Binding of von Willebrand Factor to Collagen Type III: Role of Specific Amino Acids in the Collagen Binding Domain of vWF and Effects of Neighboring Domains

Plas, R. Martijn van der; Gomes, Lucio; Marquart, J. Arnoud; Vink, Tom; Meijers, Joost C. M.; Groot, Philip G. de; Sixma, Jan J.; Huizinga, Eric G.

doi:10.1055/s-0037-1614163

Cited by 38 publications

(41 citation statements)

References 44 publications

(65 reference statements)

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“…5c,d), as calculated from curve fits according to a one-site binding model. Besides soluble collagen, PTMP1 also bound prefibrillized collagens 29 , which has also been shown for the human von Willebrand factor 28 . The isolated A1 and A2 domains both bound collagens in this test, but with much ARTICLE lower affinities than the wild-type protein or the DNDC mutant, which, in contrast to the SPR results, exhibited lower-binding affinity than the full-length protein in this assay.…”

Section: Resultssupporting

confidence: 55%

“…In static ELISA-like assays 28 , PTMP1 bound to a broad range of immobilized soluble heterologous collagens (type I, II, III, IV, V), as well as the collagen-resembling triple-helical peptide (PPG) 10 , with affinities in the sub-micromolar range (Fig. 5c,d), as calculated from curve fits according to a one-site binding model.…”

Section: Resultsmentioning

confidence: 99%

“…It has previously been hypothesized that PTMP1, like other VWA domain containing proteins, binds with and interconnects byssal collagens 9,11 . Due to the lack of available PreCol proteins, we analysed binding of heterologous collagens to PTMP1 and its isolated VWA domains using surface plasmon resonance spectroscopy (SPR) 13,27,28 , since all fibrous collagens show similar structural features. PTMP1 bound immobilized collagen type I with apparent high affinity in the sub-micromolar range as shown by the difference-sensorgram of the collagen-coated versus the reference cell (Fig.…”

Section: Resultsmentioning

confidence: 99%

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Structural and functional features of a collagen-binding matrix protein from the mussel byssus

et al. 2014

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Blue mussels adhere to surfaces by the byssus, a holdfast structure composed of individual threads representing a collagen fibre reinforced composite. Here, we present the crystal structure and function of one of its matrix proteins, the proximal thread matrix protein 1, which is present in the proximal section of the byssus. The structure reveals two von Willebrand factor type A domains linked by a two-b-stranded linker yielding a novel structural arrangement. In vitro, the protein binds heterologous collagens with high affinity and affects collagen assembly, morphology and arrangement of its fibrils. By providing charged surface clusters as well as insufficiently coordinated metal ions, the proximal thread matrix protein 1 might interconnect other byssal proteins and thereby contribute to the integrity of the byssal threads in vivo. Moreover, the protein could be used for adjusting the mechanical properties of collagen materials, a function likely important in the natural byssus.

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Section: Resultssupporting

confidence: 55%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

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Structural and functional features of a collagen-binding matrix protein from the mussel byssus

et al. 2014

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“…Binding of monoclonal antibody RU5 (22) to VWF was analyzed as described previously (23), with some modifications. Microtiter plate wells (Costar, Cambridge, MA) were coated with a polyclonal antibody directed against the DЈ and D3 domains of VWF (22) diluted to 2.5 g/ml with 50 mM carbonate buffer (pH 9.6).…”

Section: Methodsmentioning

confidence: 99%

“…The A3 domain of VWF does not contain a functional MIDAS motif, and binding of A3 to collagen is cation-independent (20, 21). The involvement of the top face of A3 in collagen binding has been excluded by mutagenesis studies (13,22). Recently, we showed that His 1023 , located close to the edge of the front and bottom face of A3, is critical for binding of VWF to collagen (23).…”

mentioning

confidence: 99%

Mapping the Collagen-binding Site in the von Willebrand Factor-A3 Domain

Romijn

Westein

Bouma

et al. 2003

Journal of Biological Chemistry

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The multimeric glycoprotein von Willebrand factor (VWF) mediates platelet adhesion to collagen at sites of vascular damage. The binding site for collagen types I and III is located in the VWF-A3 domain. Recently, we showed that His 1023 , located near the edge between the "front" and "bottom" faces of A3, is critical for collagen binding (Romijn, R. A., Bouma, B., Wuyster, W., Gros, P., Kroon, J., Sixma, J. J., and Huizinga, E. G. (2001) reduced binding affinity about 10-fold. Together, these residues define a flat and rather hydrophobic collagenbinding site located at the front face of the A3 domain. The collagen-binding site of VWF-A3 is distinctly different from that of the homologous integrin ␣ 2 I domain, which has a hydrophilic binding site located at the top face of the domain. Based on the surface characteristics of the collagen-binding site of A3, we propose that it interacts with collagen sequences containing positively charged and hydrophobic residues. Docking of a collagen triple helix on the binding site suggests a range of possible engagements and predicts that at most eight consecutive residues in a collagen triple helix interact with A3.Under conditions of high shear stress, platelet adhesion to collagen at sites of vascular injury is initiated by the interaction of platelet receptor glycoprotein (Gp) 1 Ib-IX-V with collagen-bound von Willebrand factor (VWF) (1). Transient interactions between VWF and GpIb-IX-V mediate platelet rolling, which slows down the platelet and allows other platelet receptors such as integrin ␣ 2 ␤ 1 (2) and GpVI to bind to collagen (2-4). These interactions result in firm adhesion and activation of platelets at the site of vascular injury.VWF is a multimeric glycoprotein consisting of ϳ270-kDa monomers that are linked by disulfide bonds (5). The affinity of VWF for collagen depends on multimer size (6). The binding site for fibrillar collagens type I and III is located in the VWF-A3 domain (7), whereas collagen type VI has been shown to bind to the VWF-A1 domain (8, 9). The latter domain also contains the binding site for GpIb␣ of the GpIb-IX-V complex (10, 11).VWF A-type domains and homologous integrin I domains adopt a so-called dinucleotide-binding fold, or Rossman fold, composed of a central ␤-sheet flanked on both sides by amphipathic ␣-helices (12-15). Binding of the I domains of integrins ␣ 1 ␤ 1 , ␣ 2 ␤ 1 , ␣ 10 ␤ 1 , and ␣ 11 ␤ 1 to collagen involves a divalent cation (16, 17) located in the metal ion-dependent adhesion site (MIDAS) motif, and amino acid residues at the top face of the domain (18,19). Binding of the I domain of integrin ␣ 2 ␤ 1 to collagen induces a major displacement of its carboxyl-terminal ␣-helix that is thought to be critical for integrin signaling (18). The A3 domain of VWF does not contain a functional MIDAS motif, and binding of A3 to collagen is cation-independent (20, 21). The involvement of the top face of A3 in collagen binding has been excluded by mutagenesis studies (13,22). Recently, we showed that His 1023 , located close to th...

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Prolonged bleeding time and lupus anticoagulant: A second paradox in the antiphospholipid syndrome

Urbanus

Laat

Groot

et al. 2004

Arthritis & Rheumatism

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Objective. Systemic lupus erythematosus and antiphospholipid syndrome (APS) often appear concomitantly. Lupus nephritis and antiphospholipid antibodyrelated ischemic nephropathy cannot be distinguished clinically, although their etiology and treatment differ greatly. Examination of a renal biopsy sample is therefore essential in order to provide the correct treatment. We have observed that patients with lupus anticoagulant (LAC), a serologic marker for APS, often have a prolonged bleeding time, which is a contraindication for performing a percutaneous renal biopsy. We undertook this study to evaluate systematically the bleeding time in 27 consecutive patients.Methods. The bleeding time was measured in 27 patients who were persistently positive for LAC and who were not exposed to aspirin or nonsteroidal antiinflammatory drugs. Platelet function and von Willebrand factor (vWF) parameters were subsequently assessed in patients with a prolonged bleeding time.

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Binding of von Willebrand Factor to Collagen Type III: Role of Specific Amino Acids in the Collagen Binding Domain of vWF and Effects of Neighboring Domains

Cited by 38 publications

References 44 publications

Structural and functional features of a collagen-binding matrix protein from the mussel byssus

Structural and functional features of a collagen-binding matrix protein from the mussel byssus

Mapping the Collagen-binding Site in the von Willebrand Factor-A3 Domain

Prolonged bleeding time and lupus anticoagulant: A second paradox in the antiphospholipid syndrome

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