Document Detail


Antimicrobial skin peptides and proteins.
MedLine Citation:
PMID:  16416029     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Human skin is permanently exposed to microorganisms, but rarely infected. One reason for this natural resistance might be the existence of a 'chemical barrier' consisting in constitutively and inducibly produced antimicrobial peptides and proteins (AMPs). Many of these AMPs can be induced in vitro by proinflammatory cytokines or bacteria. Apart from being expressed in vivo in inflammatory lesions, some AMPs are also focally expressed in skin in the absence of inflammation. This suggests that non-inflammatory stimuli of endogenous and/or exogenous origin can also stimulate AMP synthesis without inflammation. Such mediators might be ideal 'immune stimulants' to induce only the innate antimicrobial skin effector molecules without causing inflammation.
Authors:
J M Schröder; J Harder
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Publication Detail:
Type:  Journal Article; Review    
Journal Detail:
Title:  Cellular and molecular life sciences : CMLS     Volume:  63     ISSN:  1420-682X     ISO Abbreviation:  Cell. Mol. Life Sci.     Publication Date:  2006 Feb 
Date Detail:
Created Date:  2006-03-21     Completed Date:  2006-04-21     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  9705402     Medline TA:  Cell Mol Life Sci     Country:  Switzerland    
Other Details:
Languages:  eng     Pagination:  469-86     Citation Subset:  IM    
Affiliation:
Department of Dermatology, University-Hospital Schleswig-Holstein, Campus Kiel, Schittenhelmstr. 7, 24105 Kiel, Germany. jschroeder@dermatology.uni-kiel.de
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MeSH Terms
Descriptor/Qualifier:
Animals
Anti-Bacterial Agents / biosynthesis*
Antimicrobial Cationic Peptides / metabolism*
Calcium-Binding Proteins / metabolism
Epidermis / metabolism*
Humans
Immunity, Innate
Muramidase / metabolism
Peptides / metabolism
Ribonucleases / metabolism
S100 Proteins
Chemical
Reg. No./Substance:
0/Anti-Bacterial Agents; 0/Antimicrobial Cationic Peptides; 0/Calcium-Binding Proteins; 0/Peptides; 0/S100 Proteins; 0/S100A7 protein, human; 0/dermcidin; EC 3.1.-/Ribonucleases; EC 3.1.27.-/Ribonuclease 7; EC 3.2.1.17/Muramidase

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