Andersen U O, Bøg-Hansen T C, Kirkeby S
Protein Laboratory, Faculty of Health Sciences, University of Copenhagen, Denmark.
Prostate. 1996 Dec;29(6):356-61. doi: 10.1002/(SICI)1097-0045(199612)29:6<356::AID-PROS3>3.0.CO;2-6.
A receptor for alpha 1-acid glycoprotein glycoforms AGP-B and AGP-C in the epithelium of the rat prostate gland and seminal vesicles is described.
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.
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.
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.
描述了大鼠前列腺和精囊上皮中α1-酸性糖蛋白糖型AGP-B和AGP-C的一种受体。
AGP糖型与其受体之间的相互作用是一种凝集素样相互作用，甘露糖和N-乙酰-D-葡萄糖胺对结合的抑制作用证实了这一点。
在体外，该受体也受到皮质酮、醛固酮、孕酮和雌二醇等甾体激素的抑制，但不受睾酮的抑制。在大鼠前列腺和精囊中，AGP凝集素受体的表达和AGP的定位存在显著的区域差异。将AGP凝集素受体的定位与糖蛋白AGP的定位进行比较，发现存在细微差异。
提出前列腺和精囊中的AGP受体属于一组在分化和器官形成控制中的凝集素。
