ArticleFish physiology and biochemistry2012
Molecular cloning and expression analysis of P-selectin glycoprotein ligand-1 from zebrafish (Danio rerio).
Article in Fish physiology and biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 17 citations in OpenAlex.
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
To date, the best characterized glycoprotein ligand for P-selectin is P-selectin glycoprotein ligand-1 (PSGL-1). In this study, we cloned the full-length cDNA of PSGL-1 from zebrafish (Danio rerio). Zebrafish PSGl-1 cDNA is 1,594 bp and encodes a putative 284 amino acid protein with a theoretical molecular weight of 30.33 kDa and isoelectric point of 7.96. A signal peptide of 27 amino acids is predicted. The putative protein contains an extracellular mucin-like domain, a transmembrane domain and a cytoplasmic domain, with homology to mammalian PSGL-1. In the putative P-selectin binding region, there are 1 potential tyrosine sulfation site and 12 potential threonine O-glycosylation sites. A single extracellular cysteine, at the junction of the extracellular and transmembrane domains, suggests a disulfide-bonding pattern. The amino acid sequence of zebrafish PSGL-1 is 19-22% identical to that of mammalian PSGL-1. RT-PCR and whole-mount in situ hybridization analysis revealed that zebrafish PSGL-1 was expressed in early embryonic development, and the expression has an increased trend from 0.2 (1-cell stage) to 72 hpf. The results indicate that the general domain structure of PSGL-1 protein is conserved among species, and zebrafish PSGL-1 plays important roles in embryonic development and probably has similar biological function to that of mammalian PSGL-1.
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