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Related Experiment Videos

Human liver and plasma aspirin esterase.

F M Williams1, E M Mutch, E Nicholson

  • 1Wolfson Unit of Clinical Pharmacology, University of Newcastle upon Tyne, UK.

The Journal of Pharmacy and Pharmacology
|June 1, 1989
PubMed
Summary

The plasma and liver are key sites for aspirin hydrolysis. Individual variations in aspirin esterase activity were observed in both human plasma and liver, showing a significant correlation between the two.

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Area of Science:

  • Biochemistry
  • Pharmacology
  • Human Physiology

Background:

  • Aspirin (acetylsalicylic acid) is a widely used medication.
  • Understanding its metabolic pathways is crucial for drug efficacy and safety.
  • Aspirin hydrolysis is primarily mediated by esterase enzymes.

Purpose of the Study:

  • To investigate the role of plasma and liver as sites for aspirin hydrolysis.
  • To quantify aspirin esterase activity in human plasma and liver.
  • To explore the relationship between plasma and liver aspirin esterase activities.

Main Methods:

  • Enzyme activity assays were performed on human plasma and liver samples.
  • Aspirin esterase activity was measured.
  • Correlation analysis was conducted between plasma and liver enzyme activities.

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  • Subcellular fractionation of liver tissue was performed to isolate cytosolic and microsomal enzymes.

    • Main Results:

    • Both plasma and liver demonstrated significant aspirin esterase activity.
    • A two-fold variation in enzyme activity was observed across individuals.
    • A significant positive correlation was found between plasma and liver aspirin esterase levels.
    • Human liver aspirin esterase was localized in both cytosolic and microsomal fractions.
    • Cytosolic and microsomal enzymes exhibited distinct activities and substrate affinities for aspirin.

    Conclusions:

    • Plasma is a significant site for aspirin hydrolysis, alongside the liver.
    • Individual variability in aspirin metabolism exists and is correlated between plasma and liver.
    • Human liver aspirin esterase exists in multiple forms with differing kinetic properties.