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Human hepatic microsomal epoxide hydrolase: comparative analysis of polymorphic expression

C Hassett¹, J Lin, C L Carty

¹Department of Environmental Health, University of Washington, Seattle 98105-6099, USA.

Archives of Biochemistry and Biophysics

|January 15, 1997

Summary

Interindividual variation in human microsomal epoxide hydrolase (mEH) expression impacts chemical toxicity risk. Hepatic mEH activity and protein levels vary significantly, suggesting post-transcriptional regulation.

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Area of Science:

Biochemistry
Toxicology
Genetics

Background:

Interindividual variability in human microsomal epoxide hydrolase (mEH) expression is a potential risk factor for chemical toxicities.
Understanding this variation is crucial for assessing individual susceptibility to carcinogens and teratogens.

Purpose of the Study:

To investigate phenotypic variability and genetic polymorphisms of mEH in human liver samples.
To correlate mEH enzyme activity, protein content, and RNA levels.

Main Methods:

Analyzed 40 human liver samples for mEH protein content, enzymatic activity, and RNA levels.
Assessed enzymatic activity using (+/-)-benzo[a]pyrene-4,5-epoxide.
Examined common polymorphic amino acid loci in the mEH protein.

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Main Results:

Enzymatic activity showed an 8-fold range and correlated strongly with mEH protein content (r > 0.74).
mEH protein and activity levels were poorly correlated with mEH RNA levels, which varied 49-fold.
Common polymorphic amino acid loci did not solely explain activity variations.

Conclusions:

Significant functional variability exists in hepatic mEH across individuals.
mEH protein expression is likely regulated by post-transcriptional controls, possibly involving non-coding regions of the transcript.