Proteinase-activated receptor-2 (PAR(2)) and mouse osteoblasts: Regulation of cell function and lack of specificity of PAR(2)-activating peptides
Smitha R Georgy, Charles N Pagel, David M Wong, Sutharshani Sivagurunathan, Lay H Loh, Damian E Myers, Morley D Hollenberg, Robert N Pike, Eleanor J Mackie
CLINICAL AND EXPERIMENTAL PHARMACOLOGY AND PHYSIOLOGY | WILEY-BLACKWELL | Published : 2010
1. Using synthetic proteinase-activated receptor-2 (PAR(2))-activating peptides (PAR(2)APs) corresponding to the tethered ligand domain of the extracellular N-terminus of PAR(2) to mimic the actions of activating proteinases and using primary cultures of calvarial osteoblasts derived from both wild-type (WT) and PAR(2)-null (KO) mice, we investigated the potential role of PAR(2) in regulating osteoblast function. 2. Primary calvarial osteoblasts from WT and KO mice were evaluated for their growth kinetics and mineralization in the absence of PAR(2) agonists and for their responses in a variety of functional assays to the PAR(2)APs Ser-Leu-Ile-Gly-Arg-Leu-amide (SLIGRL-NH(2)) and 2-furoyl-Leu..View full abstract
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Awarded by National Health and Medical Research Council of Australia
This work was supported by a National Health and Medical Research Council of Australia Program Grant (284233), with minor support from a Canadian Institutes of Health Research operating grant (to MDH). The authors thank Ms S Toulson (School of Veterinary Science, University of Melbourne) for the care of the mouse colony and excellent technical assistance.