Appearance and cellular distribution of lectin-like receptors for alpha 1-acid glycoprotein in the developing rat testis
Research output: Contribution to journal › Journal article › Research › peer-review
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.
Original language | English |
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Journal | Reproduction |
Volume | 107 |
Issue number | 1 |
Pages (from-to) | 11-6 |
Number of pages | 5 |
ISSN | 1470-1626 |
Publication status | Published - 1996 |
Bibliographical 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
ID: 10116167