Linked Life Data

12713586

Source:http://linkedlifedata.com/resource/pubmed/id/12713586

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2003-4-25
pubmed:abstractText
Cathelicidins are a class of small cationic peptide antibiotics that are expressed in skin and in other epithelial cells and are an active component of mammalian innate immunity. Human cathelicidin (hCAP18/LL-37) consists of a conserved prosequence called the cathelin-like domain and a C-terminal peptide named LL-37. To date, our understanding of the cathelin-like domain was very limited. To bring insight into the function of this evolutionarily conserved prosequence, we produced recombinant human cathelin-like protein and full-length hCAP18/LL-37 in Escherichia coli. As the cathelin-like protein shares homology with the cystatin family of cysteine protease inhibitors, we first analyzed the effect of the cathelin-like recombinant protein on the cysteine protease cathepsin L. We found that the cathelin-like protein inhibited protease activity. Next, we tested the cathelin-like protein for antimicrobial activity using solid phase radial diffusion and liquid phase killing assays. The cathelin-like prosequence, but not full-length hCAP18/LL-37, killed human pathogens including E. coli and methicillin-resistant Staphylococcus aureus at concentrations ranging from 16 to 32 microM. Together these findings suggest that after proteolytic cleavage the cathelin-like domain can contribute to innate host defense through inhibition of bacterial growth and limitation of cysteine-proteinase-mediated tissue damage. As these dual functions are complementary to the LL-37 peptide released from the C-terminus of full-length hCAP18/LL-37, human cathelicidin represents an elegant multifunctional effector molecule for innate immune defense of the skin.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0022-202X
pubmed:author
pubmed:issnType
Print
pubmed:volume
120
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
810-6
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed-meshheading:12713586-Anti-Bacterial Agents, pubmed-meshheading:12713586-Anti-Infective Agents, pubmed-meshheading:12713586-Antimicrobial Cationic Peptides, pubmed-meshheading:12713586-Cathelicidins, pubmed-meshheading:12713586-Drug Resistance, pubmed-meshheading:12713586-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:12713586-Endopeptidases, pubmed-meshheading:12713586-Enzyme Inhibitors, pubmed-meshheading:12713586-Escherichia coli, pubmed-meshheading:12713586-Genetic Vectors, pubmed-meshheading:12713586-Humans, pubmed-meshheading:12713586-Protein Structure, Tertiary, pubmed-meshheading:12713586-Recombinant Proteins, pubmed-meshheading:12713586-Spectrometry, Mass, Matrix-Assisted Laser..., pubmed-meshheading:12713586-Staphylococcus aureus, pubmed-meshheading:12713586-Time Factors
pubmed:year
2003
pubmed:articleTitle
Antimicrobial and protease inhibitory functions of the human cathelicidin (hCAP18/LL-37) prosequence.
pubmed:affiliation
Department of Medicine and Pediatrics, Division of Dermatology, University of California at San Diego and VA San Diego Healthcare System, 92161, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.