Carboxy-terminal PTH fragments stimulate [3H]thymidine incorporation in vascular endothelial cells

Research output: Contribution to journalArticle

1 Scopus citations

Abstract

We have previously reported that the intact PTH molecule (1-84) stimulates proliferation of human umbilical vein endothelial cells (HUVECs). To define the bioactive portion of the PTH molecule we utilized amino, mid and carboxy-terminal PTH fragments. Carboxy- but not amino-terminal fragments were equivalent to the intact PTH molecule in stimulating [3H]thymidine incorporation in HUVEC. Carboxy- but not amino-terminal PTH fragments increased intracellular calcium. Blocking the rise in intracellular calcium with calcium chelators abolished PTHs proliferative effect on HUVEC. In contrast to PTH 1-84, the carboxy-terminal fragment effect on [3H]thymidine incorporation was blocked by KN-93 an inhibitor of CaM kinase II. Taken together, these data suggest that the carboxy-terminal PTH is (or contains) the bioactive fragment responsible for the changes in intracellular calcium and thymidine incorporation in HUVEC stimulated with the intact PTH molecule.

Original languageEnglish (US)
Pages (from-to)853-862
Number of pages10
JournalPeptides
Volume26
Issue number5
DOIs
StatePublished - May 2005

Keywords

  • Calcium
  • Endothelial cells
  • PTH
  • Proliferation
  • Receptors
  • Signaling

ASJC Scopus subject areas

  • Biochemistry
  • Physiology
  • Endocrinology
  • Cellular and Molecular Neuroscience

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