C-terminal fragments of parathyroid hormone-related protein, PTHrP-(107-111) and (107-139), and the N-terminal PTHrP-(1-40) fragment stimulate membrane-associated protein kinase C activity in rat spleen lymphocytes

  • J Cell Physiol. 1994 Mar;158(3):518-22. doi: 10.1002/jcp.1041580317.
J F Whitfield  1 ,  R J Isaacs ,  B R Chakravarthy ,  J P Durkin ,  P Morley ,  W Neugebauer ,  R E Williams ,  G Willick ,  R H Rixon
Affiliations
  • 1. Cell Systems Section, National Research Council of Canada, Ottawa, Ontario.
PMID: 8126075 DOI: 10.1002/jcp.1041580317
Abstract

Membrane-associated protein kinase C (PKC) activity in lymphocytes freshly isolated from rat spleen was stimulated by the C-terminal parathyroid hormone-related protein fragments, PTHrP-(107-111) and PTHrP-(107-139), at concentrations from 10(-3) to 10(4) pM. By contrast, the same concentrations of PTHrP-(120-139), without the 107-111 TRSAW (-Thr-Arg-Ser-Ala-Trp-) sequence of the Other C terminal fragments, did not stimulate spleen lymphocyte PKC. Low concentrations of the N-terminal PTHrP-(1-40) fragment also stimulated membrane-associated PKC activity in the spleen lymphocytes. These results suggest that PTHrP might be an important physiological regulator of the immune response.

Products