Adhesion-dependent heparin production by platelets

Vannucchi, Simonetta; Fibbi, Gabriella; Pasquali, Franca; Rosso, Mario Del; Cappelletti, R; Chiarugi, Vincenzo

doi:10.1038/296352a0

Cited by 25 publications

(7 citation statements)

References 7 publications

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“…Among plasmatic GAGs, heparin is the most interesting one for its anticoagulant/antithrombotic properties, but it is also the most elusive one. Plasmatic heparin, together with heparin and heparan sulfate bound to endothelial cells, might play a physiological role in the maintenance of the hemostatic balance and might be involved in thrombotic/hemorrhagic pathologies [4][5][6][7][8]. The presence of heparin in human plasma was previously suggested, and all studies agree that heparin is associated with proteins or peptides [1,[9][10][11].…”

Section: Introductionsupporting

confidence: 57%

Isolation of Endogenous Anticoagulant N-Sulfated Glycosaminoglycans in Human Plasma from Healthy Subjects

Ruggiero

Melli²,

Parma³

et al. 2002

Pathophysiol Haemos Thromb

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Endogenous N-sulfated glycosaminoglycans (GAGs) comigrating with standard heparin and sensitive to nitrous acid treatment were isolated from plasma of healthy donors. The amount of these compounds was 7–10 µg/ml, and activated partial thromboplastin time, anti-Xa and anti-IIa activities were similar to those of standard heparin of high molecular mass. Analysis with gradient PAGE of the putative endogenous heparin showed a mean molecular mass of 12 kD. These N-sulfated GAGs could be isolated only after removal of binding peptides that impaired purification by ion-exchange chromatography. We used SDS-PAGE as a tool to separate peptides from endogenous GAGs. N-sulfated GAGs exited the gel before peptides when the electrophoresis was overrun. Endogenous GAGs could be recovered by ion-exchange chromatography of the SDS-PAGE buffer, ‘free’ from associating peptides. These results strongly support the hypothesis that endogenous heparin is associated in vitro with a variety of proteins and that this association could be responsible for modification of both heparin and protein activities.

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Section: Introductionsupporting

confidence: 57%

Isolation of Endogenous Anticoagulant N-Sulfated Glycosaminoglycans in Human Plasma from Healthy Subjects

Ruggiero

Melli²,

Parma³

et al. 2002

Pathophysiol Haemos Thromb

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“…We hypothesize that they are part of native supramolecular structure(s) in which GAGs, including heparin, are vehicled in human plasma; alternatively, they could be generated by proteolysis of plasma proteins. Dilution of these peptides with loss of aggregation might play a role in the interaction between GAGs and endothelial cells [16] or platelets where dilution causes the release of heparin [19].…”

Section: Resultsmentioning

confidence: 99%

Heparin binding peptides co‐purify with glycosaminoglycans from human plasma

Chevanne¹,

Caldini²,

Manao³

et al. 1999

FEBS Letters

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Glycosaminoglycans (GAGs) are complexed with plasma proteins and proteolysis of plasma reduced the proteinĜ AG ratio about 140-fold. After dialysis, analysis by gradient PAGE revealed heparinase-1-sensitive GAGs, thus suggesting that heparin could be among the plasma GAGs. However, after dialysis most of the plasma GAGs were still not`free'. PAGE of peptides resistant to proteolysis showed high molecular weight bands on the two sides of the dialysis membrane despite the 3.5 kDa molecular weight cut-off. Progressive dilution of the sample allowed passage of peptides appearing as high molecular weight bands in the diffusate. We interpret this phenomenon as the presence of low molecular weight peptides that aggregate when concentrated. Peptides on both sides of the membranes bound heparin.z 1999 Federation of European Biochemical Societies.

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“…An endoglycosidase, present within platelet lysosomes (2,9,23), has been noted to both liberate and degrade heparan sulfate, a proteoglycan possessing heparin-like anticoagulant properties present on the surface of endothelial cells (2). Platelets themselves have been reported to release heparin after in vitro adhesion has been induced (32).…”

Section: Discussionmentioning

confidence: 99%

Heparin‐like anticoagulants in asthma

Lasser

Simon

Lyon

et al. 1987

Allergy

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In a previous study, and in the present study, we have found that the baseline plasma samples of patients with asthma contain average levels of an endogenous heparin-like material (EHM) that is significantly higher than that noted in non-allergic, non-asthmatic controls. This material appears to have properties of both heparin and heparan sulfate. Three out of six patients responding to inhalational antigen challenge displayed an acute increment in EHM concentration that coincided with a fall in FEV values. The relation of EHM concentration to provoked asthma, or to asthma in general, remains to be determined.

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Adhesion-dependent heparin production by platelets

Cited by 25 publications

References 7 publications

Isolation of Endogenous Anticoagulant N-Sulfated Glycosaminoglycans in Human Plasma from Healthy Subjects

Isolation of Endogenous Anticoagulant N-Sulfated Glycosaminoglycans in Human Plasma from Healthy Subjects

Heparin binding peptides co‐purify with glycosaminoglycans from human plasma

Heparin‐like anticoagulants in asthma

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