69633-04-1
Chemical Structure
Natrin
- CAS No.: 69633-04-1
- Formula:C8H7Cl3O5S
- Molecular Weight:321.56
InChIKey: YWNCRLWPJZLWGH-UHFFFAOYSA-N
SMILES: O=S(O)(OCCOC1=CC(Cl)=C(C=C1Cl)Cl)=O
Biological Activity: Natrin is a cysteine-rich secretory protein (CRISP) toxin found in snake venom that acts as an ion channel modulator. Natrin blocks the large-conductance calcium-activated potassium channel BKCa with an IC50 of 34.4 nM; it acts as a non-competitive antagonist to inhibit the ryanodine binding capacity and calcium release channel activity of RyR1, with an IC50 of 1.03 μM for purified RyR1. Natrin induces vasoconstrictor responses without affecting basal tension. Natrin induces apoptosis in human hepatoma cells, elevating the Bax/Bcl‑2 ratio through the mitochondrial apoptotic pathway and causing metabolic perturbation. Natrin can be used in research on diseases such as hepatocellular carcinoma[1][2][3][4][5].
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Natrin | Natrin is a cysteine-rich secretory protein (CRISP) toxin found in snake venom that acts as an ion channel modulator. Natrin blocks the large-conductance calcium-activated potassium channel BKCa with an IC50 of 34.4 nM; it acts as a non-competitive antagonist to inhibit the ryanodine binding capacity and calcium release channel activity of RyR1, with an IC50 of 1.03 μM for purified RyR1. Natrin induces vasoconstrictor responses without affecting basal tension. Natrin induces apoptosis in human hepatoma cells, elevating the Bax/Bcl‑2 ratio through the mitochondrial apoptotic pathway and causing metabolic perturbation. Natrin can be used in research on diseases such as hepatocellular carcinoma. | |||||||||||||||||||||
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References
- [1]. Wang J, et al. Blocking effect and crystal structure of natrin toxin, a cysteine-rich secretory protein from Naja atra venom that targets the BKCa channel. Biochemistry. 2005 Aug 2;44(30):10145-52. [Content Brief]
- [2]. Deka A, et al. Naja kaouthia venom protein, Nk-CRISP, upregulates inflammatory gene expression in human macrophages. International journal of biological macromolecules. 2020 Oct 1;160:602-11.
- [3]. Zhou Q, et al. Structural and functional characterization of ryanodine receptor-natrin toxin interaction. Biophysical journal. 2008 Nov 01;95(9):4289-99. [Content Brief]
- [4]. Lu S, et al. Metabolomic study of natrin-induced apoptosis in SMMC-7721 hepatocellular carcinoma cells by ultra-performance liquid chromatography-quadrupole/time-of-flight mass spectrometry. International journal of biological macromolecules. 2019 Mar 1;124:1264-73. [Content Brief]
- [5]. Averin AS, et al. Cardiovascular Effects of Snake Toxins: Cardiotoxicity and Cardioprotection. Acta naturae. 2021;13(3):4-14. [Content Brief]