|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
3
|
|
pubmed:dateCreated |
1999-10-12
|
|
pubmed:databankReference |
|
|
pubmed:abstractText |
Cathelicidins are precursors of defense peptides of the innate immunity and are widespread in mammals. Their structure comprises a conserved prepropiece and an antimicrobial domain that is structurally varied both intra- and inter-species. We investigated the complexity of the cathelicidin family in horse by a reverse transcription-PCR-based cloning strategy of myeloid mRNA and by Southern and Western analyses. Three novel cathelicidin sequences were deduced from bone marrow mRNA and designated equine cathelicidins eCATH-1, eCATH-2 and eCATH-3. Putative antimicrobial domains of 26, 27 and 40 residues with no significant sequence homology to other peptides were inferred at the C-terminus of the sequences. Southern analysis of genomic DNA using a probe based on the cathelicidin-conserved propiece revealed a polymorphic DNA region with several hybridization-positive fragments and suggested the presence of additional genes. A null eCATH-1 allele was also demonstrated with a frequency of 0.71 in the horse population analyzed and low amounts of eCATH-1-specific mRNA were found in myeloid cells of gene-positive animals. A Western analysis using antibodies to synthetic eCATH peptides revealed the presence of eCATH-2 and eCATH-3 propeptides, but not of eCATH-1-related polypeptides, in horse neutrophil granules and in the secretions of phorbol myristate acetate-stimulated neutrophils. These results thus suggest that eCATH-2 and eCATH-3 are functional genes, whereas eCATH-1 is unable to encode a polypeptide.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Sep
|
|
pubmed:issn |
0014-5793
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
3
|
|
pubmed:volume |
457
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
459-64
|
|
pubmed:dateRevised |
2010-11-18
|
|
pubmed:meshHeading |
pubmed-meshheading:10471829-Amino Acid Sequence,
pubmed-meshheading:10471829-Animals,
pubmed-meshheading:10471829-Antimicrobial Cationic Peptides,
pubmed-meshheading:10471829-Base Sequence,
pubmed-meshheading:10471829-Blood Proteins,
pubmed-meshheading:10471829-Blotting, Southern,
pubmed-meshheading:10471829-Blotting, Western,
pubmed-meshheading:10471829-Cathelicidins,
pubmed-meshheading:10471829-Cytoplasmic Granules,
pubmed-meshheading:10471829-Horses,
pubmed-meshheading:10471829-Leukocytes,
pubmed-meshheading:10471829-Molecular Sequence Data,
pubmed-meshheading:10471829-Multigene Family,
pubmed-meshheading:10471829-Neutrophils,
pubmed-meshheading:10471829-Protein Precursors,
pubmed-meshheading:10471829-Reference Values,
pubmed-meshheading:10471829-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:10471829-Sequence Analysis,
pubmed-meshheading:10471829-Sequence Homology, Amino Acid,
pubmed-meshheading:10471829-Short Interspersed Nucleotide Elements,
pubmed-meshheading:10471829-Tetradecanoylphorbol Acetate,
pubmed-meshheading:10471829-Transcription, Genetic
|
|
pubmed:year |
1999
|
|
pubmed:articleTitle |
Novel cathelicidins in horse leukocytes(1).
|
|
pubmed:affiliation |
Laboratorio Nazionale Consorzio Interuniversitario Biotecnologie, AREA Science Park, Padriciano, I-34012, Trieste, Italy.
|
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
