Toxicity Mechanism of Dangerous Scorpion Stings in Iran

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Abstract

Background:

Considering the importance of scorpions and recognizing the mechanisms of toxicity caused by their medically important species in Iran and adopting the best therapeutic approach based on these mechanisms, this study was performed by reviewing the clinical manifestations of scorpion stings.

Methods:

The research was conducted by searching for articles and researches in related websites (PubMed, EMBASE, Scopus, Web of Science and CINAHL) and using domestic and international authoritative journals using the keywords of scorpion, clinical manifestations, in a review method. Finally, 104 qualified sources were selected and after reviewing and criticizing these studies, the author’s point of view was presented.

Results:

Clinical manifestations of Scorpion sting toxicity vary due to the existence of two toxic classes of neurotoxins and cytotoxins or hemotoxins in these arthropods in Iran. The number and distribution of species with neurotoxic venom are higher than the scorpions with cytotoxic venom and are reported throughout Iran. Scorpions with cytotoxic venom are mostly widespread in south and southwest of Iran.

Conclusion:

Treatment and prevention of scorpion stings in Iran and neighboring countries in the Middle East should be planned based on the mechanism of toxicity and the presence of toxic classes with neurotoxic or cytotoxic venoms.

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Most cited references 102

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Therapeutic peptides: Historical perspectives, current development trends, and future directions

Michael K. Dunn, Jolene L. Lau (2018)

Peptide therapeutics have played a notable role in medical practice since the advent of insulin therapy in the 1920s. Over 60 peptide drugs are approved in the United States and other major markets, and peptides continue to enter clinical development at a steady pace. Peptide drug discovery has diversified beyond its traditional focus on endogenous human peptides to include a broader range of structures identified from other natural sources or through medicinal chemistry efforts. We maintain a comprehensive dataset on peptides that have entered human clinical studies that includes over 150 peptides in active development today. Here we provide an overview of the peptide therapeutic landscape, including historical perspectives, molecular characteristics, regulatory benchmarks, and a therapeutic area breakdown.

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Snake venom metalloproteinases: their role in the pathogenesis of local tissue damage.

J Gutiérrez, A Rucavado (2000)

The biochemical characteristics of hemorrhagic metalloproteinases isolated from snake venoms are reviewed, together with their role in the pathogenesis of the local tissue damage characteristic of crotaline and viperine snake envenomations. Venom metalloproteinases differ in their domain structure. Some enzymes comprise only the metalloproteinase domain, others have disintegrin-like and high cysteine domains and others present, besides these domains, an additional lectin-like subunit. All of them are zinc-dependent enzymes with highly similar zinc binding environments. Some metalloproteinases induce hemorrhage by directly affecting mostly capillary blood vessels. It is suggested that hemorrhagic enzymes cleave, in a highly selective fashion, key peptide bonds of basement membrane components, thereby affecting the interaction between basement membrane and endothelial cells. As a consequence, these cells undergo a series of morphological and functional alterations in vivo, probably associated with biophysical hemodynamic factors such as tangential fluid shear stress. Eventually, gaps are formed in endothelial cells through which extravasation occurs. In addition to hemorrhage, venom metalloproteinases induce skeletal muscle damage, myonecrosis, which seems to be secondary to the ischemia that ensues in muscle tissue as a consequence of bleeding and reduced perfusion. Microvessel disruption by metalloproteinases also impairs skeletal muscle regeneration, being therefore responsible of fibrosis and permanent tissue loss after snakebites. Moreover, venom metalloproteinases participate in the degradation of extracellular matrix components and play a relevant role in the prominent local inflammatory response that characterizes snakebite envenomations, since they induce edema, activate endogenous matrix metalloproteinases (MMPs) and are capable of releasing TNF-alpha from its membrane-bound precursor. Owing to their protagonic role in the pathogenesis of local tissue damage, snake venom metalloproteinases constitute relevant targets for natural and synthetic inhibitors which may complement antivenoms in the neutralization of these effects.

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Scorpion venom components that affect ion-channels function.

Raphael H. Valdivia, L Possani, Jose G Gurrola … (2013)

The number and types of venom components that affect ion-channel function are reviewed. These are the most important venom components responsible for human intoxication, deserving medical attention, often requiring the use of specific anti-venoms. Special emphasis is given to peptides that recognize Na(+)-, K(+)- and Ca(++)-channels of excitable cells. Knowledge generated by direct isolation of peptides from venom and components deduced from cloned genes, whose amino acid sequences are deposited into databanks are nowadays in the order of 1.5 thousands, out of an estimate biodiversity closed to 300,000. Here the diversity of components is briefly reviewed with mention to specific references. Structural characteristic are discussed with examples taken from published work. The principal mechanisms of action of the three different types of peptides are also reviewed. Na(+)-channel specific venom components usually are modifier of the open and closing kinetic mechanisms of the ion-channels, whereas peptides affecting K(+)-channels are normally pore blocking agents. The Ryanodine Ca(++)-channel specific peptides are known for causing sub-conducting stages of the channels conductance and some were shown to be able to internalize penetrating inside the muscle cells. Copyright © 2013 Elsevier Ltd. All rights reserved.

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Author and article information

Journal

Journal ID (nlm-ta): J Arthropod Borne Dis

Journal ID (iso-abbrev): J Arthropod Borne Dis

Journal ID (publisher-id): JAD

Title: Journal of Arthropod-Borne Diseases

Publisher: Tehran University of Medical Sciences

ISSN (Print): 2322-1984

ISSN (Electronic): 2322-2271

Publication date Collection: June 2023

Publication date (Electronic): 30 June 2023

Volume: 17

Issue: 2

Pages: 105-119

Affiliations

[1 ]Social Determinants of Health (SDH) Research Center and Department of Environmental Health, Kashan University of Medical Sciences, Kashan, Iran

[2 ]Toxicology Research Center, Medical Basic Sciences Institute, Ahvaz Jundishapur University of Medical Sciences, Ahvaz, Iran

[3 ]Department of Clinical Toxicology and Poisoning, Afzalipour Hospital, Kerman University of Medical Sciences, Kerman, Iran

[4 ]Clinical Research Development Unit, Afzalipour Hospital, Kerman University of Medical Sciences, Kerman, Iran

Author notes

Corresponding author: Dr Masoomeh Varzandeh, E-mail: Varzandeh37@ 123456gmail.com

Article

Publisher ID: JAD-17-105

DOI: 10.18502/jad.v17i2.13616

PMC ID: 10562200

PubMed ID: 37822761

SO-VID: e1daea25-8ab9-4787-bb29-74ffd4e96686

License:

This work is licensed under a Creative Commons Attribution-NonCommercial 4.0 International license ( https://creativecommons.org/licenses/by-nc/4.0/). Non-commercial uses of the work are permitted, provided the original work is properly cited.

Toxicity Mechanism of Dangerous Scorpion Stings in Iran

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Abstract

Background:

Methods:

Results:

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China Tropical Medicine

Most cited references 102

Therapeutic peptides: Historical perspectives, current development trends, and future directions

Snake venom metalloproteinases: their role in the pathogenesis of local tissue damage.

Scorpion venom components that affect ion-channels function.

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