| pubmed-article:15963828 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15963828 | lifeskim:mentions | umls-concept:C0008051 | lld:lifeskim |
| pubmed-article:15963828 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:15963828 | lifeskim:mentions | umls-concept:C1136254 | lld:lifeskim |
| pubmed-article:15963828 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:15963828 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:15963828 | pubmed:issue | 3-4 | lld:pubmed |
| pubmed-article:15963828 | pubmed:dateCreated | 2005-6-20 | lld:pubmed |
| pubmed-article:15963828 | pubmed:abstractText | Cathelicidins, antimicrobial peptides with broad spectrum activity, have been almost exclusively found in mammals. Here, we report the cloning of a novel avian cathelicidin, chicken myeloid antimicrobial peptide 27 (CMAP27) from chicken bone marrow cells. A combined expressed sequence tag (EST) and genomic based search revealed a cathelicidin-like gene located at the terminus of chromosome 2. Reverse transcriptase-polymerase chain reaction (RT-PCR) and 5'RACE techniques resulted in a 154 amino acid prepropeptide, homologous to chicken cathelicidin 1 (51%) and most similar to alpha-helical myeloid antibacterial peptides (MAPs; 29-33%). A putative elastase cleavage site (LVQRG/RF) suggests the production of a 27 amino acid antimicrobial peptide, predicted to adopt an alpha-helical configuration followed by a hydrophobic tail. Comparative analyses between antimicrobial peptide domains showed marked similarity between CMAP27 and MAP members of the bovidae family, but not with the alpha-helical chicken cathelicidin 1. Strongest expression of CMAP27 mRNA was found in myeloid/lymphoid tissues, testis and uropygial gland. In accordance with the phylogenetic tree analysis, these findings support the theory of a common ancestral cathelicidin gene and suggest an important role for cathelicidins in chicken innate host defense. | lld:pubmed |
| pubmed-article:15963828 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15963828 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15963828 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15963828 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15963828 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15963828 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15963828 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15963828 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:15963828 | pubmed:issn | 0165-2427 | lld:pubmed |
| pubmed-article:15963828 | pubmed:author | pubmed-author:HaagsmanHenk... | lld:pubmed |
| pubmed-article:15963828 | pubmed:author | pubmed-author:VeldhuizenEdw... | lld:pubmed |
| pubmed-article:15963828 | pubmed:author | pubmed-author:van... | lld:pubmed |
| pubmed-article:15963828 | pubmed:author | pubmed-author:van... | lld:pubmed |
| pubmed-article:15963828 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15963828 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:15963828 | pubmed:volume | 106 | lld:pubmed |
| pubmed-article:15963828 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15963828 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15963828 | pubmed:pagination | 321-7 | lld:pubmed |
| pubmed-article:15963828 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
| pubmed-article:15963828 | pubmed:meshHeading | pubmed-meshheading:15963828... | lld:pubmed |
| pubmed-article:15963828 | pubmed:meshHeading | pubmed-meshheading:15963828... | lld:pubmed |
| pubmed-article:15963828 | pubmed:meshHeading | pubmed-meshheading:15963828... | lld:pubmed |
| pubmed-article:15963828 | pubmed:meshHeading | pubmed-meshheading:15963828... | lld:pubmed |
| pubmed-article:15963828 | pubmed:meshHeading | pubmed-meshheading:15963828... | lld:pubmed |
| pubmed-article:15963828 | pubmed:meshHeading | pubmed-meshheading:15963828... | lld:pubmed |
| pubmed-article:15963828 | pubmed:meshHeading | pubmed-meshheading:15963828... | lld:pubmed |
| pubmed-article:15963828 | pubmed:meshHeading | pubmed-meshheading:15963828... | lld:pubmed |
| pubmed-article:15963828 | pubmed:meshHeading | pubmed-meshheading:15963828... | lld:pubmed |
| pubmed-article:15963828 | pubmed:meshHeading | pubmed-meshheading:15963828... | lld:pubmed |
| pubmed-article:15963828 | pubmed:meshHeading | pubmed-meshheading:15963828... | lld:pubmed |
| pubmed-article:15963828 | pubmed:meshHeading | pubmed-meshheading:15963828... | lld:pubmed |
| pubmed-article:15963828 | pubmed:meshHeading | pubmed-meshheading:15963828... | lld:pubmed |
| pubmed-article:15963828 | pubmed:meshHeading | pubmed-meshheading:15963828... | lld:pubmed |
| pubmed-article:15963828 | pubmed:meshHeading | pubmed-meshheading:15963828... | lld:pubmed |
| pubmed-article:15963828 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:15963828 | pubmed:articleTitle | CMAP27, a novel chicken cathelicidin-like antimicrobial protein. | lld:pubmed |
| pubmed-article:15963828 | pubmed:affiliation | Department of Public Health and Food Safety, Graduate School of Animal Health, Faculty of Veterinary Medicine, Utrecht University, 3508 TD Utrecht, The Netherlands. | lld:pubmed |
| pubmed-article:15963828 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15963828 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:420407 | entrezgene:pubmed | pubmed-article:15963828 | lld:entrezgene |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:15963828 | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:15963828 | lld:pubmed |
