Linked Life Data

19162067

Source:http://linkedlifedata.com/resource/pubmed/id/19162067

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2009-3-3
pubmed:abstractText
Psoriasin, a member of the S100 family of calcium-binding proteins (S100A7) is highly upregulated in the skin of psoriasis patients. As it has recently been found to exhibit antimicrobial activity, an important role of psoriasin in surface defence has been suggested. The similarity of the three-dimensional structures of psoriasin and amoebapore A, an ancient antimicrobial, pore-forming peptide from Entamoeba histolytica, intrigued us to investigate whether the human psoriasin is also able to permeabilize bacterial membranes. Here, we demonstrate that psoriasin exerts pore-forming activity at pH values below 6 demonstrating that disruption of microbial membranes is the basis of its antimicrobial activity at low pH. Furthermore, the killing activity of psoriasin shows pH-dependent target specificity. At neutral pH, the Gram-negative bacterium E. coli is killed apparently without compromising its membrane, whereas at low pH exclusively the Gram-positive bacterium B. megaterium is killed by permeabilization of its cytoplasmic membrane.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
1879-0089
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
33
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
740-6
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
The human antimicrobial protein psoriasin acts by permeabilization of bacterial membranes.
pubmed:affiliation
Institute of Biochemistry, University of Kiel, Olshausenstr. 40, 24098 Kiel, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't