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Published on: November 3, 2013
The human androgen receptor: complementary deoxyribonucleic acid cloning, sequence analysis and gene expression in
D B Lubahn1, D R Joseph, M Sar
1Laboratories for Reproductive Biology, University of North Carolina, Chapel Hill 27599.
Molecular Endocrinology (Baltimore, Md.)
|December 1, 1988
Summary
Researchers cloned the human androgen receptor (hAR), a key protein for male development. This finding advances understanding of nuclear receptor family members and their roles in male sex differentiation.
Area of Science:
- Molecular Biology
- Endocrinology
- Genetics
Background:
- Androgenic hormones are crucial for male sex differentiation and development.
- These hormones exert their effects via a high-affinity receptor protein.
Purpose of the Study:
- To clone the complete coding sequence of the human androgen receptor (hAR).
- To analyze the sequence homology of hAR with other nuclear receptors.
- To investigate the localization of hAR in human prostate tissue.
Main Methods:
- Cloning of the complete coding sequence of hAR.
- Sequence homology analysis comparing hAR to other nuclear receptors (progesterone, mineralocorticoid, glucocorticoid receptors).
- Raised rabbit polyclonal antibodies against a synthetic peptide from the N-terminal region of hAR.
- Immunocytochemical analysis of human prostate tissue.
Main Results:
- The complete coding sequence of hAR was cloned, revealing a 919 amino acid protein.
- hAR belongs to the nuclear receptor family, showing highest homology in DNA-binding and ligand-binding domains with progesterone, mineralocorticoid, and glucocorticoid receptors.
- Comparison with rat AR showed 85% overall homology, with identical DNA- and hormone-binding domains.
- The major androgen receptor mRNA species in human prostate is 10 kilobases.
- Immunocytochemistry confirmed hAR localization predominantly in the nuclei of glandular epithelial cells in human prostate tissue.
Conclusions:
- The cloning of hAR provides a molecular basis for understanding androgen action.
- hAR shares significant structural and sequence homology with other nuclear receptors, particularly in key functional domains.
- The localization of hAR in prostate cell nuclei supports its role as a transcription factor mediating androgen effects.
