ArticleThrombosis and haemostasis2017
Joannsin, a novel Kunitz-type FXa inhibitor from the venom of Prospirobolus joannsi.
Article in Thrombosis and haemostasis, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 12 citations in OpenAlex.
- Peptides derived from exocrine secretions of venomous animals used as traditional Chinese "worm" medicines.Zoological research · 2026Review
- Discovery of a Novel Anticoagulant Cystine Knot Peptide from Spider Venom Gland Transcriptome.International journal of molecular sciences · 2025Article
- Article
- Structural, Biochemical Characterization and Molecular Mechanism of Cerastokunin: A New Kunitz-Type Peptide with Potential Inhibition of Thrombin, Factor Xa and Platelets.The protein journal · 2024Article
- L-Palmitoylcarnitine potentiates plasmin and tPA to inhibit thrombosis.Natural products and bioprospecting · 2023Article
- Peptide OPTX-1 FromFrontiers in microbiology · 2021Article
- Identification and Characterization of ShSPI, a Kazal-Type Elastase Inhibitor from the Venom ofToxins · 2019Article
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Authors and funding
10 authors at 2 institutions in 1 country.
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Abstract
The repugnatorial glands of millipedes release various defensive chemical secretions. Although varieties of such defensive secretions have been studied, none of them is protein or peptide. Herein, a novel factor Xa (FXa) inhibitor named joannsin was identified and characterised from repugnatorial glands of Prospirobolus joannsi. Joannsin is composed of 72 amino acid residues including six cysteines, which form three intra-molecular disulfide bridges. It is a member of Kunitz-type protease inhibitor family, members of which are also found in the secretory glands of other arthropods. Recombinant joannsin exhibited remarkable inhibitory activity against trypsin and FXa with a Ki of 182.7 ± 14.6 and 29.5 ± 4.7 nM, respectively. Joannsin showed strong anti-thrombosis functions in vitro and in vivo. Joannsin is the first peptide component in millipede repugnatorial glands to be identified and is a potential candidate and/or template for the development of anti-thrombotic agents. These results also indicated that there is Kunitz-type protease inhibitor toxin in millipede repugnatorial glands as in other arthropods secretory glands.
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