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1.
Acta Histochem ; 101(1): 113-9, 1999 Feb.
Article in English | MEDLINE | ID: mdl-10093645

ABSTRACT

Using a histochemical technique with three different alpha 1-acid glycoprotein glycoform one glycoform specific receptor has been identified in human adrenal cortex. The receptor is associated to alpha 1-acid glycoprotein glycoform B and alpha 1-acid glycoprotein glycoform C. The glycoform specific receptor was located in the cytoplasm of glomerulosa and outer fasciculata cells. The intensity of the reaction product decreased in the fasciculata, and no staining was seen in inner fasciculata and reticularis. Inhibition with the simple sugars, mannose and GlcNAc confirmed a lectin-like reaction. The binding activity was dependent on the presence of calcium ions and not on thiol reagents. Thus the lectin-like receptor may belong to the C-type lectin family. Using an antibody to alpha 1-acid glycoprotein the presence of alpha 1-acid glycoprotein was observed in the same location as the glycoform specific receptor. The binding of alpha 1-acid glycoprotein glycoform B and alpha 1-acid glycoprotein glycoform C to the glycoform specific receptor is inhibited by the steroid hormones cortisone, aldosterone, estradiol and progesterone but not by testosterone. The pronounced changes in the distribution of AGP and its glycoform receptors during cell differentiation in the adrenal cortex suggest that AGP and its complementary lectins belong to the group of lectins which control differentiation and spatial position.


Subject(s)
Adrenal Cortex/metabolism , Glycoprotein Hormones, alpha Subunit/metabolism , Lectins, C-Type , Platelet Glycoprotein GPIb-IX Complex , Platelet Membrane Glycoproteins , Receptors, Cell Surface/metabolism , Adrenal Cortex/anatomy & histology , Humans , Immunohistochemistry
2.
Prostate ; 29(6): 356-61, 1996 Dec.
Article in English | MEDLINE | ID: mdl-8977632

ABSTRACT

BACKGROUND: 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. 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.


Subject(s)
Orosomucoid/metabolism , Platelet Glycoprotein GPIb-IX Complex , Platelet Membrane Glycoproteins , Prostate/chemistry , Receptors, Cell Surface/analysis , Receptors, Cell Surface/metabolism , Receptors, Mitogen/analysis , Receptors, Mitogen/metabolism , Seminal Vesicles/chemistry , Aldosterone/pharmacology , Animals , Cell Differentiation/physiology , Cell Division/physiology , Cortisone/pharmacology , Epithelial Cells , Epithelium/chemistry , Epithelium/physiology , Estradiol/pharmacology , Immunohistochemistry , Male , Orosomucoid/physiology , Progesterone/pharmacology , Prostate/cytology , Prostate/physiology , Rats , Receptors, Cell Surface/drug effects , Receptors, Mitogen/drug effects , Seminal Vesicles/cytology , Seminal Vesicles/physiology
3.
J Mol Recognit ; 9(5-6): 364-7, 1996.
Article in English | MEDLINE | ID: mdl-9174911

ABSTRACT

Three glycoforms of alpha 1-acid glycoprotein (AGP) were biotinylated to examine their binding in mouse testis by light microscopy. The transition from one stage to another in the spermatogenic cycle is marked with an appearance of a receptor for the Concanavalin A (Con A) non-reactive glycoform AGP-A in the cytoplasm of spermatocytes, young spermatids and Sertoli cells. This receptor disappears in the late stages of the spermatids. The Con-A intermediately reactive and the Con-A reactive glycoforms, AGP-B and AGP-C, showed weak reaction in the cytoplasm of spermatocytes, spermatids and Sertoli cells and, at the last stages in the spermatogenic cycle, a very strong reaction in the late elongated spermatids and the apical extensions of Sertoli cells. The interactions are lectin-like as confirmed by inhibition with simple sugars. In addition, the bindings were inhibited by steroid hormones. AGP-A was inhibited by testosterone, oestradiol and progesterone, while AGP-B and AGP-C were inhibited by mannose, GlcNAc, cortisone, aldosterone, oestradiol and progesterone. The receptors and the corresponding AGP glycoforms may be adhesion molecules between Sertoli cells and the spermatogenic cells and may have a function as a regulatory factor for spermatozoa development.


Subject(s)
Lectins/metabolism , Orosomucoid/metabolism , Receptors, Cell Surface/metabolism , Testis/metabolism , Animals , Humans , Male , Mice , Testis/cytology
4.
J Reprod Fertil ; 107(1): 11-6, 1996 May.
Article in English | MEDLINE | ID: mdl-8699423

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.


Subject(s)
Orosomucoid/metabolism , Receptors, Mitogen/analysis , Testis/metabolism , Aldosterone/pharmacology , Animals , Cells, Cultured , Cortisone/pharmacology , Estradiol/pharmacology , Histocytochemistry , Leydig Cells/metabolism , Male , Mannose/pharmacology , Progesterone/pharmacology , Protein Binding/drug effects , Rats , Sertoli Cells/metabolism , Spermatozoa/metabolism , Spermatozoa/physiology , Testis/growth & development , Testosterone/pharmacology
5.
Ugeskr Laeger ; 152(10): 653-5, 1990 Mar 05.
Article in Danish | MEDLINE | ID: mdl-2181747

ABSTRACT

Experimental hypertensive vascular damage in rats resembles periarteritis nodosa microscopically and thus resembles immunologically produced cell infiltration. The immune system in patients with hypertension has, therefore, been investigated. High serum concentrations of immune globulins and increased prevalence of auto-antibodies have been found. Immune complexes and deposition of complement are present in the renal arteries. On transfer of lymphocytes from hypertensive experimental animals, normotensive animals develop hypertension and vascular changes resembling periarteritis nodosa. The leucocyte-migration-inhibition test demonstrates a cell-mediated immunological reaction to vascular wall antigens. Normal thymus function is essential for maintenance of the chronic phase of hypertension and for development of vascular wall changes. The genetic conditions are still obscure but a definite association to the C3F gene has, however, been found. The investigation reveals immunological reactions occur in arterial hypertension. It is not yet possible to differentiate between immunological reactions in the pathogenesis of hypertension and immunological reactions caused by hypertensive vascular damage. According to one of the hypotheses about the mechanisms of action, the immunological processes are mediated by complement. Complement activation may be initiated by a virus inter alii. Thus, hypertension may possibly be compared with other auto-immune disease where virus infections and genetic conditions are of great significance in the pathogenesis.


Subject(s)
Hypertension/immunology , Animals , Antibodies/analysis , Complement Activation/genetics , Humans , Immunity, Cellular/genetics , Rats
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