TY - JOUR
T1 - The human cathelicidin hCAP18/LL-37
T2 - A multifunctional peptide involved in mycobacterial infections
AU - Méndez-Samperio, Patricia
N1 - Funding Information:
This work was supported in part by grant 20101177 from the Secretaría de Investigación y Posgrado (SIP) del IPN. PMS is a research of COFAA, EDI and SNI.
PY - 2010/9
Y1 - 2010/9
N2 - Antimicrobial peptides are predominantly small cationic polypeptides that are classified together on the basis of these molecules to directly kill or inhibit the growth of microorganisms including mycobacteria, and to activate mechanisms of cellular and adaptive immunity. Various families of antimicrobial peptides have been identified, including the cathelicidins. The cathelicidin family is characterised by a conserved N-terminal cathelin domain and a variable C-terminal antimicrobial domain that can be released from the precursor protein after cleavage by proteinases. LL-37 is the C-terminal part of the only human cathelicidin identified to date called human cationic antimicrobial protein (hCAP18), which is mainly expressed by neutrophils and epithelial cells. The cathelicidin hCAP18/LL-37 is a multifunctional molecule that may mediate various host responses, including bactericidal action, chemotaxis, epithelial cell activation, angiogenesis, epithelial wound repair and activation of chemokine secretion. The antimicrobial peptide LL-37 is produced from human cells during infection of mycobacteria and exerts a microbicidal effect. The discussion will (1) describe recent work on the antimicrobial and immunomodulatory functions of the cathelicidin hCAP18/LL-37, (2) highlight the effectiveness of the cathelicidin hCAP18/LL-37 as a potent component in antimycobacterial immune responses and (3) summarise current progress in the understanding of the therapeutic application of hCAP18/LL-37 and its derivates antimicrobial peptides in mycobacterial infection.
AB - Antimicrobial peptides are predominantly small cationic polypeptides that are classified together on the basis of these molecules to directly kill or inhibit the growth of microorganisms including mycobacteria, and to activate mechanisms of cellular and adaptive immunity. Various families of antimicrobial peptides have been identified, including the cathelicidins. The cathelicidin family is characterised by a conserved N-terminal cathelin domain and a variable C-terminal antimicrobial domain that can be released from the precursor protein after cleavage by proteinases. LL-37 is the C-terminal part of the only human cathelicidin identified to date called human cationic antimicrobial protein (hCAP18), which is mainly expressed by neutrophils and epithelial cells. The cathelicidin hCAP18/LL-37 is a multifunctional molecule that may mediate various host responses, including bactericidal action, chemotaxis, epithelial cell activation, angiogenesis, epithelial wound repair and activation of chemokine secretion. The antimicrobial peptide LL-37 is produced from human cells during infection of mycobacteria and exerts a microbicidal effect. The discussion will (1) describe recent work on the antimicrobial and immunomodulatory functions of the cathelicidin hCAP18/LL-37, (2) highlight the effectiveness of the cathelicidin hCAP18/LL-37 as a potent component in antimycobacterial immune responses and (3) summarise current progress in the understanding of the therapeutic application of hCAP18/LL-37 and its derivates antimicrobial peptides in mycobacterial infection.
KW - Antimicrobial peptides
KW - Cathelicidin
KW - Innate immunity
KW - LL-37
KW - Mycobacteria
UR - http://www.scopus.com/inward/record.url?scp=77955654919&partnerID=8YFLogxK
U2 - 10.1016/j.peptides.2010.06.016
DO - 10.1016/j.peptides.2010.06.016
M3 - Artículo de revisión
C2 - 20600427
SN - 0196-9781
VL - 31
SP - 1791
EP - 1798
JO - Peptides
JF - Peptides
IS - 9
ER -