help button home button Am J Pathol ASIP 2008 Summer Academy, Molecular Methcanisms of Human Disease: Injury, Inflammation, and Tissue Repair
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS

This Article
Right arrow Order Full text via Infotrieve
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by McGregor, D. H.
Right arrow Articles by Cohn, D. V.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by McGregor, D. H.
Right arrow Articles by Cohn, D. V.

American Journal of Pathology, Vol 102, 336-345, Copyright © 1981 by American Society for Investigative Pathology


REGULAR ARTICLES

The effects of tris(hydroxymethyl)aminomethane and calcium ionophores on the biosynthesis of proparathormone and the formation and degradation of parathormone in bovine parathyroid tissue

DH McGregor, JJ Morrissey and DV Cohn

A comparative study of ultrastructural and biochemical effects of Tris and ionophores X537A and A23187 on bovine parathyroid tissue is presented. When parathyroid slices were incubated with 3H-leucine and 3H-lysine for 10 minutes alone or with Tris (50 mM), A23187 (9.5-19 microM) or X537A (8.5-17 microM), the incorporation of the amino acids into radioactive proparathormone (proPTH) was similar, indicating that biosynthesis of the hormone was not affected. After 120 minutes of incubation, however, Tris inhibited the conversion of proPTH to parathormone (PTH), judged by a decrease in cellular and secreted radioactive PTH and a corresponding increase in radioactive cellular proPTH. These changes were accompanied by marked dilatation of Golgi membranes. With both concentrations of A23187 and the low concentration of X537A there were no changes in amounts of radioactive proPTH, moderate decreases in cellular and secreted radioactive PTH, and little discernible distension of the Golgi membranes. At 17 microM X537A there was moderate increase in amount of radioactive proPTH, a marked decrease in amount of radioactive PTH and swelling of the Golgi membranes. Taken together, these findings suggest that Tris inhibited conversion of proPTH to PTH by disrupting the Golgi zone-the site of conversion of proPTH to PTH; that A23187 and the low concentration of X537A decreased production of PTH by enhancing its degradation; and that X537A at the higher concentration acted both by inhibiting conversion of proPTH to PTH and by enhancing the degradation of PTH.





HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1981 by the American Society for Investigative Pathology.