment and spreading of eukaryotic cells on different substrates.…”

Section: Introductionmentioning

confidence: 99%

“…FN is also important in wound healing and involved in clot stabilization. A characteristic of FN is its ability to interact with a wide variety of mammalian molecules and cells [4][5][6].…”

Section: Introductionmentioning

confidence: 99%

“…So far, many specific domains have been identified, including those binding to fibrin, heparin, collagen, gelatin, DNA and several bacterial species [5]. A specific cell-attachment domain containing the sequence Arg-Gly-Asp-Ser in FN is recognized by fibroblasts, platelets and other eukaryotic cells [5,6]. Kuusela [7] described the binding of 125I-labelled, soluble FN to Staphylococcus aureus.…”

Section: Introductionmentioning

confidence: 99%

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A novel lectin‐independent interaction of P fimbriae of Escherichia coli with immobilized fibronectin

et al. 1989

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Binding of P fimbriae of uropathogenic Escherichia coil to purified human plasma flbronectin and human placental type IV collagen was studied. In an enzyme immunoassay, purified P fimbriae bound strongly to immobilized intact fibronectin and to the aminoterminal 30-kDa fragment and the 120-140-kDa carboxyterminal fragments of fibronectin. Binding to the gelatin-binding 40-kDa fragment of fibronectin was considerably weaker. No binding to immobilized type IV collagen was seen. The interaction between P fimbriae and immobilized flbronectin was not inhibited by ,,-D-GaI-( 1-4)-fl-D-Gal-1-O-Me, a receptor analog of P funbriae. Moreover, a mutated P fimbria lacking the lectin activity behaved similarly in the adherence assays. Recombinant strains expressing the corresponding cloned fimbriae genes bound to immobilized fibronectin, but no binding to soluble ~'5I-labelled fibronectin was found. The results suggest that P fimbriae interact with immobilized fibronectin and that the binding mechanism does not involve the lectin activity of the flmbriae.

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Section: Resultsmentioning

confidence: 94%

“…This concentration of the Arg-Gly-AspSer peptide is enough to inhibit adhesion of normal rat kidney cells to immobilized intact FN [6].…”

Section: Resultsmentioning

confidence: 96%

Section: Introductionmentioning

confidence: 99%

“…FN is also important in wound healing and involved in clot stabilization. A characteristic of FN is its ability to interact with a wide variety of mammalian molecules and cells [4][5][6].…”

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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A novel lectin‐independent interaction of P fimbriae of Escherichia coli with immobilized fibronectin

et al. 1989

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Modulation of α5β1 and αVβ3 integrins on the cell surface during mitosis

et al. 1996

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One of the hallmarks of cells undergoing mitotic division is their rounded morphology and reduced adhesion to the substratum. We have studied and compared the attachment of interphase and mitotic cells to substrata coated with fibronectin and vitronectin. We have found that adhesion of mitotic cells, as compared to interphase cells, is significantly reduced to fibronectin, but is higher to vitronectin. These results correlate well with the expression of alpha 5 beta 1 and alpha V beta 3 integrins, the respective receptors for fibronectin and vitronectin, on the cell surface. Mitotic cells show higher levels of alpha V beta 3 and very low levels of alpha 5 beta 1 proteins on the cell surface as compared to interphase cells. This difference in the levels of these integrins also reflects in the total amounts of fibronectin and vitronectin present on the cell surface of these cells. We have further shown, by flow cytometry, that binding of vitronectin, or the synthetic peptide -GRGDSP-, causes an increase in the intracellular levels of Ca2+ in mitotic cells, but no change is seen in the interphase cells. Binding of fibronectin to either of these cells fails to elicit any response. One interesting feature of our results is that the levels of total, i.e., cytoplasmic plus membrane bound, alpha 5 beta 1 and alpha V beta 3 integrins of mitotic and interphase cells remain the same, thus implying an alteration in the distribution of integrin chains between the plasma membrane and the cytoplasm during the conversion of interphase cells into the mitotic phase.

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Divalent cations regulate the organization of integrins αvβ3 and αvβ5 on the cell surface

1996

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Extracellular divalent cations are important regulators of integrin ligand binding activity. In this study we evaluated how divalent cations affect the organization of integrins into focal adhesion sites. Integrins alpha v beta 3 and alpha v beta 5 were compared because they share a high degree of structural homology and because both integrins mediate cell adhesion to vitronectin. On MG-63 osteosarcoma cells, we found that both the extent and pattern of integrin organization was regulated by the type of extracellular divalent ion. Integrin alpha v beta 3 organized in focal contacts when Mn2+ or Mg2+ was present, but not in Ca2+. In contrast, alpha v beta 5 organized in focal contacts only when Ca2+ or Mg2+ was present. Integrin alpha v beta 5 clustered in a centrally located punctate field on the ventral surface of the cell in the presence of Mn2+. These observations reveal a previously unappreciated role for divalent ions in regulating the organization of integrins into focal adhesion sites.

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[27] Arginine-glycine-aspartic acid adhesion receptors

Cited by 256 publications

References 28 publications

A novel lectin‐independent interaction of P fimbriae of Escherichia coli with immobilized fibronectin

A novel lectin‐independent interaction of P fimbriae of Escherichia coli with immobilized fibronectin

Modulation of α5β1 and αVβ3 integrins on the cell surface during mitosis

Divalent cations regulate the organization of integrins αvβ3 and αvβ5 on the cell surface

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