The specificity of combination between ristocetins and peptides related to bacterial cell wall mucopeptide precursors

Nieto, Manuel; Perkins, H. R.

doi:10.1042/bj1240845

Cited by 108 publications

(73 citation statements)

References 6 publications

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“…The mechanism by which ristocetin aggregates platelets is not yet known. Previous studies have shown that ristocetin inhibits the synthesis of peptidoglycans in bacterial cell walls either by steric interference with their polymerization or by forming stable complexes with mucopeptide precursors (25)(26)(27). Whether similar interactions with the platelet surface are involved in ristocetin-induced platelet aggregation remains to be determined.…”

Section: Discussionmentioning

confidence: 96%

Defective Ristocetin-Induced Platelet Aggregation in von Willebrand's Disease and its Correction by Factor VIII

Weiss¹,

Rogers²,

Brand³

1973

J. Clin. Invest.

227

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A B S T RA CT The antibiotic ristocetin, in concentrations of 1.0-1.5 mg/ml, aggregated normal platelets in citrated platelet-rich plasma by a mechanism in which the release reaction played only a minor role. Platelet aggregation by ristocetin in a concentration of 1.2 mg/ ml was absent or markedly decreased in 10 patients with von Willebrand's disease. Lesser degrees of abnormality were obtained with a concentration of 1.5 mg/ml. The magnitude of the defect in ristocetin-induced platelet aggregation correlated well with the degree of abnormality of the bleeding time and the levels of antihemophilic factor (AHF, VIIIAHF) procoagulant activity. In all patients, the defect in ristocetin-induced platelet aggregation was corrected in vitro by normal plasma. Correction was also obtained with a fraction of normal cryoprecipitate that eluted in the void volume with VIIIATF after chromatography on a gel that excludes molecules larger than 5 X 10g. A similar fraction, devoid of VIIIAHF activity, obtained from patients with von Willebrand's disease had no corrective effect, but fractions obtained from patients with hemophilia were just as effective as those obtained from normal subjects. The correction activity of plasma and partially purified factor VIII was inhibited by a rabbit antibody to human factor VIII but not by a human antibody against VIIIAHF procoagulant activity. The studies provide further evidence that patients with von Willebrand's disease are deficient in a plasma factor that is necessary for normal platelet function. The activity of this factor appears to be associated with factor VIII but is unrelated to VIIIAHF procoagulant activity.

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Section: Discussionmentioning

confidence: 96%

Defective Ristocetin-Induced Platelet Aggregation in von Willebrand's Disease and its Correction by Factor VIII

Weiss¹,

Rogers²,

Brand³

1973

J. Clin. Invest.

227

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“…After paper electrophoresis, the major portion of the counts appeared to be linked to ristocetin, which is known to combine only with those peptides having a C-terminal D-D sequence (16 (Fig. 3).…”

Section: Methodsmentioning

confidence: 99%

Transpeptidase Activity of Streptomyces D-Alanyl-D Carboxypeptidases

Pollock

Ghuysen

Linder

et al. 1972

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

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In the presence of Na,NE-diacetyl-L-Lys- Paper electrophoresis was performed in 0.2 N acetic acid (pH 2.9), in acetic acid-l)yridine-water 0.33:4: 1000, pH 5.6, and in acetic acid-collidine-water 2.65:9.10: 1000, pH 7.Radioactive chromatograms or electrophoretograms were quantitatively analyzed by cutting strips (3.6 cm in width) into sections of 5-10 mm (12). The paper sections were placed in counting vials, 0.5 ml of water was added, and the vials were allowed to stand overnight. Bray's (13) dioxanescintillant (11 ml) was added and the samples were counted. In some experiments, samples were eluted before addition of the scintillant.Free D-alanine was estimated by reaction with fluorodinitrobenzene (14,15). RESULTSTranspeptidase Activity of the R61 and R39 Enzymes at High Acceptor Concentrations. Fig. la shows the rate of release of the C-terminal D-alanine from N',Nf-diacetyl-iLyS-D-Ala-D-Ala by R61 and R39 DD carboxypeptidases. Incubations were at 37°C in 17 mM phosphate buffer, pH 8, for the R61 enzyme and either in the same phosphate buffer or in 34 mi\M veronal buffer, pH 8.5, for the R39 enzyme; the final enzyme concentrations were 27 units/Al and 4 units/,l, respectively.The concentration of tripeptide was 1.5 mM; maximal hydrolysis was reached after about 90 min. Fig. 1 With both the R61 and R39 enzymes, -alanine and glycine were found to be acceptors, while iLalanine, even at a ratio to tripeptide of 100:1, was not an acceptor. At the 100:1 ratio of D-alanine or glycine to tripeptide, formation of either N',-N'-diacetyl-iLys-D-Ala-['4C]D-Ala or Na,NE-diacetyl-iLysn-Ala-[14C]Gly closely paralleled hydrolysis of the donor tripeptide in the absence of amino acid acceptor (Fig. lb and c, compare with a). After 90 min, at which time hydrolysis was 662 § To whom correspondence should be addressed.

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“…A very small peak (_1%) was present in a position slightly more cathodal than the largest peak. Vancomycin (16) and a mol wt of 2,000 (17).…”

Section: Methodsmentioning

confidence: 99%

The Effects of Ristocetin and von Willebrand Factor on Platelet Electrophoretic Mobility

Coller¹

1978

J. Clin. Invest.

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The specificity of combination between ristocetins and peptides related to bacterial cell wall mucopeptide precursors

Cited by 108 publications

References 6 publications

Defective Ristocetin-Induced Platelet Aggregation in von Willebrand's Disease and its Correction by Factor VIII

Defective Ristocetin-Induced Platelet Aggregation in von Willebrand's Disease and its Correction by Factor VIII

Transpeptidase Activity of Streptomyces D-Alanyl-D Carboxypeptidases

The Effects of Ristocetin and von Willebrand Factor on Platelet Electrophoretic Mobility

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