Cited by 567Antimicrobial Peptides and ActivitiesStreptococcal Infections and TreatmentsWound Healing and Treatments

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Cutaneous Injury Induces the Release of Cathelicidin Anti-Microbial Peptides Active Against Group A Streptococcus

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Dorschner, Robert A., Pestonjamasp, Vasumati K., Tamakuwala, Seema, Ohtake, Takaaki, Rudisill, Jennifer, Nizet, Victor, Agerberth, Birgitta, Gudmundsson, Gudmunder H., Gallo, Richard L.·2001·Journal of Investigative Dermatology

DOI 10.1046/j.1523-1747.2001.01340.x

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Abstract

Cathelicidins are a family of peptides thought to provide an innate defensive barrier against a variety of potential microbial pathogens. The human and mouse cathelicidins (LL-37 and CRAMP, respectively) are expressed at select epithelial interfaces where they have been proposed to kill a number of gram-negative and gram-positive bacteria. To determine if these peptides play a part in the protection of skin against wound infections, the anti-microbial activity of LL-37 and CRAMP was determined against the common wound pathogen group A Streptococcus, and their expression was examined after cutaneous injury. We observed a large increase in the expression of cathelicidins in human and murine skin after sterile incision, or in mouse following infection by group A Streptococcus. The appearance of cathelicidins in skin was due to both synthesis within epidermal keratinocytes and deposition from granulocyctes that migrate to the site of injury. Synthesis and deposition in the wound was accompanied by processing from the inactive prostorage form to the mature C-terminal peptide. Analysis of anti-microbial activity of this C-terminal peptide against group A Streptococcus revealed that both LL-37 and CRAMP potently inhibited bacterial growth. Action against group A Streptococcus occurred in conditions that typically abolish the activity of anti-microbial peptides against other organisms. Thus, cathelicidins are well suited to provide defense against infections due to group A Streptococcus, and represent an important element of cutaneous innate immunity.

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Authors: Dorschner, R. A., Pestonjamasp, V. K., Tamakuwala, S., Ohtake, T., Rudisill, J., Nizet, V., Agerberth, B., Gudmundsson, G. H., & Gallo, R. L.
Affiliations: University of California San Diego (US)
Karolinska Institutet (SE)
Corresponding author: Gallo, Richard L.
ORCID: Dorschner, Robert A.
Ohtake, Takaaki
Nizet, Victor
Gallo, Richard L.
Venue: Journal of Investigative Dermatology
Publisher: Elsevier BV
Published: 2001-07
Volume: 117
Issue: 1
Pages: 91-97
ISSN: 0022-202X (ISSN-L)
DOI: 10.1046/j.1523-1747.2001.01340.x
OpenAlex: W2085793178
Cited by: 567
References: 56
Citations by year: 2026: 8 · 2025: 10 · 2024: 13 · 2023: 17 · 2022: 11 · 2021: 12 · 2020: 16 · 2019: 25 · 2018: 23 · 2017: 24 · 2016: 20 · 2015: 26 · 2014: 25 · 2013: 23 · 2012: 33
FWCI: 14.20
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 5267 d)
Locations: Journal of Investigative Dermatology (publishedVersion)
PubMed (publishedVersion)
Funders: National Institute of Allergy and Infectious Diseases (AI48176, R21AI048176)
National Institute of Arthritis and Musculoskeletal and Skin Diseases (AR-44379)
Topics: Life Sciences › Immunology and Microbiology › Microbiology › Antimicrobial Peptides and Activities
Health Sciences › Medicine › Infectious Diseases › Streptococcal Infections and Treatments
Health Sciences › Medicine › Surgery › Wound Healing and Treatments
Keywords: cathelicidin, LL-37, cramps, Streptococcus pyogenes, skin wounds, wound infection, antimicrobial peptides, innate immunity, keratinocytes, granulocytes, skin
MeSH terms: Amino Acid Sequence, Animals, Female, Humans, Male, Mice, Inbred C57BL, Molecular Sequence Data, Proteins, RNA, Messenger, Skin, Streptococcal Infections, Streptococcus pyogenes, Wound Healing, Keratinocytes, Gene Expression, Antimicrobial Cationic Peptides, Mice, Cathelicidins

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Cutaneous Injury Induces the Release of Cathelicidin Anti-Microbial Peptides Active Against Group A Streptococcus

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