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PubMed · 7543446

Porcine E-selectin: cloning and functional characterization.

Y T Tsang·P E Stephens·S T Licence·D O Haskard·R M Binns·M K Robinson
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Abstract

E-selectin, a member of the selectin family, is believed to play an important role in mediating the initial adhesive events between leucocytes and the endothelium during inflammation. A monoclonal antibody against human E-selectin was found to cross-react with the porcine equivalent, a glycoprotein of 92,000 MW. Isolation of the cDNA for porcine E-selectin showed that it was 71% homologous with human E-selectin but had two less short consensus repeats. The porcine adhesion molecule could also support the adhesion of both porcine and human neutrophils. Expression of E-selectin on interleukin-1 alpha (IL-1 alpha)- or tumour necrosis factor-alpha (TNF-alpha)-activated porcine aortic endothelial cells in culture was prolonged, persisting for up to 48 hr. Binding studies using a chimeric molecule consisting of the lectin domain of porcine E-selectin and the epidermal growth factor (EGF) domain of human E-selectin fused to the human IgG constant region, further characterized porcine E-selectin as recognizing mainly granulocytic leucocytes and a subpopulation of lymphocytes.

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AnimalsAntibodies, MonoclonalCell Adhesion MoleculesCells, CulturedCross ReactionsDNA, ComplementaryE-SelectinEndothelium, VascularHumansInterleukin-1KineticsLeukocytesMolecular Sequence DataRecombinant ProteinsSpecies SpecificitySwineTumor Necrosis Factor-alphaJournal ArticleResearch Support, Non-U.S. Gov't

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Y T Tsang, P E Stephens, S T Licence, D O Haskard, R M Binns, M K Robinson. 1995. Porcine E-selectin: cloning and functional characterization.. https://pubmed.ncbi.nlm.nih.gov/7543446/

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