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• W2068045646 abstract "In a recent paper published in this journal, Drs Moroi and Jung investigated the binding of von Willebrand factor (VWF) to different types of collagen, and subsequently assessed the importance of platelet glycoprotein Ibα and integrin α2β1 in platelet adhesion to collagen types I and III under conditions of flow [1Moroi M. Jung S.M. A mechanism to safeguard platelet adhesion under high‐shear flow: von Willebrand factor–glycoprotein Ib and integrin α2β1–collagen interactions make complementary, collagen‐type‐specific contributions to adhesion: reply to a rebuttal.J Thromb Haemost. 2007; 5: 1340-2Abstract Full Text Full Text PDF Google Scholar]. Conclusions drawn from these experiments are in sharp contrast with a substantial amount of previously published data and with our own experience in this field. Moroi and Jung state that VWF interacts selectively with type III, and not with types I, II, IV, and V collagen. Furthermore, under conditions of flow, integrin α2β1 was found to be important for platelet adhesion to collagen type I, but adhesion to type III was not inhibited by α2β1 blockade. Glycoprotein Ibα (GPIbα) was found to be involved, but not essential for adhesion to both collagens I and III at high shear conditions (1600 s−1). Collagen types I and III are the most abundant collagens in the extracellular matrix, and are considered to be essential for platelet deposition following vessel wall injury [2Farndale R.W. Sixma J.J. Barnes M.J. De Groot P.G. The role of collagen in thrombosis and hemostasis.J Thromb Haemost. 2004; 2: 561-73Abstract Full Text Full Text PDF PubMed Scopus (294) Google Scholar]. In contrast to what has been described by Moroi and Jung, both collagen I and III have been shown to bind VWF [3De Groot P.G. Ottenhof‐Rovers M. Van Mourik J.A. Sixma J.J. Evidence that the primary binding site of von Willebrand factor that mediates platelet adhesion on subendothelium is not collagen.J Clin Invest. 1988; 82: 65-73Crossref PubMed Google Scholar, 4Santoro S.A. Adsorption of von Willebrand factor/factor VIII by the genetically distinct interstitial collagens.Thromb Res. 1981; 21: 689-91Abstract Full Text PDF PubMed Scopus (0) Google Scholar, 5Scott D.M. Griffin B. Pepper D.S. Barnes M.J. The binding of purified factor VIII/von Willebrand factor to collagens of differing type and form.Thromb Res. 1981; 24: 467-72Abstract Full Text PDF PubMed Google Scholar] and the GPIbα–VWF interaction has been shown to be essential for platelet adhesion to both collagen I and III at higher shear rates by multiple groups [6Houdijk W.P. Sakariassen K.S. Nievelstein P.F. Sixma J.J. Role of factor VIII–von Willebrand factor and fibronectin in the interaction of platelets in flowing blood with monomeric and fibrillar human collagen types I and III.J Clin Invest. 1985; 75: 531-40Crossref PubMed Scopus (0) Google Scholar, 7Savage B. Saldivar E. Ruggeri Z.M. Initiation of platelet adhesion by arrest onto fibrinogen or translocation on von Willebrand factor.Cell. 1996; 84: 289-97Abstract Full Text Full Text PDF PubMed Scopus (1006) Google Scholar]. Integrin α2β1 has been shown to be important in adhesion to both collagen I and III [8Saelman E.U. Nieuwenhuis H.K. Hese K.M. De Groot P.G. Heijnen H.F. Sage E.H. Williams S. McKeown L. Gralnick H.R. Sixma J.J. Platelet adhesion to collagen types I through VIII under conditions of stasis and flow is mediated by GPIa/IIa (alpha 2 beta 1‐integrin).Blood. 1994; 83: 1244-50Crossref PubMed Google Scholar, 9Verkleij M.W. Morton L.F. Knight C.G. De Groot P.G. Barnes M.J. Sixma J.J. Simple collagen‐like peptides support platelet adhesion under static but not under flow conditions: interaction via alpha2 beta1 and von Willebrand factor with specific sequences in native collagen is a requirement to resist shear forces.Blood. 1998; 91: 3808-16Crossref PubMed Google Scholar], which also contradicts the current data from Moroi and Jung. Indeed, specific α2β1‐binding sequences have been demonstrated in collagen I (GFOGER, in which O is hydroxyproline) and III (GXXGER and GXXGEN) [10Knight C.G. Morton L.F. Peachey A.R. Tuckwell D.S. Farndale R.W. Barnes M.J. The collagen‐binding A‐domains of integrins alpha(1) beta(1) and alpha(2)beta(1) recognize the same specific amino acid sequence, GFOGER, in native (triple‐helical) collagens.J Biol Chem. 2000; 275: 35-40Abstract Full Text Full Text PDF PubMed Scopus (0) Google Scholar, 11Raynal N. Hamaia S.W. Siljander P.R. Maddox B. Peachey A.R. Fernandez R. Foley L.J. Slatter D.A. Jarvis G.E. Farndale R.W. Use of synthetic peptides to locate novel integrin alpha2beta1‐binding motifs in human collagen III.J Biol Chem. 2006; 281: 3821-31Abstract Full Text Full Text PDF PubMed Scopus (0) Google Scholar]. Moreover, we specifically showed that α2β1 is important for platelet adhesion to both collagen types I and III, irrespective of the physical state in which the collagen was coated onto the coverslip. Collagen is an insoluble protein; to study its properties in in vitro experiments, the protein is often proteolytically solubilized, which undoubtedly influences its characteristics. Collagen is only soluble in acidic buffers and it is possible to coat commercially available collagen preparations in a monomeric state. However, it is preferable to immobilize collagen after dialysis against a neutral phosphate buffer to form collagen fibres, which resemble collagen fibres found in vivo, as shown by electron microscopy [9Verkleij M.W. Morton L.F. Knight C.G. De Groot P.G. Barnes M.J. Sixma J.J. Simple collagen‐like peptides support platelet adhesion under static but not under flow conditions: interaction via alpha2 beta1 and von Willebrand factor with specific sequences in native collagen is a requirement to resist shear forces.Blood. 1998; 91: 3808-16Crossref PubMed Google Scholar]. However, it has been demonstrated that the requirement of platelet deposition for α2β1 also depends on the physical properties of fibrillar collagen [12Savage B. Ginsberg M.H. Ruggeri Z.M. Influence of fibrillar collagen structure on the mechanisms of platelet thrombus formation under flow.Blood. 1999; 94: 2704-15Crossref PubMed Google Scholar]. We have recently described the amino acid sequence RGQOGVMGF (O is hydroxyproline) as the VWF binding sequence in human collagen type III [13Lisman T. Raynal N. Groeneveld D. Maddox B. Peachey A.R. Huizinga E.G. De Groot P.G. Farndale R.W. A single high‐affinity binding site for von Willebrand factor in collagen III, identified using synthetic triple‐helical peptides.Blood. 2006; 108: 3753-6Crossref PubMed Scopus (0) Google Scholar]. This sequence is also present in human collagen type II, and in contrast to the results from Moroi and Jung, in our hands collagen type II interacts potently with VWF via this sequence. In human collagen I, a heterotrimer comprises two α1 and one α2 chains, and a closely related sequence occurs in the α1 chain, differing by one single amino acid (RGQAGVMGF). However, the sequence RGQAGVMGF of the human α1(I) chain aligns with the sequence RGEOGNIGF of the α2(I) chain, suggesting that the essential O in position 4 of the VWF‐binding homotrimer is provided by position 4 of the α2(I) chain sequence. Indeed, a synthetic triple helical peptide containing the sequence RGQOGVMGF fully inhibits the interaction of VWF with immobilized collagen type I, which may suggest that VWF binds collagen type I using this sequence (unpublished data). Thus, Moroi and Jung challenge the generally accepted concept that both collagens I and III bind VWF. We can offer several possible explanations for the discrepancy between their results and the general consensus. Firstly, human collagen I was only shown to interact with VWF when present in fibrillar structure [3De Groot P.G. Ottenhof‐Rovers M. Van Mourik J.A. Sixma J.J. Evidence that the primary binding site of von Willebrand factor that mediates platelet adhesion on subendothelium is not collagen.J Clin Invest. 1988; 82: 65-73Crossref PubMed Google Scholar]. Secondly, in our hands, radiolabeling of VWF as performed by Moroi and Jung substantially alters its properties (only VWF labeling with a low amount of 125I results in reliable binding data in our hands), which may explain the lack of interaction of 125I–VWF with collagen type I. It would have been informative to see experiments in which the 125I–VWF was incubated with collagen in the presence of excess unlabeled VWF to validate the specificity of 125I–VWF for the tested collagens. Moroi and Jung found a Kd value for the interaction with collagen type III that is an order of magnitude higher than Kd values reported previously, suggesting that radiolabeling VWF has changed its binding characteristics. Finally, it has recently been shown that commercial preparations of collagen I contain substantial amounts of VWF, so it might be possible that the preparation used by Moroi and Jung was already saturated with VWF, so that no interaction with added 125I–VWF could be observed [14Bernardo A. Bergeron A.L. Sun C.W. Guchhait P. Cruz M.A. Lopez J.A. Dong J.F. Von Willebrand factor present in fibrillar collagen enhances platelet adhesion to collagen and collagen‐induced platelet aggregation.J Thromb Haemost. 2004; 2: 660-9Abstract Full Text Full Text PDF PubMed Scopus (0) Google Scholar]. In conclusion, the current work by Moroi and Jung reveals different receptor requirements for platelet adhesion to collagen types I and III as compared to the literature. Because the physical properties of collagens from commercial sources are unclear and are not analyzed by Moroi and Jung, we have to be cautious to draw definitive and unexpected conclusions from in vitro data. Moreover, commercially available collagen preparations often contain substantial impurities, and may contain far less protein mass than that indicated by the manufacturer (R. W. Farndale, unpubl. data), which further complicates the comparison of experiments from laboratories using different reagents. In vivo experiments or experiments performed with well‐characterized and pure, perhaps synthetic, collagens will be required to reveal the true contribution of the different types of collagen on platelet deposition and the role the different platelet membrane proteins play in this process. The authors state that they have no conflict of interest." @default.
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• W2068045646 title "A mechanism to safeguard platelet adhesion under high‐shear flow: von Willebrand factor–glycoprotein Ib and integrin α2β1–collagen interactions make complementary, collagen‐type‐specific contributions to adhesion: a rebuttal" @default.
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