Biomedical subjects

H Kadeva

Publications and source records attributed to H Kadeva.

3 recordsLinked to original sources

PubMed1989

Modulation of platelet function by SIN-1A, a metabolite of molsidomine.

Molsidomine or its active metabolite SIN-1A have antithrombotic properties in experimental models. This effect seems to be related, at least in part, to their antiplatelet activities. SIN-1A inhibited platelet adhesion to collagen, platelet aggregation, and the release reaction in in vitro experiments. SIN-1A acts as an early step of platelet activation by inhibiting calcium influx and phospholipase activity, which leads to inhibition of thromboxane formation and fibrinogen binding. Antiplatelet properties were observed after oral absorption in healthy volunteers and in patients with myocardial infarction after intravenous infusion.

Collagen↗

PubMed1983

Plasma fibronectin-C1q complex formation and its effect on C1q inhibition of collagen-induced platelet aggregation.

The first component of complement (C1q) contains a collagen-like structure which evidently accounts for its ability to bind to platelets and to inhibit collagen-induced platelet aggregation. This present investigation explored the interaction among C1q, plasma fibronectin (Pl Fn) and platelets. Gel filtration chromatography (Sepharose 2B and 4B) of preincubated mixtures of C1q and Pl Fn yielded evidence of complex formation. Preincubation of Pl Fn with platelets did not affect collagen-induced platelet aggregation nor did preincubation of Pl Fn with C1q significantly affect C1q-mediated inhibition of collagen-induced platelet aggregation. These observations may indicate that the site of interaction between Pl Fn and C1q is different from the site of interaction between C1q and platelets.

Blood Platelets↗

PubMed1981

First component of complement and thrombosis.

The previous demonstration of an association between the collagen-like region of C1q (subcomponent of the first component of complement) and human platelets and of the inhibitory properties of C1q on platelet adhesion and aggregation to or by collagen has led us to consider the first component of complement as a possible modulator of the platelet-collagen interaction. Since collagen represents a major component of the vessel wall, the modification of C1 could play a role in the development of thrombosis. We have therefore studied two patients with abnormalities of complement (low or undetectable C1, C4, C2 and deficiency in C1 inhibitor) who presented with acquired angioneurotic oedema. Both patients had a history of multiple episodes of arterial and/or venous thrombosis. Platelet associated C1q was decreased or undetectable, and this condition was associated with a specific increase of collagen induced aggregation thereby suggesting a possible mechanism for the recurrent thromboembolic episodes.

Adult↗