REVIEW ARTICLE
Activity of Antimicrobial Peptide; Cathelicidin, on Bacterial Infection
Ami Febriza1, *, Mochammad Hatta2, Rosdiana Natzir3, Vivien N.A. Kasim4, Hasta H. Idrus5
Article Information
Identifiers and Pagination:
Year: 2019Volume: 13
First Page: 45
Last Page: 53
Publisher ID: TOBIOCJ-13-45
DOI: 10.2174/1874091X01913010045
Article History:
Received Date: 12/01/2019Revision Received Date: 15/05/2019
Acceptance Date: 22/05/2019
Electronic publication date: 30/06/2019
Collection year: 2019
open-access license: This is an open access article distributed under the terms of the Creative Commons Attribution 4.0 International Public License (CC-BY 4.0), a copy of which is available at: https://creativecommons.org/licenses/by/4.0/legalcode. This license permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Abstract
Antimicrobial peptide is an effector molecule from the natural immune system which plays a central role in defense as an antimicrobial. Cathelicidin is one of the antimicrobial peptides. Human only has one cathelicidin antimicrobial peptide called LL-37 or hCAP18. The detailed mechanism on CAMP (Cathelicidin Antimicrobial Peptide) gene regulation is still unknown, however, cathelicidin is found to have upregulation when there is bacterial infection. The most effective expression inducer of CAMP gene is 1,25-dihydroxyvitamin D3 (1,25(OH)2 D3), which is the active form of vitamin D. Vitamin D mediates cathelicidin synthesis through the expression of Vitamin D Receptor (VDR), then the interaction activates CAMP gene to express cathelicidin. The work mechanisms of cathelicidin against bacterial infection include damaging the bacterial cell membrane, inducing autophagy process of macrophage cell, neutralizing LPS produced by bacteria, and chemotactic activities of PMNs, monocytes and lymphocytes.
