Enzymatic Basis for Platelet: Collagen Adhesion as the Primary Step in Haemostasis

Jamieson, G.A.; Urban, Christin; Barber, A.J.

doi:10.1038/newbio234005a0

Cited by 166 publications

(54 citation statements)

References 20 publications

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“…5 is theoretical and was plotted according to the equation below. This relationship follows from the law of mass action (42) reported that although neither native bone nor tendon collagen will produce platelet aggregation (19,43), other insoluble collagens as well as soluble collagens are effective (10,12). Our results clearly demonstrate that purified RSSC and other soluble collagens are effective in extremely small amounts in platelet aggregation.…”

Section: Collagen-platelet Interactions 2497supporting

confidence: 62%

“…In contrast, Jamieson et al (19) found that a carbohydraterich fraction isolated from a collagenase digest of bovine tendon collagen was able to inhibit collagen aggregation. We found that Hyl-Gal (29 AM) and Hyl-Gal-Glc (18 AM) neither produce nor inhibit the native collagenmediated aggregation of platelets.…”

Section: Collagen-platelet Interactions 2497mentioning

confidence: 97%

“…It was initially shown by Butler and Cunningham (13,14) that soluble collagen contains only galactose and galactosyl-glucose units O-glycosidically linked to the hydroxyl group of hydroxylysine. The insoluble collagen fraction was later shown by Cunningham and Ford (15) (16)(17)(18) has led to the proposal (18)(19)(20) that the collagen carbohydrate sidechain represents the "recognition site" and that the binding involves an enzyme-substrate (or inhibitor) type interaction, e.g., platelet-glucosyltransferase complexed with collagen-gal. This hypothesis is a specific example of Roseman's (21) generalized theory regarding intercellular interactions and Cunningham's (22) suggestions pertinent to the role of glycoproteins in cellular recognition.…”

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confidence: 99%

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Collagen-Mediated Platelet Aggregation EFFECTS OF COLLAGEN MODIFICATION INVOLVING THE PROTEIN AND CARBOHYDRATE MOIETIES

Puett¹,

Wasserman²,

Ford³

et al. 1973

J. Clin. Invest.

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A B ST R A CT In an effort to elucidate the nature of the collagen-platelet interaction, the effects of collagen modification on platelet aggregation have been studied. We have shown that purified rat skin (salt) soluble collagen is effective at about 20 nM in mediating platelet aggregation in human platelet-rich plasma. This conce-ntration is somewhat greater than that required of several skin insoluble collagens (ca. 10 nM). Both the al(I) and a2 chains from rat skin soluble collagen produced platelet aggregation, but only at concentrations of about 13 AM and 55 AM, respectively. In contrast, heat-denatured collagen and chains (e.g., 65 AM al(I) and 160 AM a2) failed to induce platelet aggregation and to inhibit platelet aggregation by native collagen.Glycopeptides were prepared from human skin insoluble collagen by extended digestion with bacterial collagenase and trypsin, and were purified by gel filtration into two classes. One class of higher molecular weight contained sialic acid, glucosamine, galactosamine, fucose, mannose, galactose, and glucose, and the other of lower molecular weight consisted primarily of a mixture of galactose and galactosyl-glucose units O-glycosidically linked to hydroxylysine-containing peptides. We found that, after the residual tryptic activity contaminating the higher molecular weight fraction was inhibited, neither of the glycopeptide classes produced nor inhibited native human skin insoluble collagen-mediated platelet aggregation at the highest concentration examined (ca. 1-2 mg glycopeptide per ml of platelet-rich plasma glucose (Hyl-Gal and Hyl-Gal-Glc, respectively), were prepared from human urine and labeled at galactose using galactose oxidase followed by reduction with tritiated borohydride. Binding studies with platelet-rich plasnma showed that, at concentrations greater than 50 nM, Hyl-Gal gives apparent binding to platelets, but there was no evidence of Hyl-Gal-Glc binding to platelets at concentrations up to 250 nM. At concentrations several hundredfold higher than the equivalents present in the minimum concentration of rat skin soluble collagen required for platelet aggregation, neither Hyl-Gal (at 29 iM) nor Hyl-Gal-Glc (at 18 AM) caused platelet aggregation or inhibited platelet aggregation by native collagen. Also, at a concentration of 85 ,M (which represents a concentration about two thousandfold higher than the equivalents in the minimum concentration of soluble collagen required for platelet aggregation) the Gal-Glccontaining 36 residue rat skin soluble collagen al(I)-cyanogen bromide #5 peptide had no platelet aggregating or inhibiting activity.Modification of at least 90% of the rat skin soluble collagen carbohydrate by mild periodate oxidation had no effect on the platelet aggregating activity. Human skin insoluble collagen was reacted with periodate under the same conditions, and this had no demonstrable effect on its ability to induce platelet aggregation. This indicates that the normal carbohydrate side chains of these collagens are not required for t...

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Section: Collagen-platelet Interactions 2497supporting

confidence: 62%

Section: Collagen-platelet Interactions 2497mentioning

confidence: 97%

mentioning

confidence: 99%

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Collagen-Mediated Platelet Aggregation EFFECTS OF COLLAGEN MODIFICATION INVOLVING THE PROTEIN AND CARBOHYDRATE MOIETIES

Puett¹,

Wasserman²,

Ford³

et al. 1973

J. Clin. Invest.

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“…Since Roseman [ 1 ] has proposed implications of ectoglycosyltransferase systems in intercellular adhesion and cell recognition, many works tend to demonstrate the occurrence of cell surface glycosyltransferase ( [2,7] and for review, see ref.…”

Section: Introductionmentioning

confidence: 99%

New evidence for cell surface galactosyltransferase

1976

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“…Their presence is important from several points of view: first, for their possible implication in biosynthesis or repair of the carbohydrate moiety of membrane glycoconjugates [2], secondly, for their assumed role in intercellular adhesion [3] and in glycoprotein [4] or cell recognition During the past few years, biochemical evidence for the surface localization of glycosyltransferases has accumulated (for review see [7]). However, as pointed out by Keenan and Morre [8], this evidence is not necessarily conclusive.…”

mentioning

confidence: 99%

Ectogalactosyltransferase. Presence of Enzyme and Acceptors on the Rat Lymphocyte Cell Surface

1976

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Experiments are described to demonstrate the existence of ectogalactosyltransferase activity on the lymphocyte surface. The procedures described enable us to exclude the possibility of misleading results due to precursor hydrolysis and intracellular utilization of the free galactose. This depicted transferase is able to catalyse the transfer of a galactosyl residue from UDP-galactose to a nonphagocytosable exogenous acceptor and to endogenous membrane acceptors. The cells galactosylated in this way acquired new agglutinating properties with soybean agglutinin, which proves the external position of the galactosyl residues incorporated on the cell surface.

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Enzymatic Basis for Platelet: Collagen Adhesion as the Primary Step in Haemostasis

Cited by 166 publications

References 20 publications

Collagen-Mediated Platelet Aggregation EFFECTS OF COLLAGEN MODIFICATION INVOLVING THE PROTEIN AND CARBOHYDRATE MOIETIES

Collagen-Mediated Platelet Aggregation EFFECTS OF COLLAGEN MODIFICATION INVOLVING THE PROTEIN AND CARBOHYDRATE MOIETIES

New evidence for cell surface galactosyltransferase

Ectogalactosyltransferase. Presence of Enzyme and Acceptors on the Rat Lymphocyte Cell Surface

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