The plausible role of antimicrobial peptides in periodontal disease

© 2012 Nova Science Publishers, Inc. In this review article, a background of two families of antimicrobial peptides, including defensin and cathelicidin, and their role in periodontal disease will be discussed in detail. Members of the defensin family are cysteine-rich peptides, synthesized by plant...

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Main Authors: Sakornrat Khongkhunthian, Vichai Reutrakul, Suttichai Krisanaprakornkit
Format: Book
Published: 2018
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Online Access:https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85048681793&origin=inward
http://cmuir.cmu.ac.th/jspui/handle/6653943832/51963
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Institution: Chiang Mai University
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spelling th-cmuir.6653943832-519632018-09-04T06:12:31Z The plausible role of antimicrobial peptides in periodontal disease Sakornrat Khongkhunthian Vichai Reutrakul Suttichai Krisanaprakornkit Medicine © 2012 Nova Science Publishers, Inc. In this review article, a background of two families of antimicrobial peptides, including defensin and cathelicidin, and their role in periodontal disease will be discussed in detail. Members of the defensin family are cysteine-rich peptides, synthesized by plants, insects, and mammals. These peptides vary in length and in the number of disulfide bonds, and have a beta-sheet structure. In the oral cavity, four alpha-defensins are synthesized and stored in neutrophil granules, which are converted into active peptides by proteolytic processing, while three human betadefensins (hBDs), hBD-1, hBD-2, and hBD-3, are predominantly produced by oral epithelial cells. The only member of the cathelicidin family found in humans is LL-37, an alpha-helical peptide that contains 37 amino acids and begins with two leucines at its NH3-terminus. LL-37 is derived from enzymatic cleavage of a precursor peptide, namely, human cationic antimicrobial peptide 18. Clinically, differential expression of antimicrobial peptides has been reported in specific types of periodontal disease, and their presence has been shown in saliva and gingival crevicular fluid. Current evidence suggests that alpha-defensins, beta-defensins, and LL-37 have distinct, but overlapping, roles in antimicrobial and pro-inflammatory activities. Several studies have shown antimicrobial activities of hBD-2, hBD- 3, and LL-37 against several periodontal pathogens, suggesting their potential role as antimicrobial agents for periodontal disease. Although researchers initially focused their attention on antimicrobial activities, it is now becoming evident that defensins and LL-37 are multifunctional molecules that mediate various host immune responses, and may thus represent essential molecules of innate immunity in periodontal disease. 2018-09-04T06:12:31Z 2018-09-04T06:12:31Z 2012-01-01 Book 2-s2.0-85048681793 https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85048681793&origin=inward http://cmuir.cmu.ac.th/jspui/handle/6653943832/51963
institution Chiang Mai University
building Chiang Mai University Library
country Thailand
collection CMU Intellectual Repository
topic Medicine
spellingShingle Medicine
Sakornrat Khongkhunthian
Vichai Reutrakul
Suttichai Krisanaprakornkit
The plausible role of antimicrobial peptides in periodontal disease
description © 2012 Nova Science Publishers, Inc. In this review article, a background of two families of antimicrobial peptides, including defensin and cathelicidin, and their role in periodontal disease will be discussed in detail. Members of the defensin family are cysteine-rich peptides, synthesized by plants, insects, and mammals. These peptides vary in length and in the number of disulfide bonds, and have a beta-sheet structure. In the oral cavity, four alpha-defensins are synthesized and stored in neutrophil granules, which are converted into active peptides by proteolytic processing, while three human betadefensins (hBDs), hBD-1, hBD-2, and hBD-3, are predominantly produced by oral epithelial cells. The only member of the cathelicidin family found in humans is LL-37, an alpha-helical peptide that contains 37 amino acids and begins with two leucines at its NH3-terminus. LL-37 is derived from enzymatic cleavage of a precursor peptide, namely, human cationic antimicrobial peptide 18. Clinically, differential expression of antimicrobial peptides has been reported in specific types of periodontal disease, and their presence has been shown in saliva and gingival crevicular fluid. Current evidence suggests that alpha-defensins, beta-defensins, and LL-37 have distinct, but overlapping, roles in antimicrobial and pro-inflammatory activities. Several studies have shown antimicrobial activities of hBD-2, hBD- 3, and LL-37 against several periodontal pathogens, suggesting their potential role as antimicrobial agents for periodontal disease. Although researchers initially focused their attention on antimicrobial activities, it is now becoming evident that defensins and LL-37 are multifunctional molecules that mediate various host immune responses, and may thus represent essential molecules of innate immunity in periodontal disease.
format Book
author Sakornrat Khongkhunthian
Vichai Reutrakul
Suttichai Krisanaprakornkit
author_facet Sakornrat Khongkhunthian
Vichai Reutrakul
Suttichai Krisanaprakornkit
author_sort Sakornrat Khongkhunthian
title The plausible role of antimicrobial peptides in periodontal disease
title_short The plausible role of antimicrobial peptides in periodontal disease
title_full The plausible role of antimicrobial peptides in periodontal disease
title_fullStr The plausible role of antimicrobial peptides in periodontal disease
title_full_unstemmed The plausible role of antimicrobial peptides in periodontal disease
title_sort plausible role of antimicrobial peptides in periodontal disease
publishDate 2018
url https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85048681793&origin=inward
http://cmuir.cmu.ac.th/jspui/handle/6653943832/51963
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