The presence of a hitherto undefined high-capacity androgen binding macromolecule in human ovarian cancer tissue.
Sex hormone binding globulin (SHBG) is known to interfere in the quantitation of androgen receptors (AR) if dihydrotestosterone (DHT) is used. We used a monoclonal antibody to remove SHBG from cytosol. In cytosol of benign prostatic hyperplastic (BPH) tissue low capacity binding for DHT, but not for R1881, was found after removal of SHBG. AR were detected in 18 of 20 ovarian cancer cytosols. In the two AR-negative cases, non-saturable binding for DHT, testosterone and R1881 was observed. Incubation with anti-SHBG did not change this. An hitherto undefined androgen binding macromolecule(s), with high-capacity binding for natural and synthetic androgens, but not for estrogen and progesterone, seems to be present in these ovarian cancer tissues. The functionality of these androgen binding macromolecules in ovarian cancer is yet to be demonstrated.
Slotman
B J
BJ
Department of Endocrinology, Academisch Ziekenhuis Vrije Universiteit,Amsterdam, The Netherlands.
Rao
B R
BR
D000727:Androgen-Binding Protein / Q000302:isolation & purification* / Q000378:metabolism; D000728:Androgens / Q000378:metabolism; D000911:Antibodies, Monoclonal; D002499:Centrifugation, Density Gradient; D003600:Cytosol / Q000378:metabolism; D005260:Female; D006801:Humans; D007700:Kinetics; D010051:Ovarian Neoplasms / Q000378:metabolism*
D000727:Androgen-Binding Protein; D000728:Androgens; D000911:Antibodies, Monoclonal