Lectin-like receptor for α1-acid glycoprotein in the epithelium of the rat prostate gland and seminal vesicles

• Published in: The Prostate Vol. 29; no. 6; pp. 356 - 361
• Main Authors: Andersen, Ulla Overgaard, Bøg-Hansen, Thorkild C., Kirkeby, Svend
• Format: Journal Article
• Language: English
• Published: New York Wiley Subscription Services, Inc., A Wiley Company 01.12.1996; Wiley-Liss
• Subjects: Biological and medical sciences; Fundamental and applied biological sciences. Psychology; glycoforms; lectins; prostate gland; receptors; seminal vesicles; Vertebrates: urinary system; α1-acid glycoprotein; Lectin; Rat; Seminal vesicle; Rodentia; Epithelium; Male genital system; Vertebrata; Mammalia; Urinary system; Animal; α1-acid-Glycoprotein; Prostate; Histochemistry; Biological receptor
• ISSN: 0270-4137; 1097-0045
• DOI: 10.1002/(SICI)1097-0045(199612)29:6<356::AID-PROS3>3.0.CO;2-6

BACKGROUND A receptor for α1‐acid glycoprotein glycoforms AGP‐B and AGP‐C in the epithelium of the rat prostate gland and seminal vesicles is described. METHODS The interaction between AGP‐glycoforms and their receptor is a lectin‐like interaction confirmed by inhibition of the binding by mannose and N‐Acetyl‐D‐glucosamine. RESULTS In vitro the receptor was also inhibited by the steroid hormones cortisone, aldosterone, progesterone, and estradiol, but not by testosterone. A significant regional variation in the expression of AGP‐lectin receptor and in the localization of AGP was seen in rat prostate and seminal vesicles. The localization of the AGP lectin receptor is compared to the localization of glycoprotein AGP, and small differences are found. CONCLUSIONS It is proposed the AGP receptors in the prostate and seminal vesicles belong to a group of lectins in the control of differentiation and organ formation. © 1996 Wiley‐Liss, Inc.