Platelet collagen adhesion characterization of collagen glucosyltransferase of plasma membranes of human blood platelets

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

doi:10.1016/0304-4165(71)90156-5

Cited by 101 publications

(33 citation statements)

References 27 publications

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“…At high concentrations (e.g., about 20,000 tLM), Katzman et al (46) demonstrated that Hyl-Gal-Glc inhibits aggregation of platelets by the chick al (I) chains, although Hyl-GalGlc itself did not induce platelet aggregation. The binding sites we found for Hyl-Gal may represent the platelet membrane glycosyltransferases (16,18,19) ; however, our data suggest that these do not represent the binding sites which are responsible for platelet aggregation.…”

Section: Collagen-platelet Interactions 2497contrasting

confidence: 70%

“…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 2497contrasting

confidence: 70%

mentioning

confidence: 99%

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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“…Although our data presented in this paper clearly indicate that the 65-kD protein serves as platelet receptor for type I collagen, it does not exclude the possibility that other platelet surface proteins (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12)(13)(14)(15)(16)(17)(18)(19) may also play a role in collagen-platelet interaction. Moreover, the relationship between the cloned receptor described here and other nonintegrin receptors described by others is not known.…”

Section: Discussionmentioning

confidence: 57%

“…Other integrins reported as platelet surface receptors for collagen include GPIIb/IIIa and Ia/IIa (3,4), and GPIb-IX (5,6). Other nonintegrin proteins have also been proposed as collagen receptors, including GPIV (7), a 61-kD protein (8), a 62-kD protein called p62 (9), and a 65-kD protein (10), among others (11)(12)(13)(14)(15)(16)(17)(18)(19).…”

Section: Introductionmentioning

confidence: 99%

Cloning, characterization, and functional studies of a nonintegrin platelet receptor for type I collagen.

Chiang

Rinaldy²,

Kang³

1997

J. Clin. Invest.

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“…Because the collagen-platelet interaction is an important event in hemostasis, a great deal of interest has centered on the determination of the mechanism of the interaction. A major stimulus to interest in the collagen-platelet interaction came as a result of the investigations of Barber and Jamieson (4,5). They presented evidence that membrane-bound glucosyl transferases on the surface of platelets bind to the galactose and glucose residues of collagen in an enzyme-substrate and enzyme-product complex, respectively.…”

mentioning

confidence: 99%

Evidence that fibronectin is the collagen receptor on platelet membranes.

Bensusan¹,

Koh²,

Henry³

et al. 1978

Proc. Natl. Acad. Sci. U.S.A.

113

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Evidence is presented that fibronectin is present on the platelet cell membrane and that it is a receptor for collagen in the platelet-collagen interaction. First, sodium dodecyl sulfate/acrylamide gel electrophoresis was performed on the proteins remaining attached to the surface of collagen after the removal of the remainder of the platelet by sonication. The material was relatively enriched in a glycoprotein that comigrated with cold-insoluble globulin (CIG), a form of fibronectin, and in other proteins which comigrated with myosin, actin, and tropomyosin. The presumptive presence of contractile proteins is consistent with the presence of microfibrillar proteins. Second, the collagen-attached material was shown to contain a protein that reacted'with anti-GIG serum by immunoelectrophoresis. Third, when CIG was preincubated with fibrous collagen, the platelet-collagen interaction was inhibited. Fourth, rabbit anti-human CIG stimulated human platelets to secrete the contents of their dense granules. The stimulation was not due to antibody complexes present in the solution. Fifth, a protein was extracted from wel -washed platelets and purified on affinity columns of anti-GIG antibodies. The isolated protein was found to bind to fibrous collagen. When the endothelial lining of blood vessels is breached, blood platelets come in contact with the components of connective tissue. The platelets adhere to the collagen in the connective tissue and are stimulated to release the contents of their dense granules, including ADP, Ca2+, and serotonin (1, 2). The Ca2+ and ADP are required for the subsequent platelet-platelet interactions, which lead to the formation of aggregates on a nucleus of the platelets bound to collagen (3). The aggregates form a platelet plug as an initial step in hemostasis. Because the collagen-platelet interaction is an important event in hemostasis, a great deal of interest has centered on the determination of the mechanism of the interaction. A major stimulus to interest in the collagen-platelet interaction came as a result of the investigations of Barber and Jamieson (4, 5). They presented evidence that membrane-bound glucosyl transferases on the surface of platelets bind to the galactose and glucose residues of collagen in an enzyme-substrate and enzyme-product complex, respectively. Further investigations by others tended to support this hypothesis (6, 7). However, evidence to the contrary has been presented. Menashi et al. (8) have shown that only denatured collagen can act as a substrate for the platelet glucosyl transferase, whereas only native, fibrous collagen serves as a platelet substrate in the collagen-platelet interaction (9, 10). In addition, others have shown that the carbohydrate residues of collagen can be completely destroyed by periodate oxidation without affecting the ability of the fibrous form of the oxidized collagen to interact normally with platelets (10, 11).Because the only current hypothesis as to the nature of the collagen receptor of platelets has been severe...

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Platelet collagen adhesion characterization of collagen glucosyltransferase of plasma membranes of human blood platelets

Cited by 101 publications

References 27 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

Cloning, characterization, and functional studies of a nonintegrin platelet receptor for type I collagen.

Evidence that fibronectin is the collagen receptor on platelet membranes.

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