Identification of equine P-selectin glycoprotein ligand-1 (CD162).
Abstract: P-selectin glycoprotein ligand-1 (PSGL-1, CD162) is a dimeric, mucin-like, transmembrane glycoprotein constitutively expressed on leukocytes. A high baseline level of P-selectin expression in circulating equine platelets suggests a primed state toward inflammation and thrombosis via P-selectin/PSGL-1 adhesion. To investigate the potential role of equine P-selectin in these events, we first identified the cDNA sequence of equine PSGL-1 (ePSGL-1) using degenerate PCR and RACE-PCR and then compared the predicted sequence with that of human PSGL-1 (hPSGL-1). ePSGL-1 protein subunit is predicted to be 43 kDa and composed of 420 amino acids with a predicted 18-amino-acid signal sequence showing 78% homology to hPSGL-1. Previously published work has shown that binding of P-selectin requires sulfation of at least one of three tyrosines and O-glycosylation of one threonine in the N-terminus of human PSGL-1. However, the corresponding domain in ePSGL-1, spanning residues 19-43, contains only one tyrosine in the vicinity of two threonines at positions 25 and 41. ePSGL-1 contains 14 threonine/serine-rich decameric repeats as compared to hPSGL-1 which contains 14-16 threonine-rich decameric repeats. The transmembrane and cytoplasmic domains display 91% and 74% homology to corresponding human PSGL-1 domains, respectively. In summary, there is 71% homology in comparing the open reading frame (ORF) of ePSGL-1 with that of hPSGL-1. The greatest homologies between species exist in the transmembrane domain and cytoplasmic tail while substantial differences exist in the extracellular domain.
Publication Date: 2005-01-28 PubMed ID: 15674735DOI: 10.1007/s00335-004-2348-6Google Scholar: Lookup
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- Comparative Study
- Journal Article
Summary
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The research article is centered around the identification and investigation of P-selectin glycoprotein ligand-1’s (also known as PSGL-1 or CD162) role in horses, especially in relation to inflammation and thrombosis.
Summary of the Research
The researchers set out to further understand the role of P-selectin glycoprotein ligand-1 (PSGL-1) in horses. PSGL-1 is a mucin-like protein present on the cell surface of leukocyte cells. A high level of P-selectin expression was found in circulating horse platelets, which points towards it having an active role in the body’s internal defence processes.
- The researchers employed degenerate PCR and RACE-PCR techniques to identify the cDNA sequence of equine PSGL-1 (ePSGL-1), with the aim of understanding more about its structure and potential function.
- The ePSGL-1 protein was found to be composed of 420 amino acids, weighing in at 43 kDa, and having an 18-amino-acid signal sequence. This showed significant homology (78%) to the human PSGL-1 (hPSGL-1), suggesting a similar biological function in both species.
Comparative Analysis
Their research on ePSGL-1 also involved comparing it with the previously known attributes of hPSGL-1.
- It was found that ePSGL-1 has only one tyrosine, located near two threonines at positions 25 and 41, as opposed to hPSGL-1 requiring sulfation of three tyrosines and O-glycosylation of one threonine.
- ePSGL-1 was found to contain 14 threonine/serine-rich decameric repeats in comparison to hPSGL-1’s 14-16 threonine-rich decameric repeats.
- The transmembrane and cytoplasmic domains of ePSGL-1 displayed a high level of homology to the corresponding domains of hPSGL-1, with a 91% and 74% match respectively.
Overall Homology and Variations
When the full-length protein sequence of ePSGL-1 was compared with hPSGL-1, it showed a homology of 71%.
- The most significant similarities between the horse and human proteins occurred in the transmembrane domain and cytoplasmic tail.
- However, the researchers identified substantial differences in the extracellular domain of the protein in both species.
- These variations may lead to differences in the physiological roles and biological effects of PSGL-1 in horses and humans.
Cite This Article
APA
Xu J, Lasry JB, Svaren J, Wagner B, Darien BJ.
(2005).
Identification of equine P-selectin glycoprotein ligand-1 (CD162).
Mamm Genome, 16(1), 66-71.
https://doi.org/10.1007/s00335-004-2348-6 Publication
Researcher Affiliations
- Department of Medical Sciences, School of Veterinary Medicine, University of Wisconsin, Madison, Wisconsin, 53706-1102, USA.
MeSH Terms
- Amino Acid Sequence
- Animals
- Base Sequence
- Horses / genetics
- Humans
- Ligands
- Membrane Glycoproteins / blood
- Membrane Glycoproteins / chemistry
- Membrane Glycoproteins / genetics
- Membrane Glycoproteins / isolation & purification
- Molecular Sequence Data
- P-Selectin
- Polymerase Chain Reaction
- Sequence Homology
References
This article includes 21 references
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Citations
This article has been cited 1 times.- Sun G, Pan J, Liu K, Wang S, Wang X, Wang X. Molecular cloning and expression analysis of P-selectin glycoprotein ligand-1 from zebrafish (Danio rerio). Fish Physiol Biochem 2012 Apr;38(2):555-64.
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