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Steroidogenic enzymes in skin.

¹Department of Obstetrics-Gynecology and Biochemistry, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390-9032, USA. stefan.andersson@UTSouthwestern.edu

European Journal of Dermatology : EJD

|June 12, 2001

Summary

Dihydrotestosterone (DHT) drives androgenetic alopecia by binding strongly to androgen receptors. Inhibiting 5α-reductase enzymes lowers DHT, promoting hair growth and potentially slowing balding.

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Area of Science:

Endocrinology
Dermatology
Biochemistry

Background:

Testosterone synthesis involves key enzymes like cytochrome P450s and hydroxysteroid dehydrogenases.
Plasma testosterone is converted to dihydrotestosterone (DHT) in target tissues, including skin, by 5α-reductase isoenzymes.
DHT is the primary androgen responsible for androgenetic alopecia due to its high affinity for the nuclear androgen receptor.

Purpose of the Study:

To investigate the enzymatic pathways involved in dihydrotestosterone (DHT) synthesis in scalp skin.
To explore the role of aberrant enzyme expression in the pathogenesis of androgenetic alopecia.
To provide a biochemical basis for the efficacy of 5α-reductase inhibitors in treating hair loss.

Main Methods:

Review of established biochemical pathways for steroidogenesis.
Analysis of enzyme kinetics and substrate specificities.
Discussion of the role of local enzyme expression in androgenetic alopecia.

Main Results:

The conversion of testosterone to DHT by 5α-reductase is crucial for androgenetic alopecia.
Alternative pathways involving C19-steroids and specific hydroxysteroid dehydrogenases contribute to scalp DHT production.
Aberrant expression of these enzymes may increase local DHT levels, accelerating hair loss.

Conclusions:

DHT is the key androgen mediating androgenetic alopecia.
Finasteride's efficacy stems from inhibiting 5α-reductase, reducing DHT levels.
Understanding local scalp enzyme activity offers potential targets for novel hair loss treatments.

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