Source:http://linkedlifedata.com/resource/pubmed/id/15674735
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2005-1-27
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pubmed:databankReference | |
pubmed:abstractText |
P-selectin glycoprotein ligand-1 (PSGL-1, CD162) is a dimeric, mucin-like, transmembrane glycoprotein constitutively expressed on leukocytes. A high baseline level of P-selectin expression in circulating equine platelets suggests a primed state toward inflammation and thrombosis via P-selectin/PSGL-1 adhesion. To investigate the potential role of equine P-selectin in these events, we first identified the cDNA sequence of equine PSGL-1 (ePSGL-1) using degenerate PCR and RACE-PCR and then compared the predicted sequence with that of human PSGL-1 (hPSGL-1). ePSGL-1 protein subunit is predicted to be 43 kDa and composed of 420 amino acids with a predicted 18-amino-acid signal sequence showing 78% homology to hPSGL-1. Previously published work has shown that binding of P-selectin requires sulfation of at least one of three tyrosines and O-glycosylation of one threonine in the N-terminus of human PSGL-1. However, the corresponding domain in ePSGL-1, spanning residues 19-43, contains only one tyrosine in the vicinity of two threonines at positions 25 and 41. ePSGL-1 contains 14 threonine/serine-rich decameric repeats as compared to hPSGL-1 which contains 14-16 threonine-rich decameric repeats. The transmembrane and cytoplasmic domains display 91% and 74% homology to corresponding human PSGL-1 domains, respectively. In summary, there is 71% homology in comparing the open reading frame (ORF) of ePSGL-1 with that of hPSGL-1. The greatest homologies between species exist in the transmembrane domain and cytoplasmic tail while substantial differences exist in the extracellular domain.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0938-8990
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
16
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
66-71
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:15674735-Amino Acid Sequence,
pubmed-meshheading:15674735-Animals,
pubmed-meshheading:15674735-Base Sequence,
pubmed-meshheading:15674735-Horses,
pubmed-meshheading:15674735-Humans,
pubmed-meshheading:15674735-Ligands,
pubmed-meshheading:15674735-Membrane Glycoproteins,
pubmed-meshheading:15674735-Molecular Sequence Data,
pubmed-meshheading:15674735-P-Selectin,
pubmed-meshheading:15674735-Polymerase Chain Reaction,
pubmed-meshheading:15674735-Sequence Homology
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pubmed:year |
2005
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pubmed:articleTitle |
Identification of equine P-selectin glycoprotein ligand-1 (CD162).
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pubmed:affiliation |
Department of Medical Sciences, School of Veterinary Medicine, University of Wisconsin, Madison, Wisconsin, 53706-1102, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study
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