Inhibition of platelet aggregation by a whole cell extract from strains of group B streptococcus

• Published in: Thrombosis research Vol. 58; no. 3; pp. 283 - 291
• Main Authors: Usui, Yukio, Ichiman, Yoshitoshi, Ohtomo, Toshichika, Suganuma, Masaru, Yoshida, Kosaku
• Format: Journal Article
• Language: English
• Published: New York, NY Elsevier Ltd 01.05.1990; Elsevier Science
• Subjects: Biological and medical sciences; Blood coagulation. Blood cells; Fibrinogen - metabolism; Fundamental and applied biological sciences. Psychology; Humans; Hydrochloric Acid; Molecular and cellular biology; Platelet; platelet aggregation; Platelet Aggregation Inhibitors; Protein Binding; Streptococcus agalactiae - physiology; platelet aggregation; Aggregation; Streptococcaceae; Platelet; Enzyme; Collagen; Microorganism culture; Gel filtration; Bacteria; Micrococcales; Thrombin; Inhibition
• ISSN: 0049-3848; 1879-2472
• DOI: 10.1016/0049-3848(90)90098-W

A whole cell extract (HC1-Ext) from strains of group B streptococci (GBS) possessing fibrinogen binding activity prevented the platelet aggregation induced with adenosine 5′-diphosphate (ADP), collagen and thrombin, while aggregation by epinephrine and ristocetin was slightly inhibited and arachidonic acid-induced platelet aggregation was not affected whatsoever. When the HCl-Ext was added after commencement of the aggregation, deaggregation was observed in cases induced by ADP, collagen, and thrombin. By precoating the washed platelets with HC1-Ext, both of ADP- and collagen-induced platelet aggregation were suppressed. The active factor in the HCl-Ext seemed to be undialyzable, trypsin-susceptible, and proteinaceous substance, unlike GBS polysaccharide type antigen.