Snake C-type lectin-like proteins and platelet receptors

Clemetson, Kenneth John; Lu, Qiumin; Clemetson, Jeannine (2006). Snake C-type lectin-like proteins and platelet receptors. Pathophysiology of haemostasis and thrombosis, 34(4-5), pp. 150-155. Karger 10.1159/000092414

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Snake venoms are complex mixtures of biologically active proteins and peptides. Many affect haemostasis by activating or inhibiting coagulant factors or platelets, or by disrupting endothelium. Snake venom components are classified into various families, such as serine proteases, metalloproteinases, C-type lectin-like proteins, disintegrins and phospholipases. Snake venom C-type lectin-like proteins have a typical fold resembling that in classic C-type lectins such as the selectins and mannose-binding proteins. Many snake venom C-type lectin-like proteins have now been characterized, as heterodimeric structures with alpha and beta subunits that often form large molecules by multimerization. They activate platelets by binding to VWF or specific receptors such as GPIb, alpha2beta1 and GPVI. Simple heterodimeric GPIb-binding molecules mainly inhibit platelet functions, whereas multimeric ones activate platelets. A series of tetrameric snake venom C-type lectin-like proteins activates platelets by binding to GPVI while another series affects platelet function via integrin alpha2beta1. Some act by inducing VWF to bind to GPIb. Many structures of these proteins, often complexed with their ligands, have been determined. Structure-activity studies show that these proteins are quite complex despite similar backbone folding. Snake C-type lectin-like proteins often interact with more than one platelet receptor and have complex mechanisms of action.

Item Type:

Journal Article (Original Article)

Division/Institute:

04 Faculty of Medicine > Pre-clinic Human Medicine > Theodor Kocher Institute

UniBE Contributor:

Clemetson, Kenneth John and Clemetson, Jeannine

Subjects:

600 Technology > 610 Medicine & health

ISSN:

1424-8832

Publisher:

Karger

Language:

English

Submitter:

Factscience Import

Date Deposited:

04 Oct 2013 14:51

Last Modified:

17 Jul 2017 14:22

Publisher DOI:

10.1159/000092414

PubMed ID:

16707918

Web of Science ID:

000237698600002

BORIS DOI:

10.7892/boris.21631

URI:

https://boris.unibe.ch/id/eprint/21631 (FactScience: 9276)

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