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Characterization and functional analysis of cathelicidin-MH, a novel frog-derived peptide with anti-septicemic properties
J. Chai, X. Chen, T. Ye, B. Zeng, Q. Zeng, J. Wu, B. Kascakova, LA. Martins, T. Prudnikova, IK. Smatanova, M. Kotsyfakis, X. Xu
Jazyk angličtina Země Velká Británie
Typ dokumentu časopisecké články, práce podpořená grantem
Grantová podpora
31772476
National Natural Science Foundation of China
31861143050
National Natural Science Foundation of China
31911530077
National Natural Science Foundation of China
82070038
National Natural Science Foundation of China
NLK
Directory of Open Access Journals
od 2013
Free Medical Journals
od 2012
PubMed Central
od 2012
Europe PubMed Central
od 2012
ProQuest Central
od 2012-01-01
Open Access Digital Library
od 2012-01-01
Open Access Digital Library
od 2013-01-01
Health & Medicine (ProQuest)
od 2012-01-01
ROAD: Directory of Open Access Scholarly Resources
od 2012
PubMed
33875135
DOI
10.7554/elife.64411
Knihovny.cz E-zdroje
- MeSH
- antiinfekční látky chemie farmakologie MeSH
- fylogeneze MeSH
- kathelicidiny chemie farmakologie MeSH
- proteiny obojživelníků chemie farmakologie MeSH
- sekvence aminokyselin MeSH
- sekvence nukleotidů MeSH
- sekvenční seřazení MeSH
- sepse farmakoterapie MeSH
- žáby * MeSH
- zvířata MeSH
- Check Tag
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
Antimicrobial peptides form part of the innate immune response and play a vital role in host defense against pathogens. Here we report a new antimicrobial peptide belonging to the cathelicidin family, cathelicidin-MH (cath-MH), from the skin of Microhyla heymonsivogt frog. Cath-MH has a single α-helical structure in membrane-mimetic environments and is antimicrobial against fungi and bacteria, especially Gram-negative bacteria. In contrast to other cathelicidins, cath-MH suppresses coagulation by affecting the enzymatic activities of tissue plasminogen activator, plasmin, β-tryptase, elastase, thrombin, and chymase. Cath-MH protects against lipopolysaccharide (LPS)- and cecal ligation and puncture-induced sepsis, effectively ameliorating multiorgan pathology and inflammatory cytokine through its antimicrobial, LPS-neutralizing, coagulation suppressing effects as well as suppression of MAPK signaling. Taken together, these data suggest that cath-MH is an attractive candidate therapeutic agent for the treatment of septic shock.
Department of Respiratory Medicine Zhujiang Hospital Southern Medical University Guangzhou China
Faculty of Science University of South Bohemia in Ceske Budejovice Branisovska Czech Republic
Institute of Parasitology Biology Center of the Czech Academy of Sciences Branisovska Czech Republic
Citace poskytuje Crossref.org
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