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Animal genetics1987; 18(2); 167-180; doi: 10.1111/j.1365-2052.1987.tb00756.x

ISO-DALT characterization of 12 ‘new’ equine plasma protease inhibitor (Pi) alleles.

Abstract: Twelve equine protease inhibitory alleles, PiE, H, J, K, L2, O, P, Q, R, V, X, Z, have been characterized in terms of isoelectric point, molecular mass and inhibitory activity to bovine trypsin and chymotrypsin by ISO-DALT electrophoresis. Protein maps for 20 Pi alleles including those of the eight 'Thoroughbred' alleles (PiF, G, I, L, N, S1, S2, U) have now been determined. Five pairs of alleles, S1/S2, G/K, L/L2, P/R and U/Z, possessed varying numbers of common proteins ranging from one protein in the case of G/K and L/L2 to six in the case of U/Z. Based on these results and studies of the abnormal expressions of PiF, PiL and PiS1, a theory of at least three closely linked loci has been postulated to account for the marked heterogeneity of the equine protease inhibitory system.
Publication Date: 1987-01-01 PubMed ID: 3662116DOI: 10.1111/j.1365-2052.1987.tb00756.xGoogle Scholar: Lookup
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  • Journal Article
  • Research Support
  • Non-U.S. Gov't

Summary

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This research explores and compares the properties of twelve newly discovered equine plasma protease inhibitor (Pi) alleles, providing more insight into the complexity and heterogeneity of the equine protease inhibitory system.

Overview of Research

  • The study focuses on characterizing twelve newly discovered equine protease inhibitor (Pi) alleles using ISO-DALT electrophoresis. According to the paper, the specific alleles examined are PiE, H, J, K, L2, O, P, Q, R, V, X, Z.
  • The properties studied for each allele include its isoelectric point (the pH at which a particular molecule carries no net electric charge), molecular mass, and its inhibitory activity towards two types of proteases – bovine trypsin and chymotrypsin.
  • The authors also compiled protein maps for 20 Pi alleles in total, which covered eight alleles previously studied in Thoroughbreds (PiF, G, I, L, N, S1, S2, U).

Key Findings

  • Five pairs of alleles, namely S1/S2, G/K, L/L2, P/R and U/Z, were found to share various numbers of common proteins. The sharing ranged from one protein in the case of G/K and L/L2 pairs, up to six proteins in the case of the U/Z pair.
  • These findings, along with the abnormal expressions of PiF, PiL and PiS1, led the researchers to propose a theory of at least three closely linked loci, i.e., specific positions on the equine genetic map. The existence of these loci, which are presumably home to the genes responsible for producing protease inhibitors, explain the observed variability in the equine protease inhibitory system.

Implications of the Study

  • This study provides valuable insights into the protease inhibitory system of horses, which is crucial to understand the immune response and health in these animals.
  • More specifically, the characterization of the new Pi alleles, along with the establishment of potential shared proteins between some of these, expands our understanding of the genetic diversity and complexity of the equine protease inhibitory system.
  • Understanding these genetic bases provides new avenues for future studies on equine health and disease resistance, and could potentially inform breeding strategies aimed at improving horses’ overall health and wellbeing.

Cite This Article

APA
Patterson SD, Bell K. (1987). ISO-DALT characterization of 12 ‘new’ equine plasma protease inhibitor (Pi) alleles. Anim Genet, 18(2), 167-180. https://doi.org/10.1111/j.1365-2052.1987.tb00756.x

Publication

ISSN: 0268-9146
NlmUniqueID: 8605704
Country: England
Language: English
Volume: 18
Issue: 2
Pages: 167-180

Researcher Affiliations

Patterson, S D
  • Department of Physiology and Pharmacology, University of Queensland, St Lucia, Australia.
Bell, K

    MeSH Terms

    • Alleles
    • Animals
    • Chymotrypsin / blood
    • Electrophoresis, Polyacrylamide Gel / methods
    • Horses / genetics
    • Isoelectric Focusing / methods
    • Molecular Weight
    • Protease Inhibitors / blood
    • Protease Inhibitors / genetics
    • Trypsin Inhibitors / blood
    • Trypsin Inhibitors / genetics

    Citations

    This article has been cited 2 times.
    1. Potempa J, Wunderlich JK, Travis J. Comparative properties of three functionally different but structurally related serpin variants from horse plasma. Biochem J 1991 Mar 1;274 ( Pt 2)(Pt 2):465-71.
      doi: 10.1042/bj2740465pubmed: 2006910google scholar: lookup
    2. Patterson SD, Bell K, Shaw DC. The equine major plasma serpin multigene family: partial characterization including sequence of the reactive-site regions. Biochem Genet 1991 Oct;29(9-10):477-99.
      doi: 10.1007/BF02399689pubmed: 1772402google scholar: lookup