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Parathyroid hormone domain for protein kinase C stimulation located within amphiphilic helix

From National Research Council Canada

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EditorSearch for: Smith, John A.; Search for: Rivier, Jean E.
Affiliation
  1. National Research Council of Canada. NRC Institute for Biological Sciences
FormatText, Article
Conference12th American Peptide Symposium, June 16-21, 1991, Cambridge, Massachusetts, USA
ISSN01979000
ISBN90-72199-12-X
9789072199126
Abstract
Parathyroid hormone (PTH) plays a major role in regulating circulating levels of calcium. Biological activites of this 84-residue long peptide, as well as of the equipotent 1-34 fragment, are believed to be linked to the stimulation of adenylate cyclase activity [1]. However, recent data indicate that some major functions of PTH may be mediated by an alternative mechanism that involves stimulation of membrane-associated protein kinase C (PKC) [2]. To define the domain of the hormone responsible for PKC activation, we have synthesized a series of human PTH fragments and assayed them using ROS 17/2 rat osteosarcoma cells. Biological studies with PTH fragments were complimented by conformational analysis using the methods of CD spectroscopy, secondary structure predictions, and molecular dynamics simulations.
Publication date
In
  • Peptides: Chemistry and Biology (1992): 37–39.
LanguageEnglish
NRC numberNRC-IBD-317
NPARC number9147693
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Record identifier41636014-9673-488a-9e07-46dd4b1d0450
Record created2009-06-25
Record modified2020-04-24
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