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Life sciences2002; 70(20); 2445-2455; doi: 10.1016/s0024-3205(02)01529-1

ATPase and Adpase activities in synovial membrane of equine metacarpophalangeal joint.

Abstract: ATPase and ADPase activities capable of hydrolyzing nucleoside di- and triphosphates in the presence of Ca2+ are present in synovial membrane of metacarpophalangeal joint mainly associated to membrane fractions. These hydrolytic activities have been considered involved in the inflammatory process where ATP and ADP are inflammatory mediators while adenosine counteracts this effect. Both, subcellular localization and kinetic properties of these nucleotidase activities, suggest that could correspond to single enzyme called ATP-diphosphohydrolase or apyrase. The comparison of the activity on ATP-Ca and ADP-Ca from normal and pathological equine synovial membrane did not show significant differences either in the subcellular fraction distribution or in the enrichment of each subcellular fraction. Neither differences on 5'-nucleotidase activity present in the microsomal fraction were observed.
Publication Date: 2002-08-02 PubMed ID: 12150208DOI: 10.1016/s0024-3205(02)01529-1Google Scholar: Lookup
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Summary

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This study researches the relationship between ATPase and ADPase activities in the synovial membrane of a horse’s metacarpophalangeal joint. It also explores the potential involvement of these activities in the inflammatory process. However, no significant differences were observed in the activity from normal and pathological synovial membranes.

Understanding ATPase, ADPase, and Apyrase

  • The researchers observed ATPase (adenosine triphosphatase) and ADPase (adenosine diphosphatase) activities in the equine metacarpophalangeal joint’s synovial membrane. These activities are responsible for the hydrolysis of nucleoside di- and triphosphates, in the presence of calcium ions.
  • These ATPase and ADPase functions appear to be tightly anchored to the membrane fractions of the synovial membrane. Both these enzymes are noted for their ability to break bonds in ATP and ADP molecules, respectively, releasing energy in the process.
  • The study also explored how these functions might relate to an enzyme known as ATP-diphosphohydrolase, or more commonly, apyrase. The researchers examined their subcellular locations and kinetic properties, hinting at a possible single enzyme interaction.

Inflammation and Metacarpophalangeal Joint

  • The study takes a particular interest in the role of ATPase and ADPase functions in the inflammatory process. ATP and ADP are identified as inflammatory mediators – they play a role in signaling and creating the body’s inflammatory response.
  • In contrast, adenosine, a substance broken down by the ATPase and ADPase, is thought to counteract the inflammatory effect. It works as an anti-inflammatory mediator.

Comparison between Normal and Pathological Synovial Membranes

  • Interestingly, when the researchers compared the activity on ATP-Ca and ADP-Ca from normal and pathological (diseased) equine synovial membranes, no significant differences were noticed. This observation applies to both the subcellular fraction distribution and the enrichment of each subcellular fraction.
  • The research also studied 5′-nucleotidase activity in the microsomal fraction. There were no observable differences in this activity, even when comparing normal and pathological samples.

In summary, the research delved into the ATPase and ADPase activities in a horse’s metacarpophalangeal joint, their potential role in the inflammatory process, and their relationship with apyrase. However, despite the detailed examination and comparison, no significant differences were observed between healthy and diseased sample activities. This finding could suggest a complex relationship between these enzymes and how they contribute to inflammation and other processes within the joint.

Cite This Article

APA
Jiménez PA, García L, Adarmes H, González E, Valenzuela MA. (2002). ATPase and Adpase activities in synovial membrane of equine metacarpophalangeal joint. Life Sci, 70(20), 2445-2455. https://doi.org/10.1016/s0024-3205(02)01529-1

Publication

ISSN: 0024-3205
NlmUniqueID: 0375521
Country: Netherlands
Language: English
Volume: 70
Issue: 20
Pages: 2445-2455

Researcher Affiliations

Jiménez, Paula A
  • Departamento de Bioquímica y Biología Molecular, Facultad de Ciencias Químicas y Farmacéuticas, Universidad de Chile, Santiago.
García, Lorena
    Adarmes, H
      González, E
        Valenzuela, M A

          MeSH Terms

          • 5'-Nucleotidase / metabolism
          • Adenosine / biosynthesis
          • Adenosine Triphosphatases / antagonists & inhibitors
          • Adenosine Triphosphatases / metabolism
          • Animals
          • Apyrase / adverse effects
          • Apyrase / antagonists & inhibitors
          • Apyrase / metabolism
          • Arthritis / enzymology
          • Cytosol / drug effects
          • Cytosol / enzymology
          • Enzyme Inhibitors / pharmacology
          • Horses / metabolism
          • In Vitro Techniques
          • Joints / metabolism
          • Mitochondria / drug effects
          • Mitochondria / enzymology
          • Subcellular Fractions / enzymology
          • Synovial Membrane / enzymology

          Citations

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