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

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EditorSearch for: Smith, John A.; Search for: Rivier, Jean E.
TypeArticle
Proceedings titlePeptides: Chemistry and Biology
Conference12th American Peptide Symposium, June 16-21, 1991, Cambridge, Massachusetts, USA
ISSN01979000
ISBN90-72199-12-X
9789072199126
Pages3739; # of pages: 3
AbstractParathyroid 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
PublisherEscom Science Publishers
LanguageEnglish
AffiliationNRC Institute for Biodiagnostics; National Research Council Canada; NRC Institute for Biological Sciences
Peer reviewedNo
NRC number317
NPARC number9147693
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Record identifier41636014-9673-488a-9e07-46dd4b1d0450
Record created2009-06-25
Record modified2016-05-09
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