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Comparison of specificity of human and horse leucocyte proteinases with synthetic peptide substrates.

Abstract: Highly purified horse leucocyte proteinases 1, 2A and 2B hydrolyze synthetic substrates which are decomposed also by human leucocyte elastase but they are unable to hydrolyze typical substrates of cathepsin G. Thus in distinction to other mammalian species horse leucocytes are devoid of cathepsin G and contain only elastases.
Publication Date: 1986-01-01 PubMed ID: 3639831
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  • Comparative Study
  • Journal Article
  • Research Support
  • Non-U.S. Gov't

Summary

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The research article is about a comparative study between human and horse leucocyte proteinases’ specificity using synthetic peptide substrates. It was found that horse leucocytes lack cathepsin G, a protein found in most mammals, but contain elastases, which also decomposes synthetic substrates like human leucocyte elastase.

Objective of the Research

The objective of the research was to compare the specificity of human and horse leucocyte proteinases using synthetic peptide substrates. The researchers wanted to understand if there are key differences in the enzyme composition among different mammalian species.

  • The researchers used highly purified horse leucocyte proteinases namely 1, 2A and 2B in this study.
  • The initial observation was that these horse proteins could effectively decompose synthetic substrates, akin to how human leucocyte elastase functions.

Observations and Results

The scientists observed significant differences in the enzymatic functioning between the human and horse leucocytes.

  • They found that horse leucocyte proteinases were incapable of decomposing substrates typically broken down by cathepsin G, a proteinase observed in human leucocytes.
  • This led to the conclusion that horse leucocytes lacked cathepsin G, which is in contrast to most mammalian species where this enzyme is present.

Implications of the Study

The critical finding of the study is the distinction in the proteinase constitution between human and horse leucocyte cells, which could have significant ramifications in the field of veterinary and biological research.

  • The absence of cathepsin G in horse leucocytes indicates a different enzymatic machinery compared to human and most other mammalian cells.
  • This peculiar difference in enzyme composition can be critical in treating diseases related to leucocytes in horses.
  • Furthermore, this research could potentially pave the way for more comparative studies among different mammalian species, contributing to a better understanding of evolutionary differences at the cellular level.

Cite This Article

APA
Dubin A, Potempa J, Schnebli HP, Koj A. (1986). Comparison of specificity of human and horse leucocyte proteinases with synthetic peptide substrates. Folia Histochem Cytobiol, 24(2), 157-161.

Publication

ISSN: 0239-8508
NlmUniqueID: 8502651
Country: Poland
Language: English
Volume: 24
Issue: 2
Pages: 157-161

Researcher Affiliations

Dubin, A
    Potempa, J
      Schnebli, H P
        Koj, A

          MeSH Terms

          • Animals
          • Cathepsin G
          • Cathepsins / blood
          • Horses / blood
          • Humans
          • Hydrolysis
          • Kinetics
          • Leukocytes / enzymology
          • Oligopeptides / metabolism
          • Pancreatic Elastase / blood
          • Serine Endopeptidases
          • Substrate Specificity

          Citations

          This article has been cited 1 times.
          1. Dubin A, Potempa J, Travis J. Structural and functional characterization of elastases from horse neutrophils.. Biochem J 1994 Jun 1;300 ( Pt 2)(Pt 2):401-6.
            doi: 10.1042/bj3000401pubmed: 7516152google scholar: lookup