Glycosylation reduces the bioactivity of calcitonin

Peter J. Gkonos, Harry Charbonneau, Phillip T. Lawson, Guy A. Howard, Roger S. Birnbaum, Bernard A. Roos

Research output: Contribution to journalArticle

3 Scopus citations

Abstract

The biological significance of peptide hormone glycosylation is uncertain. To examine the effect of Asn-linked glycosylation on calcitonin's bioactivity we purified glycosylated calcitonin from a transplantable rat medullary thyroid carcinoma. Glycosylated calcitonin constituted 2.3% of the total extracted immunoreactive calcitonin. The structure of this peptide differed from nonglycosylated calcitonin only by the oligosaccharide modification of asparagine 3. Affinity of glycosylated calcitonin for lentil lectin indicated that the oligosaccharide was a complex processed form. In a standard in vivo bioassay glycosylated calcitonin had a markedly reduced hypocalcemic activity compared to nonglycosylated calcitonin, an effect most likely due to the presence of the oligosaccharide.

Original languageEnglish (US)
Pages (from-to)137-143
Number of pages7
JournalPeptides
Volume10
Issue number1
DOIs
StatePublished - Jan 1 1989

Keywords

  • Calcitonin
  • Glycosylation
  • Medullary thyroid carcinoma

ASJC Scopus subject areas

  • Biochemistry
  • Endocrinology
  • Physiology
  • Cellular and Molecular Neuroscience

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  • Cite this

    Gkonos, P. J., Charbonneau, H., Lawson, P. T., Howard, G. A., Birnbaum, R. S., & Roos, B. A. (1989). Glycosylation reduces the bioactivity of calcitonin. Peptides, 10(1), 137-143. https://doi.org/10.1016/0196-9781(89)90090-9