Metalloproteinase activity in growth plate chondrocyte cultures is regulated by 1,25-(OH)(2)D(3) and 24,25-(OH)(2)D(3) and mediated through protein kinase C

Matrix Biology : Journal of the International Society for Matrix Biology
S MaedaZ Schwartz

Abstract

During endochondral development, growth plate chondrocytes must remodel their matrix in a number of ways as they differentiate and mature. In previous studies, we have shown that matrix metalloproteinases (MMPs) extracted from matrix vesicles can extensively degrade aggrecan and that this is modulated by vitamin D metabolites in a manner involving protein kinase C (PKC). Matrix vesicles represent only a small component of the extracellular matrix, however, and it is unknown if the total metalloproteinase complement, including the MMPs and aggrecanases in the culture, is also regulated in a similar way. This study tested the hypothesis that vitamin D metabolites regulate the level of metalloproteinase activity in growth plate chondrocytes via a PKC-dependent mechanism and play a role in partitioning this proteinase activity between the media and cell layer (cells+matrix) in these cultures. To do this, resting zone cells (RC) were treated with 10(-9)-10(-7) M 24R,25-(OH)(2)D(3), while growth zone cells (GC) were treated with 10(-10)-10(-8) M 1alpha,25-(OH)(2)D(3). Cultures of both cell types were also treated with the PKC inhibitor chelerythrine in the presence and absence of vitamin D metabolites. At harvest, the media were eith...Continue Reading

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Citations

Oct 12, 2001·The Journal of Steroid Biochemistry and Molecular Biology·V L SylviaZ Schwartz
Jan 1, 2015·ELife·Igor VivancoIngo K Mellinghoff
Sep 26, 2006·Advances in Virus Research·Sijun LiuBryony C Bonning
Jul 5, 2002·Critical Reviews in Oral Biology and Medicine : an Official Publication of the American Association of Oral Biologists·B D BoyanZ Schwartz
Mar 17, 2009·Journal of Cellular Biochemistry·Tracy A DenisonBarbara D Boyan
Sep 30, 2009·Biochimica Et Biophysica Acta·Ellis E Golub

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