Evolutionary conservation of P-selectin glycoprotein ligand-1 primary structure and function.

Détails

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Etat: Public
Version: Final published version
ID Serval
serval:BIB_1350E79FFA3E
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Evolutionary conservation of P-selectin glycoprotein ligand-1 primary structure and function.
Périodique
BMC evolutionary biology
Auteur⸱e⸱s
Baïsse B., Galisson F., Giraud S., Schapira M., Spertini O.
ISSN
1471-2148 (Electronic)
ISSN-L
1471-2148
Statut éditorial
Publié
Date de publication
14/09/2007
Peer-reviewed
Oui
Volume
7
Pages
166
Langue
anglais
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: epublish
Résumé
P-selectin glycoprotein ligand-1 (PSGL-1) plays a critical role in recruiting leukocytes in inflammatory lesions by mediating leukocyte rolling on selectins. Core-2 O-glycosylation of a N-terminal threonine and sulfation of at least one tyrosine residue of PSGL-1 are required for L- and P-selectin binding. Little information is available on the intra- and inter-species evolution of PSGL-1 primary structure. In addition, the evolutionary conservation of selectin binding site on PSGL-1 has not been previously examined in detail. Therefore, we performed multiple sequence alignment of PSGL-1 amino acid sequences of 14 mammals (human, chimpanzee, rhesus monkey, bovine, pig, rat, tree-shrew, bushbaby, mouse, bat, horse, cat, sheep and dog) and examined mammalian PSGL-1 interactions with human selectins.
A signal peptide was predicted in each sequence and a propeptide cleavage site was found in 9/14 species. PSGL-1 N-terminus is poorly conserved. However, each species exhibits at least one tyrosine sulfation site and, except in horse and dog, a T [D/E]PP [D/E] motif associated to the core-2 O-glycosylation of a N-terminal threonine. A mucin-like domain of 250-280 amino acids long was disclosed in all studied species. It lies between the conserved N-terminal O-glycosylated threonine (Thr-57 in human) and the transmembrane domain, and contains a central region exhibiting a variable number of decameric repeats (DR). Interspecies and intraspecies polymorphisms were observed. Transmembrane and cytoplasmic domain sequences are well conserved. The moesin binding residues that serve as adaptor between PSGL-1 and Syk, and are involved in regulating PSGL-1-dependent rolling on P-selectin are perfectly conserved in all analyzed mammalian sequences. Despite a poor conservation of PSGL-1 N-terminal sequence, CHO cells co-expressing human glycosyltransferases and human, bovine, pig or rat PSGL-1 efficiently rolled on human L- or P-selectin. By contrast, pig or rat neutrophils were much less efficiently recruited than human or bovine neutrophils on human selectins. Horse PSGL-1, glycosylated by human or equine glycosyltransferases, did not interact with P-selectin. In all five species, tyrosine sulfation of PSGL-1 was required for selectin binding.
These observations show that PSGL-1 amino acid sequence of the transmembrane and cytoplasmic domains are well conserved and that, despite a poor conservation of PSGL-1 N-terminus, L- and P-selectin binding sites are evolutionary conserved. Functional assays reveal a critical role for post-translational modifications in regulating mammalian PSGL-1 interactions with selectins.

Mots-clé
Amino Acid Sequence, Animals, CHO Cells, Cattle, Cell Adhesion, Cricetinae, Cricetulus, Evolution, Molecular, Flow Cytometry, Furin/genetics, Horses, Humans, Immunophenotyping, Membrane Glycoproteins/genetics, Mice, Neutrophil Infiltration/genetics, Rats, Species Specificity, Swine, Transfection
Pubmed
Web of science
Open Access
Oui
Création de la notice
25/01/2008 15:27
Dernière modification de la notice
20/08/2019 12:41
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