ArticleThe Biochemical journal2007
Hemicalcin, a new toxin from the Iranian scorpion Hemiscorpius lepturus which is active on ryanodine-sensitive Ca2+ channels.
Article in The Biochemical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 87 citations in OpenAlex.
- Review
- Properties and Pharmacology of Scorpion Toxins and Their Biotechnological Potential in Agriculture and Medicine.Toxins · 2025Review
- Biochemical characterization and activity profiling of recombinant phospholipase A2 from Hemiscorpius lepturus expressed in E. coli with in vivo antibody response.Scientific reports · 2025Article
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- Hemolytic Uremic Syndrome Secondary to Scorpion Envenomation in a 7-Year-Old Boy from Southwestern Iran.Iranian journal of pathology · 2024Article
- Venom-derived peptides for breaking through the glass ceiling of drug development.Frontiers in chemistry · 2024Review
- Scorpion Peptides and Ion Channels: An Insightful Review of Mechanisms and Drug Development.Toxins · 2023Review
- Discovery of Leptulipin, a New Anticancer Protein from theIranian Scorpion,Molecules (Basel, Switzerland) · 2022Article
- Cellular Immunity in Mice Vaccinated with Recombinant Phospholipase D Toxoid ofJournal of arthropod-borne diseases · 2022Article
- Structural Insight Into Ryanodine Receptor Channelopathies.Frontiers in pharmacology · 2022Review
- Discovery of a New Analgesic Peptide, Leptucin, from the Iranian Scorpion,Molecules (Basel, Switzerland) · 2021Article
- Novel Mutant Phospholipase D fromMolecules (Basel, Switzerland) · 2020Article
- Purification and characterization of a novel type of neurotoxic peptides from the venom of the Iranian scorpionIranian journal of basic medical sciences · 2020Article
- Venoms of Iranian Scorpions (Arachnida, Scorpiones) and Their Potential for Drug Discovery.Molecules (Basel, Switzerland) · 2019Review
- Transcriptomic and Proteomic Analyses Reveal the Diversity of Venom Components from the Vaejovid ScorpionToxins · 2018Article
- Co-Localization of Crotamine with Internal Membranes and Accentuated Accumulation in Tumor Cells.Molecules (Basel, Switzerland) · 2018Article
- Scorpionism byThe journal of venomous animals and toxins including tropical diseases · 2018Review
- Recombinant expression of Intrepicalcin from the scorpion Vaejovis intrepidus and its effect on skeletal ryanodine receptors.Biochimica et biophysica acta. General subjects · 2017Article
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Authors and funding
10 authors at 3 institutions in 3 countries.
Funding
Abstract
In the present work, we purified and characterized a novel toxin named hemicalcin from the venom of the Iranian chactoid scorpion Hemiscorpius lepturus where it represents 0.6% of the total protein content. It is a 33-mer basic peptide reticulated by three disulfide bridges, and that shares between 85 and 91% sequence identity with four other toxins, all known or supposed to be active on ryanodine-sensitive calcium channels. Hemicalcin differs from these other toxins by seven amino acids at positions 9 (leucine/arginine), 12 (alanine/glutamic acid), 13 (aspartic acid/asparagine), 14 (lysine/asparagine), 18 (serine/glycine), 26 (threonine/alanine) and 28 (proline/isoleucine/alanine). In spite of these differences, hemicalcin remains active on ryanodine-sensitive Ca2+ channels, since it increases [3H]ryanodine binding on RyR1 (ryanodine receptor type 1) and triggers Ca2+ release from sarcoplasmic vesicles. Bilayer lipid membrane experiments, in which the RyR1 channel is reconstituted and its gating properties are analysed, indicate that hemicalcin promotes an increase in the opening probability at intermediate concentration and induces a long-lasting subconductance level of 38% of the original amplitude at higher concentrations. Mice intracerebroventricular inoculation of 300 ng of hemicalcin induces neurotoxic symptoms in vivo, followed by death. Overall, these data identify a new biologically active toxin that belongs to a family of peptides active on the ryanodine-sensitive channel.
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