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An estrogen-dependent esterase activity in MCF-7 cells.

J Katz, T H Finlay, S Banerjee

Journal of Steroid Biochemistry

|June 1, 1987

Summary

Esterase activity in human breast cancer cells (MCF-7) was investigated. A specific estrogen-dependent esterase was identified, suggesting a role in hormone-sensitive cancers.

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Area of Science:

Biochemistry
Cell Biology
Oncology

Background:

Steroidal esters are present in hormone-sensitive tissues.
Esterases are crucial for converting inactive steroidal esters to active forms.
Understanding esterase activity is important in breast cancer research.

Purpose of the Study:

To investigate esterase activities in the human breast cancer MCF-7 cell line.
To characterize the hydrolysis of various steroidal esters, including estradiol esters.
To identify potential estrogen-dependent esterases.

Main Methods:

Utilized tritiated estradiol esters (estradiol-17-acetate, estradiol-17-valerate, estradiol-17-stearate) and other steroidal compounds.
Assayed esterase activity in growing MCF-7 cell cultures and cell homogenates (28,000 g supernate).
Performed inhibition studies with other steroids, antiestrogens (keoxifene), and varying substrate concentrations.

Main Results:

MCF-7 cells hydrolyzed tested steroidal esters, except phorbol diesters.
Hydrolysis rates for estradiol esters followed the order: estradiol-17-acetate > estradiol-17-valerate > estradiol-17-stearate.
A distinct estradiol-17-acetate esterase was identified, stimulated by estradiol and unaffected by other estradiol esters; its activity was negated by keoxifene.
Inhibition studies suggested serine active-site esterases.

Conclusions:

MCF-7 cells possess significant esterase activity towards steroidal esters.
An estrogen-dependent esterase activity was identified, potentially playing a role in estrogen-mediated processes in breast cancer.
Further research is needed to elucidate the natural substrate(s) of this estrogen-dependent esterase.

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