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Insulin-Like Growth Factor-I Receptors in Human Hyperplastic Prostate Tissue: Characterization, Tissue Localization, and Their Modulation by Chronic Treatment with a Gonadotropin-Releasing Hormone Analog^*

GIANNA FIORELLI, ALESSANDRA De BELLIS, ANTONELLA LONGO, STEFANO GIANNINI, ALESSANDRO NATALI, ALFIERO COSTANTINI, GABRIELLA B. VANNELLI and MARIO SERIO

Endocrinology Unit, Department of Clinical Physiopathology, (G.F.; A.D.; A.L.; S.G.; M.S.), Department of Urology (A.N.; A.C.), and Department of Human Anatomy (G.B. V.), University of Florence Florence, Italy

Address correspondence and requests for reprints to: Dr. Gianna Fiorelli, Endocrinology Unit, Department of Clinical Physiopathology, University of Florence, Viale Pieraccini 6, 50134 Florence, Italy.

Recipient of a fellowship from AIRC (Milan, Italy).

Insulin-like growth factor I (IGF-I) receptors were characterized in membranes obtained from prostate tissue of patients affected by benign prostatic hyperplasia (BPH) before and after treatment with a GnRH agonist analog. Bindingof [¹²⁵I] IGF-I to membranes obtained from untreated patients was specific and time and temperature dependent. Analysis of the binding data yielded two classes of binding sites, one of high affinity (K_d, 10^–11 mol/L) and one of lower affinity (K_d, 10^–9 mol/L). BPH membrane preparations were affinity-cross linked to labeled IGF-I, and then subjected to sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Analysis by autoradiography revealed one labeled protein with an apparent M_r = 300K under nonreducing conditions and two labeled proteins with M_r = 270K and M_r = 130K under reducing conditions. Excess unlabeled IGF-II reduced both of them, whereas the same excess of IGF-I completely abolished them.

In membrane preparations of prostatic tissues from patients affected by BPH and treated for 2 months with a GnRH agonist analog, the binding capacities of both binding sites were significantly higher than those of BPH tissue from untreated patients, whereas binding affinities were unchanged.

The IGF-I receptor in BPH prostate tissue of untreated patients was mainly localized in the basal layer of the epithelium, as demonstrated by immunohistochemical staining, whereas in the tissue from treated patients positive staining was found also in the glandular epithelium.

These results demonstrate that: 1) specific binding sites for IGF-I are present in prostatic tissue from patients with BPH, 2) androgen deprivation increases their binding capacities and seems to modify their epithelial localization. (J Clin Endocrinol Metab 72: 740–746, 1991)

^* This work was supported in part by a grant from the Associazione Italiana per la Ricerca sul Cancro, by a Grant from C.N.R. (program, Senescence), and by a grant from the University of Florence.

Received May 10, 1990.

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