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Mammalian genome : official journal of the International Mammalian Genome Society2005; 16(1); 66-71; doi: 10.1007/s00335-004-2348-6

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.
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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

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

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

Mammalian genome : official journal of the International Mammalian Genome Society
ISSN: 0938-8990
NlmUniqueID: 9100916
Country: United States
Language: English
Volume: 16
Issue: 1
Pages: 66-71

Researcher Affiliations

Xu, Jin
  • Department of Medical Sciences, School of Veterinary Medicine, University of Wisconsin, Madison, Wisconsin, 53706-1102, USA.
Lasry, Joëlle B
    Svaren, John
      Wagner, Bettina
        Darien, Benjamin J

          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

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          Citations

          This article has been cited 1 times.
          1. 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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