The function of P-selectin glycoprotein ligand-1 is conserved from ancestral fishes to mammals.

The function of P-selectin glycoprotein ligand-1 is conserved from ancestral fishes to mammals.
J Leukoc Biol. 2019 Jul 14;:
Authors: Baïsse B, Spertini C, Galisson F, Smirnova T, Spertini O
Abstract
PSGL-1 is a mucin-like glycoprotein that supports, in mammals, leukocyte rolling on selectins. However, we have limited knowledge whether its function is conserved in non-mammals and how its structure adapted during evolution. To identify conserved amino acid sequences required for selectin binding, we performed multiple alignments of PSGL-1 sequences from 18 mammals, 4 birds, 3 reptiles, 1 amphibian, and 15 fishes. The amino-terminal T[D/E]PP[D/E] motif, which identifies in mammals a core-2 O-glycosylated threonine required for selectin-binding, is partially conserved in some fishes (e.g., T. rubripes) and birds (e.g., G. gallus), however, most non-mammals do not display it. The sulfated tyrosine residues of human PSGL-1, which bind L- and P-selectin, are not observed in non-mammals, suggesting that they are dispensable for selectin-binding or that other amino acids play their role. A mucin-like domain is present in all species. Interestingly, the alignment of cytoplasmic sequences of non-mammals reveals the conservation of ezrin/radixin/moesin binding site and two new motifs (M1 and M2). To examine the conservation of PSGL-1 function, we cloned PSGL-1 cDNA sequences of zebrafish and fugu, and established their cross-reactivity with hu...

Source: Journal of Leukocyte Biology - July 13, 2019 Category: Hematology Authors: Baïsse B, Spertini C, Galisson F, Smirnova T, Spertini O Tags: J Leukoc Biol Source Type: research