PUBLICATION
Molecular cloning and expression analysis of P-selectin glycoprotein ligand-1 from zebrafish (Danio rerio)
- Authors
- Sun, G., Pan, J., Liu, K., Wang, S., Wang, X., and Wang, X.
- ID
- ZDB-PUB-110719-13
- Date
- 2012
- Source
- Fish physiology and biochemistry 38(2): 555-564 (Journal)
- Registered Authors
- Keywords
- PSGL-1, zebrafish, cloning, expression, cDNA
- MeSH Terms
-
- Amino Acid Sequence
- Animals
- Base Sequence
- Cloning, Molecular
- Gene Expression
- Membrane Glycoproteins/genetics*
- Membrane Glycoproteins/metabolism
- Molecular Sequence Data
- Sequence Alignment
- Sequence Homology, Amino Acid
- Zebrafish/embryology
- Zebrafish/genetics*
- Zebrafish/metabolism
- PubMed
- 21755364 Full text @ Fish Physiol. Biochem.
Citation
Sun, G., Pan, J., Liu, K., Wang, S., Wang, X., and Wang, X. (2012) Molecular cloning and expression analysis of P-selectin glycoprotein ligand-1 from zebrafish (Danio rerio). Fish physiology and biochemistry. 38(2):555-564.
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.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping