Lectin-binding sites in human parathyroid tissue.
Open Access
- 1 September 1986
- journal article
- research article
- Published by SAGE Publications in Journal of Histochemistry & Cytochemistry
- Vol. 34 (9) , 1201-1206
- https://doi.org/10.1177/34.9.3734421
Abstract
The aim of this study was to demonstrate several lectin-binding sites in human parathyroid tissue and to correlate these results with functional activity. The following lectins were tested for binding sites with certain carbohydrates (in parentheses): Arachis hypogea (PNA) (galactose), Ulex europaeus I (UEA) (fucose) and concanavalin A (ConA) (mannose). In addition to normal parathyroids used as controls (13 cases), we examined adenomas associated with a clinical picture of primary hyperparathyroidism of differing severity (31 cases), atrophic glands contralateral to a hyperfunctioning adenoma (7 cases), and secondary (renal) hyperplasia (12 cases). Use of PNA (with and without neuraminidase treatment) and UEA yielded negative staining in normal glands, a wide variety of reactions in adenomas, and frequent dense precipitates in atrophic parathyroids, whereas ConA yielded positive staining in all kinds of parathyroid tissue. Assessment of functional activity of adenomas by clinical parameters (pre-operative serum levels of calcium and parathormone) displayed a significant correlation with the semiquantitative grading of the histochemical reactions after PNA and UEA. Lectin-binding sites in parathyroid chief cells of adenomas are believed to indicate some of the cell structures or products directly involved in the secretory process, including degradation. Although ConA may recognize constituent parathyroid glycoproteins, the binding sites for PNA and UEA are thought to be partially associated with secretory glycoprotein (SP-I), as is known from animal experiments. The positive reaction of the atrophic gland may result from degradation enforced by exposure of primarily non-terminal carbohydrate components.This publication has 11 references indexed in Scilit:
- Chromogranin A: Immunohistology reveals its universal occurrence in normal polypeptide hormone producing endocrine glandsLife Sciences, 1983
- Influence on parathyroid hormone storage in normal and adenomatous parathyroid tissue by stimulation and inhibition in vitro.Journal of Histochemistry & Cytochemistry, 1983
- Similarity of secretory protein I from parathyroid gland to chromogranin A from adrenal medulla.Proceedings of the National Academy of Sciences, 1982
- Cellular and cell-free processing of parathyroid secretory proteins.Journal of Biological Chemistry, 1982
- Isolation and partial characterization of secretory protein I from bovine parathyroid glandsBiochemistry, 1981
- Changes in the plasma membrane associated with endocrine activityVirchows Archiv B Cell Pathology Including Molecular Pathology, 1980
- Synthesis, intracellular distribution, and secretion of multiple forms of parathyroid secretory protein-I.Proceedings of the National Academy of Sciences, 1980
- Regulation of secretion of parathormone and secretory protein-I from separate intracellular pools by calcium, dibutyryl cyclic AMP, and (1)-isoproterenol.The Journal of cell biology, 1979
- The secretion of parathormone and glycosylated proteins by parathyroid cells in cultureBiochemical and Biophysical Research Communications, 1978
- CYTOCHEMICAL DEMONSTRATION OF PEROXIDASE ACTIVITY WITH 3-AMINO-9-ETHYLCARBAZOLEJournal of Histochemistry & Cytochemistry, 1965