The secretion of parathormone and glycosylated proteins by parathyroid cells in culture |
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Authors: | Jeremiah J Morrissey James W Hamilton David V Cohn |
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Institution: | 1. Calcium Research Laboratory, Veterans Administration Hospital, Kansas City, Missouri 64128, USA;2. Department of Biochemistry, University of Kansas Medical Center, College of Health Sciences and Hospital, Kansas City, Kansas 66103 USA |
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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 , 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. |
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