ArticlePloS one2013
The tick-derived anticoagulant madanin is processed by thrombin and factor Xa.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 21 citations in OpenAlex.
- Inhibition of Cancer Cell Migration and Invasion In Vitro by Recombinant Tyrosine-Sulfated Haemathrin, A Thrombin Inhibitor.International journal of molecular sciences · 2024Article
- Inhibitory effect of recombinant tyrosine‑sulfated madanin‑1, a thrombin inhibitor, on the behavior of MDA‑MB‑231 and SKOV3 cellsMolecular medicine reports · 2024Article
- Sinapicacid Inhibits Group IIA Secretory Phospholipase AAntioxidants (Basel, Switzerland) · 2022Article
- Acquired tick resistance: The trail is hot.Parasite immunology · 2021Review
- Rapid assembly and profiling of an anticoagulant sulfoprotein library.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Deciphering Biological Processes at the Tick-Host Interface Opens New Strategies for Treatment of Human Diseases.Frontiers in physiology · 2019Review
- Chemical Equilibrium at the Tick-Host Feeding Interface:A Critical Examination of Biological Relevance in Hematophagous Behavior.Frontiers in physiology · 2019Review
- Mosquito-Derived Anophelin Sulfoproteins Are Potent Antithrombotics.ACS central science · 2018Article
- Tyrosine sulfation modulates activity of tick-derived thrombin inhibitors.Nature chemistry · 2017Article
- A repertoire of protease inhibitor families in Amblyomma americanum and other tick species: inter-species comparative analyses.Parasites & vectors · 2017Article
- Identification and anticoagulant activity of a novel Kunitz-type protein HA11 from the salivary gland of the tick Hyalomma asiaticum.Experimental & applied acarology · 2017Article
- Identification and Mechanistic Analysis of a Novel Tick-Derived Inhibitor of Thrombin.PloS one · 2015Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The cysteine-less peptidic anticoagulants madanin-1 and madanin-2 from the bush tick Haemaphysalis longicornis are the founding members of the MEROPS inhibitor family I53. It has been previously suggested that madanins exert their functional activity by competing with physiological substrates for binding to the positively charged exosite I (fibrinogen-binding exosite) of α-thrombin. We hereby demonstrate that competitive inhibition of α-thrombin by madanin-1 or madanin-2 involves binding to the enzyme's active site. Moreover, the blood coagulation factors IIa and Xa are shown to hydrolyze both inhibitors at different, although partially overlapping cleavage sites. Finally, the three-dimensional structure of the complex formed between human α-thrombin and a proteolytic fragment of madanin-1, determined by X-ray crystallography, elucidates the molecular details of madanin-1 recognition and processing by the proteinase. Taken together, the current findings establish the mechanism of action of madanins, natural anticoagulants that behave as cleavable competitive inhibitors of thrombin.
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