help button home button Endocrine Society Endocrinology
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS

This Article
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
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 Request Copyright Permission
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by el-Hajj Fuleihan, G.
Right arrow Articles by Brown, E. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by el-Hajj Fuleihan, G.
Right arrow Articles by Brown, E. M.

Endocrinology, Vol 128, 2931-2936, Copyright © 1991 by Endocrine Society


ARTICLES

Effects of the lectin concanavalin-A on the regulation of second messengers and parathyroid hormone release by extracellular Ca2+ in bovine parathyroid cells

G el-Hajj Fuleihan, C Katz, O Kifor, R Gleason and EM Brown
Endocrine-Hypertension Unit, Brigham and Women's Hospital, Boston, Massachusetts 02115.

The lectin Concanavalin-A (Con-A) binds to cell surface carbohydrate- containing moieties and modulates the function of a variety of glycoprotein receptors. Since extracellular calcium (Ca2+) may regulate parathyroid function by a receptor-like process, we examined the effects of Con-A on various aspects of Ca(2+)-regulated parathyroid function. We recently showed that Con-A significantly reduces the inhibitory effects of high Ca2+ on dopamine as well as isoproterenol- and forskolin-stimulated cAMP accumulation. In our present studies Con- A similarly reduced the inhibitory effect of 2.0 mM Ca2+ on PTH release from 60 +/- 6% to 40 +/- 6% and increased the set-point for Ca(2+)- regulated PTH release from 1.25 to 1.8 mM. This effect was dose dependent. Con-A also inhibited the Ca(2+)-stimulated accumulation of inositol phosphates by 50-60% in association with a marked reduction in the high Mg(2+)-evoked spike in cytosolic Ca2+ as well as a significant decrease in the sustained rise in cytosolic Ca2+ at 2-3 mM extracellular Ca2+. These data provide further evidence for a key role for cell surface carbohydrate-containing moieties in the mechanism through which parathyroid cells "sense" Ca2+ and, in turn, regulate PTH release, phosphoinositide turnover, and the release of intracellular Ca2+ stores. It is possible that the putative Ca2+ receptor is a glycoprotein or is closely associated with glycoproteins or other moieties containing alpha-methyl-D-glucoside or alpha-methyl-D- mannoside residues.


This article has been cited by other articles:


Home page
J. Biol. Chem.Home page
J. E. Garrett, I. V. Capuano, L. G. Hammerland, B. C. P. Hung, E. M. Brown, S. C. Hebert, E. F. Nemeth, and F. Fuller
Molecular Cloning and Functional Expression of Human Parathyroid Calcium Receptor cDNAs
J. Biol. Chem., May 26, 1995; 270(21): 12919 - 12925.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Endocrinology Endocrine Reviews J. Clin. End. & Metab.
Molecular Endocrinology Recent Prog. Horm. Res. All Endocrine Journals
Copyright © 1991 by The Endocrine Society