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Home / Equine Research Bank / Biochem Genet / The equine protease inhibitory system (Pi): abnormal express...
Biochemical genetics1986; 24(7-8); 529-543; doi: 10.1007/BF00504333

The equine protease inhibitory system (Pi): abnormal expressions of PiF, PiL, and PiS1.

Abstract: Three cases of abnormal expression of the equine protease inhibitory alleles, Pi F, L, and S1, were observed following the examination of 30,000 plasma samples by one-dimensional acid (pH 4.6) polyacrylamide gel electrophoresis. Characterization of the abnormal proteins in terms of isoelectric point, molecular mass, inhibitory spectra, and sialic acid content was performed using one- and two-dimensional electrophoretic techniques. The Pi F and S1 abnormalities were postulated to be the result of amino acid substitutions causing alterations in the processing of the carbohydrate side chains. No explanation could be offered for the Pi L abnormality other than a charge shift mutation. Abnormal types, F*, L*, and S1* behaved as alleles but the distribution of L* in offspring from one stallion (present in only 6 of 83 offspring) differed significantly from expectation.
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Publication Date: 1986-08-01 PubMed ID: 3753429DOI: 10.1007/BF00504333Google Scholar: Lookup
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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.

This study investigates abnormal expressions of equine protease inhibitory alleles, Pi F, L, and S1 and hypothesizes the causes of those abnormalities based on the analysis of around 30,000 plasma samples.

Introduction to the Research

  • The research revolves around the investigation of abnormal expressions in equine protease inhibitory system, primarily focusing on alleles Pi F, L, and S1.
  • The study was initiated after observing the abnormalities in these alelles in some plasma samples.

Research Methodology

  • In total, 30,000 plasma samples were examined using a one-dimensional acid (pH 4.6) polyacrylamide gel electrophoresis, which is a common method to separate proteins by their molecular size.
  • The proteins showing abnormalities were then characterized based on their isoelectric point, molecular mass, inhibitory spectra, and sialic acid content. This was done using one- and two-dimensional electrophoretic techniques, which helps researchers understand how proteins interact with one another.

Findings and Interpretations

  • Anomalies in Pi F and S1 were believed to stem from amino acid substitutions that altered the processing of the carbohydrate side chains. The term “amino acid substitutions” refers to changes in the sequence of amino acids, which are the building blocks of proteins. These changes can significantly affect a protein’s structure and function.
  • As for the Pi L abnormality, researchers could not find an explanation other than a possible charge shift mutation, which could change the charge of the protein and potentially its behavior and interactions.
  • The types of abnormalities, designated as F*, L*, and S1*, behaved as alleles, or variations of a gene.
  • The findings also revealed that the distribution of the L* abnormality in the offspring of one particular stallion differed significantly from what was expected, presenting in only 6 out of 83 offspring.

Cite This Article

APA
Patterson SD, Bell K. (1986). The equine protease inhibitory system (Pi): abnormal expressions of PiF, PiL, and PiS1. Biochem Genet, 24(7-8), 529-543. https://doi.org/10.1007/BF00504333

Publication

Biochemical genetics
ISSN: 0006-2928
NlmUniqueID: 0126611
Country: United States
Language: English
Volume: 24
Issue: 7-8
Pages: 529-543

Researcher Affiliations

Patterson, S D
    Bell, K

      MeSH Terms

      • Alleles
      • Animals
      • Electrophoresis, Polyacrylamide Gel
      • Horses
      • Isoelectric Focusing
      • Molecular Weight
      • Neuraminidase
      • Protease Inhibitors / blood
      • Protease Inhibitors / genetics
      • Protease Inhibitors / isolation & purification

      References

      This article includes 26 references
      1. Jeppsson JO, Laurell CB, Fagerhol M. Properties of isolated human alpha1-antitrypsins of Pi types M, S and Z.. Eur J Biochem 1978 Feb 1;83(1):143-53.
        pubmed: 304805doi: 10.1111/j.1432-1033.1978.tb12078.xgoogle scholar: lookup
      2. Pellegrini A, Zweifel HR, von Fellenberg R. Horse alpha-1 protease inhibitors: relationship between the slow (S) and fast (F) isoforms.. Int J Biochem 1985;17(4):463-9.
        pubmed: 3891451doi: 10.1016/0020-711x(85)90141-7google scholar: lookup
      3. Gahne B. Studies on the inheritance of electrophoretic forms of transferrins, albumins, prealbumins and plasma esterases of horses.. Genetics 1966 Apr;53(4):681-94.
        pubmed: 5960258doi: 10.1093/genetics/53.4.681google scholar: lookup
      4. Holbrook IB, Leaver AG. A procedure to increase the sensitivity of staining by Coomassie brilliant blue G250-perchloric acid solution.. Anal Biochem 1976 Oct;75(2):634-6.
        pubmed: 62520doi: 10.1016/0003-2697(76)90118-4google scholar: lookup
      5. Juneja RK, Gahne B, Sandberg K. Genetic polymorphism and close linkage of two alpha 1-protease inhibitors in horse serum.. Anim Blood Groups Biochem Genet 1979;10(4):235-51.
        pubmed: 94978doi: 10.1111/j.1365-2052.1979.tb01031.xgoogle scholar: lookup
      6. Duggleby RG, Kinns H, Rood JI. A computer program for determining the size of DNA restriction fragments.. Anal Biochem 1981 Jan 1;110(1):49-55.
        pubmed: 6259964doi: 10.1016/0003-2697(81)90110-xgoogle scholar: lookup
      7. Comings DE. Pc 1 Duarte, a common polymorphism of a human brain protein, and its relationship to depressive disease and multiple sclerosis.. Nature 1979 Jan 4;277(5691):28-32.
        pubmed: 552595doi: 10.1038/277028a0google scholar: lookup
      8. Travis J, Garner D, Bowen J. Human alpha-1-antichymotrypsin: purification and properties.. Biochemistry 1978 Dec 26;17(26):5647-51.
        pubmed: 103576doi: 10.1021/bi00619a010google scholar: lookup
      9. Fisher RA, Scott AM. Isoelectric focusing of horse serum esterase isozymes and detection of new phenotypes.. Anim Blood Groups Biochem Genet 1978;9(4):207-13.
        pubmed: 756142doi: 10.1111/j.1365-2052.1978.tb01438.xgoogle scholar: lookup
      10. Braend M. Irregular transmissions in the acidic prealbumin (Pr) system of the horse.. Anim Blood Groups Biochem Genet 1980;11(2):109-12.
        pubmed: 7436048doi: 10.1111/j.1365-2052.1980.tb01500.xgoogle scholar: lookup
      11. Spooner RL, Baxter G. Abnormal expression of normal transferrin alleles in cattle.. Biochem Genet 1969 Jan;2(4):371-82.
        pubmed: 5770242doi: 10.1007/BF01458497google scholar: lookup
      12. Braend M. Genetics of horse acidic prealbumins.. Genetics 1970 Jul;65(3):495-503.
        pubmed: 5519647doi: 10.1093/genetics/65.3.495google scholar: lookup
      13. Cox DW. The effect of neuraminidase on genetic variants of alpha anitrypsin.. Am J Hum Genet 1975 Mar;27(2):165-77.
        pubmed: 1079112
      14. Pollitt CC, Bell K. Characterisation of the alpha 1-protease inhibitor system in Thoroughbred horse plasma by horizontal two-dimensional (ISO-DALT) electrophoresis. 1. Protein staining.. Anim Blood Groups Biochem Genet 1983;14(2):83-105.
        pubmed: 6193745doi: 10.1111/j.1365-2052.1983.tb01065.xgoogle scholar: lookup
      15. Pollitt CC, Bell K. Characterisation of the alpha 1-protease inhibitor system in Thoroughbred horse plasma by horizontal two-dimensional (ISO-DALT) electrophoresis. 2. Protease inhibition.. Anim Blood Groups Biochem Genet 1983;14(2):107-18.
        pubmed: 6604473doi: 10.1111/j.1365-2052.1983.tb01066.xgoogle scholar: lookup
      16. Hill RE, Shaw PH, Barth RK, Hastie ND. A genetic locus closely linked to a protease inhibitor gene complex controls the level of multiple RNA transcripts.. Mol Cell Biol 1985 Aug;5(8):2114-22.
        pubmed: 2427931doi: 10.1128/mcb.5.8.2114-2122.1985google scholar: lookup
      17. Powell JR, Castellino FJ. Amino acid sequence analysis of the asparagine-288 region of the carbohydrate variants of human plasminogen.. Biochemistry 1983 Feb 15;22(4):923-7.
        pubmed: 6838832doi: 10.1021/bi00273a033google scholar: lookup
      18. Elbein AD. Inhibitors of the biosynthesis and processing of N-linked oligosaccharides.. CRC Crit Rev Biochem 1984;16(1):21-49.
        pubmed: 6232113doi: 10.3109/10409238409102805google scholar: lookup
      19. Laine A, Hayem A. Purification and characterization of alpha 1-antichymotrypsin from human pleural fluid and human serum.. Biochim Biophys Acta 1981 May 29;668(3):429-38.
        pubmed: 6894551doi: 10.1016/0005-2795(81)90177-xgoogle scholar: lookup
      20. Uriel J, Berges J. Characterization of natural inhibitors of trypsin and chymotrypsin by electrophoresis in acrylamide-agarose gels.. Nature 1968 May 11;218(5141):578-80.
        pubmed: 5655186doi: 10.1038/218578b0google scholar: lookup
      21. Brown WT. Alpha 1-antitrypsin: apparent molecular weight heterogeneity shown by two-dimensional electrophoresis.. Am J Hum Genet 1982 Mar;34(2):195-208.
        pubmed: 6978611
      22. Pellegrini A, Zweifel HR, von Fellenberg R. Identification of the second alpha-2-antiprotease of equine serum as antithrombin III.. Int J Biochem 1983;15(7):917-22.
        pubmed: 6884568doi: 10.1016/0020-711x(83)90167-2google scholar: lookup
      23. Green M. Incorporation of amino acid analogs interferes with the processing of the asparagine-linked oligosaccharide of the MOPC-46B kappa light chain.. J Biol Chem 1982 Aug 10;257(15):9039-42.
        pubmed: 6284755
      24. Bell K, Patterson S, Pollitt CC. The plasma protease inhibitor system (Pi) of Standardbred horses.. Anim Blood Groups Biochem Genet 1984;15(3):191-206.
        pubmed: 6517392doi: 10.1111/j.1365-2052.1984.tb01116.xgoogle scholar: lookup
      25. Kurachi K, Schmer G, Hermodson MA, Teller DC, Davie EW. Characterization of human, bovine, and horse antithrombin III.. Biochemistry 1976 Jan 27;15(2):368-73.
        pubmed: 1247522doi: 10.1021/bi00647a020google scholar: lookup
      26. Travis J, Bowen J, Baugh R. Human alpha-1-antichymotrypsin: interaction with chymotrypsin-like proteinases.. Biochemistry 1978 Dec 26;17(26):5651-6.
        pubmed: 728423doi: 10.1021/bi00619a011google scholar: lookup

      Citations

      This article has been cited 4 times.
      1. Arthur H, Bell K, VandeBerg JL, van Oorschot RA. Plasma protease inhibitor (PI) system in the laboratory opossum, Monodelphis domestica. Biochem Genet 1996 Oct;34(9-10):389-99.
        doi: 10.1007/BF00554414pubmed: 8978911google scholar: lookup
      2. 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
      3. 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
      4. Bell K, Arthur H, van Oorschot RA, VandeBerg JL. Antithrombin III (AT3) polymorphism in the marsupial Monodelphis domestica: identification and genetics. Biochem Genet 1992 Dec;30(11-12):591-601.
        pubmed: 1296573
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