Cathelicidins - a family of multifunctional antimicrobial peptides

被引：365

作者：

Bals, R

Wilson, JM

机构：

[1] Univ Marburg, Div Pulm, Dept Internal Med, D-35043 Marburg, Germany

[2] Univ Penn, Inst Human Gene Therapy, Philadelphia, PA 19104 USA

来源：

CELLULAR AND MOLECULAR LIFE SCIENCES | 2003年 / 60卷 / 04期

关键词：

cathelicidin; antimicrobial peptide; host defence; innate immunity; resistance;

D O I：

10.1007/s00018-003-2186-9

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

One component of host defence at mucosal surfaces are epithelial-derived antimicrobial peptides. Cathelicidins are one family of antimicrobial peptides characterized by conserved pro-peptide sequences that have been identified in several mammalian species. LL-37/hCAP-18 is the only cathelicidin found in humans and is expressed in inflammatory and epithelial cells. Besides their direct antimicrobial function, cathelicidins have multiple roles as mediators of inflammation influencing diverse processes such as cell proliferation and migration, immune modulation, wound healing, angiogenesis and the release of cytokines and histamine. Finally, cathelicidin antimicrobial peptides qualify as prototypes of innovative drugs that may be used to treat infection and/or modulate the immune response. This review provides an overview of antimicrobial peptides of the cathelicidin family, the structures of their genes and peptides and their biological functions.

引用

收藏

页码：711 / 720

页数：10

相关论文

共 95 条

[61] Processing site and gene structure for the murine antimicrobial peptide CRAMP [J].

Pestonjamasp, VK ;

Huttner, KH ;

Gallo, RL .

PEPTIDES, 2001, 22 (10) :1643-1650

[62] A novel murine cathelin-like protein expressed in bone marrow [J].

Popsueva, AE ;

Zinovjeva, MV ;

Visser, JWM ;

Zijlmans, JMJM ;

Fibbe, WE ;

Belyavsky, AV .

FEBS LETTERS, 1996, 391 (1-2) :5-8

[63] PRIMARY STRUCTURE OF A NEW CYSTEINE PROTEINASE-INHIBITOR FROM PIG LEUKOCYTES [J].

RITONJA, A ;

KOPITAR, M ;

JERALA, R ;

TURK, V .

FEBS LETTERS, 1989, 255 (02) :211-214

[64] Structure of the bovine antimicrobial peptide indolicidin bound to dodecylphosphocholine and sodium dodecyl sulfate micelles [J].

Rozek, A ;

Friedrich, CL ;

Hancock, REW .

BIOCHEMISTRY, 2000, 39 (51) :15765-15774

[65] Synergistic activities of macrolide antibiotics against Pseudomonas aeruginosa, Burkholderia cepacia, Stenotrophomonas maltophilia, and Alcaligenes xylosoxidans isolated from patients with cystic fibrosis [J].

Saiman, L ;

Chen, YH ;

San Gabriel, P ;

Knirsch, C .

ANTIMICROBIAL AGENTS AND CHEMOTHERAPY, 2002, 46 (04) :1105-1107

[66] Increased levels of antimicrobial peptides in tracheal aspirates of newborn infants during infection [J].

Schaller-Bals, S ;

Schulze, A ;

Bals, R .

AMERICAN JOURNAL OF RESPIRATORY AND CRITICAL CARE MEDICINE, 2002, 165 (07) :992-995

[67] Novel cathelicidins in horse leukocytes [J].

Scocchi, M ;

Bontempo, D ;

Boscolo, S ;

Tomasinsig, L ;

Giulotto, E ;

Zanetti, M .

FEBS LETTERS, 1999, 457 (03) :459-464

[68] PROTEOLYTIC CLEAVAGE BY NEUTROPHIL ELASTASE CONVERTS INACTIVE STORAGE PROFORMS TO ANTIBACTERIAL BACTENECINS [J].

SCOCCHI, M ;

SKERLAVAJ, B ;

ROMEO, D ;

GENNARO, R .

EUROPEAN JOURNAL OF BIOCHEMISTRY, 1992, 209 (02) :589-595

[69] Modulation of Neisseria gonorrhoeae susceptibility to vertebrate antibacterial peptides due to a, member of the resistance/nodulation/division efflux pump family [J].

Shafer, WM ;

Qu, XD ;

Waring, AJ ;

Lehrer, RI .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1998, 95 (04) :1829-1833

[70] The role of protegrins and other elastase-activated polypeptides in the bactericidal properties of porcine inflammatory fluids [J].

Shi, JS ;

Ganz, T .

INFECTION AND IMMUNITY, 1998, 66 (08) :3611-3617

← 1 2 3 4 5 6 7 8 9 10 →