@article{1d96a9b0f1e911ddbf70000ea68e967b,
title = "Appearance and cellular distribution of lectin-like receptors for alpha 1-acid glycoprotein in the developing rat testis",
abstract = "A histochemical avidin-biotin technique with three different alpha 1-acid glycoprotein glycoforms showed pronounced alterations in the cellular localization of two alpha 1-acid glycoprotein lectin-like receptors during cell differentiation in the developing rat testis. The binding of alpha 1-acid glycoprotein glycoforms to their receptors is inhibited by steroids. Testosterone, oestradiol and progesterone inhibited the binding of alpha 1-acid glycoprotein glycoform A to its receptor. Cortisone, aldosterone, oestradiol and progesterone inhibited the binding of alpha 1-acid glycoprotein glycoforms B and C to their receptor. A difference in the cellular content of alpha 1-acid glycoprotein glycoforms and alpha 1-acid glycoprotein receptors separates the spermatocytes and the early spermatids from the late spermatids. The difference in receptor composition implies a difference in the effect of different steroid hormones. The Leydig cells contained alpha 1-acid glycoprotein and lectin-like receptors for one of the glycoforms of alpha 1-acid glycoprotein from birth. The interaction between alpha 1-acid glycoprotein glycoforms and their receptors may modulate the actions of testosterone and other steroids in the testis.",
author = "Andersen, {U O} and B{\o}g-Hansen, {T C} and S Kirkeby",
note = "Keywords: Aldosterone; Animals; Cells, Cultured; Cortisone; Estradiol; Histocytochemistry; Leydig Cells; Male; Mannose; Orosomucoid; Progesterone; Protein Binding; Rats; Receptors, Mitogen; Sertoli Cells; Spermatozoa; Testis; Testosterone",
year = "1996",
language = "English",
volume = "107",
pages = "11--6",
journal = "Reproduction",
issn = "1470-1626",
publisher = "BioScientifica Ltd.",
number = "1",
}