Platelet Adhesion to Collagen

Sixma, Jan J.; Zanten, G. Henrita van; Saelman, Edwin U M; Verkleji, Marilyn; Lankhof, H.; Nieuwenhuis, H. K.; Groot, Philip G. de

doi:10.1055/s-0038-1642721

Cited by 66 publications

(42 citation statements)

References 11 publications

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“…Likewise, the potency of peptide 6 is consistent with the evidence presented here that this peptide contains an ␣ 2 ␤ 1 recognition sequence. Our data lend support to the view (33, 34) that collagen-platelet interaction is a two-step process involving an initial recognition of adhesive sequences, such as those recognized by ␣ 2 ␤ 1 , as a primary interaction that may be especially important to retain platelets under flow conditions (7,35). Subsequent engagement with a second receptor induces signaling leading to platelet activation (aggregation).…”

Section: Discussionsupporting

confidence: 69%

The Platelet Reactivity of Synthetic Peptides Based on the Collagen III Fragment α1(III)CB4

Morton¹,

Peachey²,

Knight³

et al. 1997

Journal of Biological Chemistry

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The platelet-reactive collagen III-derived fragment ␣1(III)CB4 has been synthesized as seven overlapping peptides, each as a homotrimeric triple-helical species covalently linked at the C terminus. Additional Gly-ProHyp triplets were introduced at each end of the peptide sequence to ensure a stable triple-helical conformation at 20°C, the temperature at which cell reactivity was measured. A Cys-containing triplet was included at each end to allow intermolecular cross-linking. All seven peptides in triple-helical, cross-linked form were able to cause platelet aggregation. Peptide 6, the most reactive species, was more aggregatory than collagen fibers. Platelet adhesion occurred to all peptides immobilized on plastic in monomeric form. Adhesion was integrin ␣ 2 ␤ 1 -independent except in the case of peptide 6, adhesion to which was partially reduced by anti-integrin ␣ 2 ␤ 1 monoclonal antibodies. The presence of an ␣ 2 ␤ 1 recognition site in peptide 6 was confirmed using HT 1080 cells, which express ␣ 2 ␤ 1 as their major or sole collagen receptor. HT 1080 adhesion to both peptide 6 and collagen was strongly inhibited by anti-integrin ␣ 2 ␤ 1 monoclonal antibodies. These cells did not adhere to any of the other peptides. Comparison of the structure of peptide 6 with that of adjacent peptides indicates that the sequence Gly-Gly-Pro-Hyp-Gly-Pro-Arg, residues 522-528 of the collagen ␣1(III) chain, represents the minimum structure required for the recognition of ␣ 2 ␤ 1 . Our findings support the view that the collagen triple helix possesses an intrinsic platelet reactivity that can be expressed independently of integrin ␣ 2 ␤ 1 and the precise level of which is governed by the exact nature of the primary sequence. Sequences such as those recognizing ␣ 2 ␤ 1 may potentiate the activity, whereas others may have the opposite effect.Cell interaction with collagens is mediated by specific cellsurface receptors, important among which are the integrins ␣ 1 ␤ 1 and ␣ 2 ␤ 1 (1). Integrins recognize discrete amino acid sequences, the best known of which, perhaps, is the RGD 1 sequence, which serves as a cell-binding site in several matrix proteins and is recognized by a number of integrins, including the ␤ 1 -integrins ␣

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Section: Discussionsupporting

confidence: 69%

The Platelet Reactivity of Synthetic Peptides Based on the Collagen III Fragment α1(III)CB4

Morton¹,

Peachey²,

Knight³

et al. 1997

Journal of Biological Chemistry

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“…Collagen types I, II, III, and IV induce platelet adhesion (reviewed in Ref. 34). C.IV plays a role in cell migration and cell binding during tumor metastasis (35).…”

Section: Discussionmentioning

confidence: 99%

Human Factor IX Binds to Specific Sites on the Collagenous Domain of Collagen IV

Wolberg¹,

Stafford²,

Erie³

1997

Journal of Biological Chemistry

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The primary region of factor IX that mediates binding to bovine aortic endothelial cells resides in residues 3-11 of the N-terminal region known as the Gla domain. Recently, it was proposed that the observed binding to endothelial cells is actually a measure of the interaction between factor IX and collagen IV (Cheung, W. F., van den Born, J., Kuhn, K., Kjellen, L., Hudson, B. G., and Stafford, D. W. (1996) Proc. Natl. Acad. Sci. U. S. A. 93, 11068 -11073). To confirm that factor IX binds to collagen IV and to examine the specificity of this interaction, we used scanning force microscopy to examine factor IX binding to collagen IV. We imaged collagen IV in the presence and the absence of factor IX and observed specific interactions between factor IX and collagen IV. Our results demonstrate that factor IX binds to collagen IV at specific sites in the collagenous domain ϳ98 and ϳ50 nm from the C-terminal pepsin-cleaved end.

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“…Some are not very potent inducers of adhesion/aggregation [22], The collagen in vascular basal lamina is type IV. Early reports [20,23] found that type IV collagen is unable to trigger adhesion/aggregation.…”

Section: Role Of Collagenmentioning

confidence: 99%

Platelet Adhesion and Aggregation without Endothelial Denudation or Exposure of Basal Lamina and/or Collagen

Rosenblum

1997

J Vasc Res

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In vivo microvascular studies and postmortem studies of large and small blood vessels in a variety of species and vascular beds show that platelet adhesion and aggregation can occur over endothelium that is not denuded; the basal lamina and collagen need not be exposed. Moreover, evidence suggests that, at least in arterioles, locally adherent degranulating platelets can actually produce disruption and denudation of endothelial cells. Therefore, one should not assume, at least in small vessels, that observed sites of denudation were the cause rather than the result of adhesion/aggregation. All of this evidence should encourage a greatly increased emphasis on causes of adhesion/aggregation that do not depend upon collagen and/or collagen-bound von Willebrand factor (vWF). This emphasis does not deny the importance of collagen or collagen-bound vWF as the trigger for adhesion/aggregation when such exposure occurs. However, the emphasis on a structurally intact endothelial surface does lead to the corollary caution: even when endothelium is interrupted and potential triggers of adhesion/aggregation are exposed, this does not mean that these substances were, in fact, the cause of the locally observed adhesion/ aggregation. Local exposure of key endothelial cell adhesion molecules such as PEC AM may contribute to the adhesion/aggregation of platelets over structurally intact but injured endothelium. Adhesion/aggregation over injured but intact endothelium can also be modified by maneuvers that alter the local production of antiplatelet paracrine substances like endothelium-derived relaxing factor/nitric oxide. This supports the hypothesis that local decrements in the release of antiplatelet paracrine substances from perturbed but structurally intact endothelium leads to local adhesion/aggregation especially of platelets activated by a preexisting pathology. Coronary artery disease, ischemic stroke and diabetes are examples of diseases associated with both hyperaggregable platelets and with impaired endothelial synthesis/release of antiplatelet paracrine mediators. In addition, repetitive stereotypic symptoms in transient ischemic attacks may be related to repetitive and increasing damage to endothelium produced by successive episodes of platelet adhesion/ aggregation/degranulation at the same sites.

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Platelet Adhesion to Collagen

Cited by 66 publications

References 11 publications

The Platelet Reactivity of Synthetic Peptides Based on the Collagen III Fragment α1(III)CB4

The Platelet Reactivity of Synthetic Peptides Based on the Collagen III Fragment α1(III)CB4

Human Factor IX Binds to Specific Sites on the Collagenous Domain of Collagen IV

Platelet Adhesion and Aggregation without Endothelial Denudation or Exposure of Basal Lamina and/or Collagen

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