Antimicrobial peptides

被引:288
作者
Izadpanah, A
Gallo, RL
机构
[1] Univ Calif San Diego, Dept Med, Div Dermatol, San Diego, CA 92103 USA
[2] Vet Adm San Diego Healthcare Syst, San Diego, CA USA
关键词
D O I
10.1016/j.jaad.2004.08.026
中图分类号
R75 [皮肤病学与性病学];
学科分类号
100206 ;
摘要
Antimicrobial peptides (AMPs) are small molecular weight proteins with broad spectrum antimicrobial activity against bacteria, viruses, and fungi. These evolutionarily conserved peptides are usually positively charged and have both a hydrophobic and hydrophilic side that enables the molecule to be soluble in aqueous environments yet also enter lipid-rich membranes. Once in a target microbial membrane, the peptide kills target cells through diverse mechanisms. Cathelicidins and defensins are major groups of epidermal AMPs. Decreased levels of these peptides have been noted for patients with atopic dermatitis and Kostmann's syndrome, a congenital neutropenia. In addition to important antimicrobial properties, growing evidence indicates that AMI's alter the host immune response through receptor-dependent interactions. AMPs have been shown to be important in such diverse functions as angiogenesis, wound healing, and chemotaxis. As our knowledge of AMP biology expands, the precise role and relevance of these peptides will be better elucidated. Learning objective: At the completion of this learning activity, participants should be able to distinguish the different classes of antimicrobial peptides. Participants should recognize the antimicrobial properties and unique immunomodulatory effects of various antimicrobial peptides and their currently understood association in relevant skin diseases.
引用
收藏
页码:381 / 392
页数:12
相关论文
共 74 条
[1]   ISOLATION OF 3 ANTIBACTERIAL PEPTIDES FROM PIG INTESTINE - GASTRIC-INHIBITORY POLYPEPTIDE(7-42), DIAZEPAM-BINDING INHIBITOR(32-86) AND A NOVEL FACTOR, PEPTIDE-3910 [J].
AGERBERTH, B ;
BOMAN, A ;
ANDERSSON, M ;
JORNVALL, H ;
MUTT, V ;
BOMAN, HG .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1993, 216 (02) :623-629
[2]   AMINO-ACID-SEQUENCE OF PR-39 - ISOLATION FROM PIG INTESTINE OF A NEW MEMBER OF THE FAMILY OF PROLINE-ARGININE-RICH ANTIBACTERIAL PEPTIDES [J].
AGERBERTH, B ;
LEE, JY ;
BERGMAN, T ;
CARLQUIST, M ;
BOMAN, HG ;
MUTT, V ;
JORNVALL, H .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1991, 202 (03) :849-854
[3]   Granulysin crystal structure and a structure-derived lytic mechanism [J].
Anderson, DH ;
Sawaya, MR ;
Cascio, D ;
Ernst, W ;
Modlin, R ;
Krensky, A ;
Eisenberg, D .
JOURNAL OF MOLECULAR BIOLOGY, 2003, 325 (02) :355-365
[4]   The lipopolysaccharide of Bordetella bronchiseptica acts as a protective shield against antimicrobial peptides [J].
Banemann, A ;
Deppisch, H ;
Gross, R .
INFECTION AND IMMUNITY, 1998, 66 (12) :5607-5612
[5]   Human α-defensin 1 (HNP-1) inhibits adenoviral infection in vitro [J].
Bastian, A ;
Schäfer, H .
REGULATORY PEPTIDES, 2001, 101 (1-3) :157-161
[6]  
Befus AD, 1999, J IMMUNOL, V163, P947
[7]   Innate immunity and the normal microflora [J].
Boman, HG .
IMMUNOLOGICAL REVIEWS, 2000, 173 :5-16
[8]  
BOMAN HG, 1995, ANNU REV IMMUNOL, V13, P61, DOI 10.1146/annurev.iy.13.040195.000425
[9]   MECHANISMS OF ACTION ON ESCHERICHIA-COLI OF CECROPIN-P1 AND PR-39, 2 ANTIBACTERIAL PEPTIDES FROM PIG INTESTINE [J].
BOMAN, HG ;
AGERBERTH, B ;
BOMAN, A .
INFECTION AND IMMUNITY, 1993, 61 (07) :2978-2984
[10]  
Bülow E, 2002, J LEUKOCYTE BIOL, V72, P147