Appearance and cellular distribution of lectin-like receptors for α1-acid glycoprotein in the developing rat testis

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Authors:
U. O. Andersen
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T. C. Bøg-Hansen
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, and
S. Kirkeby
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DOI:
https://doi.org/10.1530/jrf.0.1070011
Volume/Issue:
Volume 107: Issue 1
Page Range:
11–16
Article Type:
Research Article
Online Publication Date:
May 1996
Free access

A histochemical avidin–biotin technique with three different α1-acid glycoprotein glycoforms showed pronounced alterations in the cellular localization of two α1-acid glycoprotein lectin-like receptors during cell differentiation in the developing rat testis. The binding of α1-acid glycoprotein glycoforms to their receptors is inhibited by steroids. Testosterone, oestradiol and progesterone inhibited the binding of α1-acid glycoprotein glycoform A to its receptor. Cortisone, aldosterone, oestradiol and progesterone inhibited the binding of α1-acid glycoprotein glycoforms B and C to their receptor. A difference in the cellular content of α1-acid glycoprotein glycoforms and α1-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 α1-acid glycoprotein and lectin-like receptors for one of the glycoforms of α1-acid glycoprotein from birth. The interaction between α1-acid glycoprotein glycoforms and their receptors may modulate the actions of testosterone and other steroids in the testis.

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Print ISSN:
1470-1626
Online ISSN:
1741-7899