Comparison study of the response with botulinum toxin muscle injection in the ICR mice from three different sources

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Abstract

Botulinum-toxin A (BoNT/A) is a widely used not only for cosmetics but also for various experimental purposes including muscle-related research. In this study, we applied BoNT/A to mouse muscle of three different sources to compare and evaluate the biological and pathological response. The three different mouse sources consist of Korl:ICR (Korea FDA source), A:ICR (USA source) and B:ICR (Japan source) which were purchased from each different vendors. To compare the responses of ICR mice with BoNT/A muscle injection, we examined the body weight, hematological and serum biochemistry analysis. Also, we evaluated the muscle change by histopathological analysis and gene expression patterns of muscle-related target by qPCR. The body weight gain was decreased in the BoNT/A-treated group compared with the control group. In clinical pathologic analysis and gene expression patterns, the data showed that the responses in the BoNT/A-treated group were similar compared with the control group. Decreased muscle fiber was observed in BoNT/A-treated group compared with control group, while Korl:ICR showed a little low response with the other mouse sources. In conclusion, our results suggest that three different sources ICR mice (Korl:ICR, A:ICR and B:ICR) have a similar biological and pathological responses in BoNT/A muscle injection.

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BOTULINUM TOXIN

P K Nigam, Anjana Nigam (2010)

Botulinum toxin, one of the most poisonous biological substances known, is a neurotoxin produced by the bacterium Clostridium botulinum. C. botulinum elaborates eight antigenically distinguishable exotoxins (A, B, C1, C2, D, E, F and G). All serotypes interfere with neural transmission by blocking the release of acetylcholine, the principal neurotransmitter at the neuromuscular junction, causing muscle paralysis. The weakness induced by injection with botulinum toxin A usually lasts about three months. Botulinum toxins now play a very significant role in the management of a wide variety of medical conditions, especially strabismus and focal dystonias, hemifacial spasm, and various spastic movement disorders, headaches, hypersalivation, hyperhidrosis, and some chronic conditions that respond only partially to medical treatment. The list of possible new indications is rapidly expanding. The cosmetological applications include correction of lines, creases and wrinkling all over the face, chin, neck, and chest to dermatological applications such as hyperhidrosis. Injections with botulinum toxin are generally well tolerated and side effects are few. A precise knowledge and understanding of the functional anatomy of the mimetic muscles is absolutely necessary to correctly use botulinum toxins in clinical practice.

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Structural analysis of the catalytic and binding sites of Clostridium botulinum neurotoxin B.

S Swaminathan, Subramaniam Eswaramoorthy (2000)

Clostridium botulinum neurotoxins are among the most potent toxins to humans. The crystal structures of intact C. botulinum neurotoxin type B (BoNT/B) and its complex with sialyllactose, determined at 1. 8 and 2.6 A resolution, respectively, provide insight into its catalytic and binding sites. The position of the belt region in BoNT/B is different from that in BoNT/A; this observation presents interesting possibilities for designing specific inhibitors that could be used to block the activity of this neurotoxin. The structures of BoNT/B and its complex with sialyllactose provide a detailed description of the active site and a model for interactions between the toxin and its cell surface receptor. The latter may provide valuable information for recombinant vaccine development.

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Properties and use of botulinum toxin and other microbial neurotoxins in medicine.

Anthony Johnson, E Schantz (1992)

Crystalline botulinum toxin type A was licensed in December 1989 by the Food and Drug Administration for treatment of certain spasmodic muscle disorders following 10 or more years of experimental treatment on human volunteers. Botulinum toxin exerts its action on a muscle indirectly by blocking the release of the neurotransmitter acetylcholine at the nerve ending, resulting in reduced muscle activity or paralysis. The injection of only nanogram quantities (1 ng = 30 mouse 50% lethal doses [U]) of the toxin into a spastic muscle is required to bring about the desired muscle control. The type A toxin produced in anaerobic culture and purified in crystalline form has a specific toxicity in mice of 3 x 10(7) U/mg. The crystalline toxin is a high-molecular-weight protein of 900,000 Mr and is composed of two molecules of neurotoxin (ca. 150,000 Mr) noncovalently bound to nontoxic proteins that play an important role in the stability of the toxic unit and its effective toxicity. Because the toxin is administered by injection directly into neuromuscular tissue, the methods of culturing and purification are vital. Its chemical, physical, and biological properties as applied to its use in medicine are described. Dilution and drying of the toxin for dispensing causes some detoxification, and the mouse assay is the only means of evaluation for human treatment. Other microbial neurotoxins may have uses in medicine; these include serotypes of botulinum toxins and tetanus toxin. Certain neurotoxins produced by dinoflagellates, including saxitoxin and tetrodotoxin, cause muscle paralysis through their effect on the action potential at the voltage-gated sodium channel. Saxitoxin used with anaesthetics lengthens the effect of the anaesthetic and may enhance the effectiveness of other medical drugs. Combining toxins with drugs could increase their effectiveness in treatment of human disease.

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Author and article information

Contributors

Kil Soo Kim: +82 53-950-7792 , kskim728@knu.ac.kr

Journal

Journal ID (nlm-ta): Lab Anim Res

Journal ID (iso-abbrev): Lab Anim Res

Title: Laboratory Animal Research

Publisher: BioMed Central (London )

ISSN (Print): 1738-6055

ISSN (Electronic): 2233-7660

Publication date (Electronic): 26 July 2019

Publication date PMC-release: 26 July 2019

Publication date Collection: 2019

Volume: 35

Electronic Location Identifier: 11

Affiliations

[1 ]ISNI 0000 0004 6401 4233, GRID grid.496160.c, Laboratory Animal Center, Daegu-Gyeongbuk Medical Innovation Foundation, ; Daegu, Korea

[2 ]KPC Coporation, Gwangju, 12773 Korea

[3 ]ISNI 0000 0001 0719 8572, GRID grid.262229.f, Department of Pharmacy, College of Pharmacy, , Pusan National University, ; Busan, Korea

[4 ]ISNI 0000 0004 0387 0116, GRID grid.411131.7, Department of Health and Exercise Science, , Korea National Sport University, ; 88-15 Oryung-dong, Songpa-gu, Seoul, Korea

[5 ]Central Research Institute, Kine sciences, F1, Milovany, 28, Inchon-ro, Seongbuk-gu, Seoul, Korea

[6 ]ISNI 0000 0001 0719 8572, GRID grid.262229.f, Department of Biomaterials Science, College of Natural Resources & Life Science/Life and Industry Convergence Research Institute, , Pusan National University, ; Miryang, Korea

[7 ]ISNI 0000 0001 0661 1556, GRID grid.258803.4, Laboratory of Histology, College of Veterinary Medicine, , Kyungpook National University, ; Daegu, Korea

[8 ]ISNI 0000 0001 0661 1556, GRID grid.258803.4, College of Veterinary Medicine, , Kyungpook National University, ; Daegu, Korea

Article

Publisher ID: 10

DOI: 10.1186/s42826-019-0010-4

PMC ID: 7081521

SO-VID: dc6ea1a8-cdb9-449d-bac1-095c1e61495b

License:

Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License ( http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver ( http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

History

Date received : 13 May 2019

Date accepted : 4 July 2019

Funding

Funded by: Ministry of Food and Drug Safety

Award ID: This project was supported by a grant of NLAR (National Laboratory Animal Resources) from Ministry of Food and Drug Safety in 2018.

Award Recipient : Dae Youn Hwang

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ScienceOpen disciplines: Life sciences

Keywords: korl:icr,botulinum toxin,muscle,icr mouse

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ScienceOpen disciplines: Life sciences

Keywords: korl:icr, botulinum toxin, muscle, icr mouse

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Comparison study of the response with botulinum toxin muscle injection in the ICR mice from three different sources

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Most cited references 24

BOTULINUM TOXIN

Structural analysis of the catalytic and binding sites of Clostridium botulinum neurotoxin B.

Properties and use of botulinum toxin and other microbial neurotoxins in medicine.

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