PMID- 15821901
OWN - NLM
STAT- MEDLINE
DCOM- 20051214
LR  - 20181113
IS  - 0946-2716 (Print)
IS  - 0946-2716 (Linking)
VI  - 83
IP  - 8
DP  - 2005 Aug
TI  - Human defensins.
PG  - 587-95
AB  - Antimicrobial peptides are small, cationic, amphiphilic peptides of 12-50 amino 
      acids with microbicidal activity against both bacteria and fungi. The eukaryotic 
      antimicrobial peptides may be divided into four distinct groups according to 
      their structural features: cysteine-free alpha-helices, extended cysteine-free 
      alpha-helices with a predominance of one or two amino acids, loop structures with 
      one intramolecular disulfide bond, and beta-sheet structures which are stabilised 
      by two or three intramolecular disulfide bonds. Mammalian defensins are part of 
      the last-mentioned group. The mammalian defensins can be subdivided into three 
      main classes according to their structural differences: the alpha-defensins, 
      beta-defensins and the recently described theta-defensins. Mammalian 
      alpha-defensins are predominantly found in neutrophils and in small intestinal 
      Paneth cells, whereas mammalian beta-defensins have been isolated from both 
      leukocytes and epithelial cells. Recently, two novel human beta-defensins, human 
      beta-defensin-3 (HBD-3), and human beta-defensin-4 (HBD-4) have been discovered. 
      Similar to HBD-1 and HBD-2, HBD-3 has microbicidal activity towards the 
      Gram-negative bacteria (Pseudomonas aeruginosa, Escherichia coli) and the yeasts 
      Candida albicans and Malassezia furfur. In addition, HBD-3 kills Gram-positive 
      bacteria such as Streptococcus pyogenes or Staphylococcus aureus, including 
      multi-resistant S. aureus strains, and even vancomycin-resistant Enterococcus 
      faecium. In contrast to HBD-1 and HBD-2, significant expression of HBD-3 has been 
      demonstrated in non-epithelial tissues, such as leukocytes, heart and skeletal 
      muscle. HBD-4 is expressed in certain epithelia and in neutrophils. Its 
      bactericidal activity against P. aeruginosa is stronger than that of the other 
      known beta-defensins. Here we present an overview of human antimicrobial peptides 
      with some emphasis on their antifungal properties.
FAU - Schneider, Josef Johann
AU  - Schneider JJ
AD  - Klinik und Poliklinik fur Dermatologie und Allergologie, 
      Ludwig-Maximilians-Universitat Munchen, Frauenlobstrasse 9-11, 80337 Munich, 
      Germany. josefschneider@gmx.de
FAU - Unholzer, Angela
AU  - Unholzer A
FAU - Schaller, Martin
AU  - Schaller M
FAU - Schafer-Korting, Monika
AU  - Schafer-Korting M
FAU - Korting, Hans Christian
AU  - Korting HC
LA  - eng
PT  - Journal Article
PT  - Review
DEP - 20050409
PL  - Germany
TA  - J Mol Med (Berl)
JT  - Journal of molecular medicine (Berlin, Germany)
JID - 9504370
RN  - 0 (Anti-Infective Agents)
RN  - 0 (Antimicrobial Cationic Peptides)
RN  - 0 (Defensins)
SB  - IM
MH  - Animals
MH  - Anti-Infective Agents/classification/metabolism
MH  - Antimicrobial Cationic Peptides/pharmacology
MH  - Chemistry, Pharmaceutical
MH  - Defensins/classification/*metabolism
MH  - Humans
RF  - 99
EDAT- 2005/04/12 09:00
MHDA- 2005/12/15 09:00
CRDT- 2005/04/12 09:00
PHST- 2004/09/09 00:00 [received]
PHST- 2005/02/02 00:00 [accepted]
PHST- 2005/04/12 09:00 [pubmed]
PHST- 2005/12/15 09:00 [medline]
PHST- 2005/04/12 09:00 [entrez]
AID - 10.1007/s00109-005-0657-1 [doi]
PST - ppublish
SO  - J Mol Med (Berl). 2005 Aug;83(8):587-95. doi: 10.1007/s00109-005-0657-1. Epub 
      2005 Apr 9.