The secretion of parathormone and glycosylated proteins by parathyroid cells in culture

Jeremiah J. Morrissey, James W. Hamilton, David V. Cohn

Research output: Contribution to journalArticlepeer-review

16 Scopus citations

Abstract

The secretion of radioactive peptides by dispersed porcine parathyroid cells incubated with [3H]- or [14C]amino acids, [3H]glucosamine and [3H]mannose was analyzed. After incubation, the culture medium contained radioactive parathormone, as expected, and two radioactive glycopeptides: SP I and SP II. SP I appears to be identical with parathyroid secretory protein, heretofore not recognized as a glycoprotein. SP II has not been previously identified. SP I, but not SP II or parathormone, was adsorbed by Concanavalin A possibly reflecting a high mannose content of this molecule. Raising the concentration of calcium in the medium suppressed the secretion of radioactive parathormone and SP I in a similar fashion but did not affect the secretion of SP II. Our results suggest that SP I may play a fundamental role in parathyroid synthetic or secretory processes.

Original languageEnglish
Pages (from-to)1279-1286
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume82
Issue number4
DOIs
StatePublished - Jun 29 1978

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