Purification and complete primary structures of the heparin-, cell-, and DNA-binding domains of bovine plasma fibronectin

Skorstengaard, Karna; Jensen, Margit S.; Petersen, Torben E.; Magnusson, Staffan

doi:10.1111/j.1432-1033.1986.tb09353.x

Cited by 53 publications

(24 citation statements)

References 47 publications

(30 reference statements)

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“…The N‐terminal sequence of the 140 kDa fragment (VATSESVTE) was identical to the first nine residues of the 2 FnIII repeat of bovine fibronectin. The N‐terminal sequences of the 30 and 40 kDa fragments were identical (AVTTIPAP) and corresponded to the first eight residues of the 12 FnIII repeat module of the bovine fibronectin primary amino acid sequence (McDonagh et al ., 1981; Vibe‐Pedersen et al ., 1982; Skorstengaard et al ., 1982; 1984; 1986a, b; Petersen et al ., 1983).…”

Section: Resultsmentioning

confidence: 99%

The ShdA adhesin binds to the cationic cradle of the fibronectin¹³FnIII repeat module: evidence for molecular mimicry of heparin binding

Kingsley¹,

Keestra

Zoete

et al. 2004

Molecular Microbiology

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SummaryIntroduction of Salmonella enterica serotype Typhimurium into food products results from its ability to persist in the intestine of healthy livestock by mechanisms that are poorly understood. The non-fimbrial adhesin ShdA is a fibronectin binding protein required for persistent intestinal carriage of S. Typhimurium. We further investigated the molecular mechanism of ShdA-mediated intestinal persistence by determining the binding-site of this receptor in fibronectin. Analysis of ShdA binding to fibronectin proteolytic fragments and to recombinant fibronectin fusion proteins identified the

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Section: Resultsmentioning

confidence: 99%

The ShdA adhesin binds to the cationic cradle of the fibronectin¹³FnIII repeat module: evidence for molecular mimicry of heparin binding

Kingsley¹,

Keestra

Zoete

et al. 2004

Molecular Microbiology

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“…Early studies have indicated that this segment contains a weak heparin and DNA binding site(s) (named Hep III domain), but its physiological relevance is unclear (13)(14)(15)(16). A recent study has proposed that the region comprising Fn repeats III1-7 may play a regulatory role in the process of matrix formation (26).…”

Section: Discussionmentioning

confidence: 99%

Fibronectin Type III5 Repeat Contains a Novel Cell Adhesion Sequence, KLDAPT, Which Binds Activated α4β1 and α4β7 Integrins

Moyano¹,

Bárbara²,

Domínguez‐Jiménez³

et al. 1997

Journal of Biological Chemistry

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The region of fibronectin encompassing type III repeats 4 -6 contains a low affinity heparin binding domain, but its physiological significance is not clear. We have studied whether this domain is able to interact Fibronectin (Fn) 1 is an extracellular matrix and plasma protein composed of structural domains that contain binding sites for other macromolecules (fibrin, heparin/proteoglycans, collagen), as well as for cells (reviewed in Hynes (1)). The NH 2 -terminal heparin binding domain or Hep I (see Fig. 1) also interacts with cell surfaces by binding to uncharacterized molecules and is mainly involved in formation of Fn matrices (1, 2). The Hep II domain displays the highest avidity for heparin and contains specific sequences which bind proteoglycans and/or the ␣4␤1 integrin at the cell surface and induce cell adhesion (3-5). One of these sites is H1, which is a ligand for ␣4␤1 in melanoma (6) and lymphoid cells (7). Two other sequences, CS-1 and CS-5, located within the IIICS segment (outside the Hep II domain) are also ligands for ␣4␤1 (8 -11) and bind with different affinities (12). These previous studies have established that ␣4␤1 may bind several sequences in the COOHterminal region of Fn and that these interactions are particularly important in lymphoid cells, where ␣4␤1 is highly expressed.The central Hep III domain is less well studied because it binds heparin only at low salt concentration, and the physiological significance of this interaction is unclear. Using DNA affinity chromatography, we and others previously isolated proteolytic fragments from this region of Fn, which displayed low affinity binding to heparin. These include a 14-kDa fragment corresponding to FN-III1 repeat (13) and two fragments of 18 -20 kDa (FN-III4-1/2 5 repeats) (14) and 30 kDa (FN-III4 -6 repeats) (15) from human and bovine plasma Fn, respectively. We also previously reported that an 80-kDa tryptic fragment (FN-III4-1/2 FN-III11) binds heparin with low avidity (16). It is not known whether this heparin binding domain also interacts with cells.The present study was undertaken to further characterize the properties of the Hep III domain of Fn. To this effect, we have prepared recombinant fragments encompassing type III homology repeats from this region and have studied their cell binding activities. We show that a fragment containing the FN-III5 repeat mediates adhesion of T and B lymphoid cells efficiently. Furthermore, we have identified a novel 6-amino acid-sequence as the active site in FN-III5, and we show that activated ␣4␤1 and ␣4␤7 integrins are receptors for this sequence and the FN-III5 fragment. These results therefore establish a novel function for the Hep III Fn domain.

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“…1 is a multidomain glycoprotein found in the plasma as an ϳ450-kDa disulfide-linked dimer and in the extracellular matrix (ECM), in the form of larger multimers (1,2). Structural variants of Fn arise from a single gene by alternative mRNA splicing and post-translational modification (3,4).…”

Section: Fibronectin (Fn)mentioning

confidence: 99%

The Low Density Lipoprotein Receptor-related Protein Mediates Fibronectin Catabolism and Inhibits Fibronectin Accumulation on Cell Surfaces

Salicioni

Mizelle

Loukinova

et al. 2002

Journal of Biological Chemistry

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Purification and complete primary structures of the heparin-, cell-, and DNA-binding domains of bovine plasma fibronectin

Cited by 53 publications

References 47 publications

The ShdA adhesin binds to the cationic cradle of the fibronectin¹³FnIII repeat module: evidence for molecular mimicry of heparin binding

The ShdA adhesin binds to the cationic cradle of the fibronectin¹³FnIII repeat module: evidence for molecular mimicry of heparin binding

Fibronectin Type III5 Repeat Contains a Novel Cell Adhesion Sequence, KLDAPT, Which Binds Activated α4β1 and α4β7 Integrins

The Low Density Lipoprotein Receptor-related Protein Mediates Fibronectin Catabolism and Inhibits Fibronectin Accumulation on Cell Surfaces

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Purification and complete primary structures of the heparin-, cell-, and DNA-binding domains of bovine plasma fibronectin

Cited by 53 publications

References 47 publications

The ShdA adhesin binds to the cationic cradle of the fibronectin13FnIII repeat module: evidence for molecular mimicry of heparin binding

The ShdA adhesin binds to the cationic cradle of the fibronectin13FnIII repeat module: evidence for molecular mimicry of heparin binding

Fibronectin Type III5 Repeat Contains a Novel Cell Adhesion Sequence, KLDAPT, Which Binds Activated α4β1 and α4β7 Integrins

The Low Density Lipoprotein Receptor-related Protein Mediates Fibronectin Catabolism and Inhibits Fibronectin Accumulation on Cell Surfaces

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The ShdA adhesin binds to the cationic cradle of the fibronectin¹³FnIII repeat module: evidence for molecular mimicry of heparin binding

The ShdA adhesin binds to the cationic cradle of the fibronectin¹³FnIII repeat module: evidence for molecular mimicry of heparin binding