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Home / Equine Research Bank / Can J Vet Res / Evaluation of plasma alpha-2-macroglobulin and interactions ...
Canadian journal of veterinary research = Revue canadienne de recherche veterinaire1996; 60(2); 150-157;

Evaluation of plasma alpha-2-macroglobulin and interactions with tumour necrosis factor-alpha in horses with endotoxemic signs.

Abstract: The electrophoretic position and behavior of the native and activated forms of equine plasma alpha-2-macroglobulin (alpha 2M) were characterized and compared to human alpha 2M by nondenaturing polyacrylamide-gel electrophoresis (PAGE). Plasma alpha 2M was also compared between 6 normal horses and 6 horses with clinical signs of colic and endotoxemia due to volvulus or enteritis. Native and activated forms of alpha 2M were quantified by PAGE and densitometry. Binding of radio-labeled recombinant human tumour necrosis factor-alpha (125I-rhTNF-alpha) to native and activated forms of equine alpha 2M was also evaluated by autoradiography and densitometry of PAGE. Equine plasma alpha 2M migrated as a single band at a position equivalent to native human alpha 2M. Methylamine-reacted equine plasma samples resulted in faster migration of alpha 2M in a similar position to activated human alpha 2M. However, in methylamine-reacted equine plasma, an intermediate alpha 2M band was consistently present between the bands corresponding to native and activated alpha 2M. Amounts of plasma alpha 2M were similar in normal and endotoxemic horses, and remained in the electrophoretically slow or unreacted native form. The vast majority of 125I-rHuTNF-alpha did not bind to alpha 2M or other equine plasma proteins. 125I-rHuTNF-alpha bound weakly to both native and fast methylamine-reacted equine forms of alpha 2M, although binding was better to the activated form. This study indicates that: (1) equine plasma alpha 2M behaves similarly to human alpha 2M on PAGE, (2) plasma alpha 2M of horses can be activated to electrophoretically fast forms, but it is neither activated nor depleted during endotoxemia, and (3) the binding interactions between equine alpha 2M and TNF-alpha are too low to implicate equine alpha 2M as a regulator of TNF-alpha during endotoxemia in horses.
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Publication Date: 1996-04-01 PubMed ID: 8785722PubMed Central: PMC1263822
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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 purpose of this research is to examine and compare the behavior of alpha-2-macroglobulin (a type of plasma protein) in normal horses and those with symptoms of colic and endotoxemia (a serious bacterial infection). The researchers also studied the interactions between this protein and the human tumour necrosis factor-alpha, an inflammatory hormone.

Study Methods

  • The research involved characterizing and comparing plasma alpha-2-macroglobulin (alpha 2M) in horse plasma to human alpha 2M using nondenaturing polyacrylamide-gel electrophoresis (PAGE) – a laboratory technique used to separate proteins.
  • They studied two groups of horses, consisting of six normal ones and six with signs of colic and endotoxemia.
  • The native (natural, un-altered state) and activated forms (changed properties due to biochemical reactions) of alpha 2M were quantified through PAGE and densitometry – a procedure that measures the blackness (and thus quantity) of bands on an electrophoretic gel.
  • The researchers also analyzed how radio-labeled recombinant human tumour necrosis factor-alpha (125I-rhTNF-alpha) – a molecule tagged with a radioactive substance for tracking – binds with both the native and activated forms of equine alpha 2M.

Key Findings

  • In normal conditions, equine plasma alpha 2M shares similarities with human alpha 2M.
  • Through a chemical reaction with methylamine, horse plasma alpha 2M can be converted into electrophoretically fast forms.
  • The amount of equine plasma alpha 2M remained the same in both normal and endotoxemic horses.
  • The vast majority of 125I-rhuTNF-alpha did not bind to alpha 2M or other equine plasma proteins.
  • 125I-rhuTNF-alpha showed weak binding to both the native and fast methylamine-reacted equine forms of alpha 2M, with the activated form showing comparatively more binding.

Conclusion

  • In horses, even during endotoxemia, plasma alpha 2M neither gets activated nor depleted.
  • The interaction between equine alpha 2M and TNF-alpha is too weak to suggest that alpha 2M can regulate TNF-alpha during endotoxemia in horses.

Cite This Article

APA
Coté N, Trout DR, Hayes AM. (1996). Evaluation of plasma alpha-2-macroglobulin and interactions with tumour necrosis factor-alpha in horses with endotoxemic signs. Can J Vet Res, 60(2), 150-157.

Publication

Canadian journal of veterinary research = Revue canadienne de recherche veterinaire
ISSN: 0830-9000
NlmUniqueID: 8607793
Country: Canada
Language: English
Volume: 60
Issue: 2
Pages: 150-157

Researcher Affiliations

Coté, N
  • Department of Large Animal Surgery,, University of Guelph, Ontario.
Trout, D R
    Hayes, A M

      MeSH Terms

      • Animals
      • Autoradiography
      • Bacteremia / blood
      • Bacteremia / physiopathology
      • Bacteremia / veterinary
      • Blood Proteins / isolation & purification
      • Blood Proteins / metabolism
      • Colic / blood
      • Colic / physiopathology
      • Colic / veterinary
      • Electrophoresis, Polyacrylamide Gel
      • Heart Rate
      • Horse Diseases
      • Horses
      • Humans
      • Iodine Radioisotopes
      • Methylamines
      • Recombinant Proteins / blood
      • Recombinant Proteins / isolation & purification
      • Reference Values
      • Toxemia / blood
      • Toxemia / physiopathology
      • Toxemia / veterinary
      • Tumor Necrosis Factor-alpha / isolation & purification
      • Tumor Necrosis Factor-alpha / metabolism
      • alpha-Macroglobulins / isolation & purification
      • alpha-Macroglobulins / metabolism

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