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Originally published In Press as doi:10.1074/jbc.M110398200 on January 22, 2002

J. Biol. Chem., Vol. 277, Issue 14, 11828-11837, April 5, 2002
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1alpha ,25(OH)2D3 Regulates Chondrocyte Matrix Vesicle Protein Kinase C (PKC) Directly via G-protein-dependent Mechanisms and Indirectly via Incorporation of PKC during Matrix Vesicle Biogenesis*

Zvi SchwartzDagger §, Victor L. Sylvia§, Dennis Larsson§||, Ilka Nemere||, David Casasola§, David D. Dean§, and Barbara D. Boyan§

From the Dagger  Hebrew University, Jerusalem 91120, Israel, § The University of Texas Health Science Center at San Antonio, San Antonio, Texas 78229-3900, and || Utah State University, Logan, Utah 84322

Matrix vesicles are extracellular organelles involved in mineral formation that are regulated by 1alpha ,25(OH)2D3. Prior studies have shown that protein kinase C (PKC) activity is involved in mediating the effects of 1alpha ,25(OH)2D3 in both matrix vesicles and plasma membranes. Here, we examined the regulation of matrix vesicle PKC by 1alpha ,25(OH)2D3 during biogenesis and after deposition in the matrix. When growth zone costochondral chondrocytes were treated for 9 min with 1alpha ,25(OH)2D3, PKCzeta in matrix vesicles was inhibited, while PKCalpha in plasma membranes was increased. In contrast, after treatment for 12 or 24 h, PKCzeta in matrix vesicles was increased, while PKCalpha in plasma membranes was unchanged. The effect of 1alpha ,25(OH)2D3 was stereospecific and metabolite-specific. Monensin blocked the increase in matrix vesicle PKC after 24 h, suggesting the secosteroid-regulated packaging of PKC. In addition, the 1alpha ,25(OH)2D3 membrane vitamin D receptor (1,25-mVDR) was involved, since a specific antibody blocked the 1alpha ,25(OH)2D3-dependent changes in PKC after both long and short treatment times. In contrast, antibodies to annexin II had no effect, and there was no evidence for the presence of the nuclear VDR on Western blots. To investigate the signaling pathways involved in regulating matrix vesicle PKC activity after biosynthesis, matrix vesicles were isolated and then treated for 9 min with 1alpha ,25(OH)2D3 in the presence and absence of specific inhibitors. Inhibition of phosphatidylinositol-phospholipase C, phospholipase D, or Gi/Gs had no effect. However, inhibition of Gq blocked the effect of 1alpha ,25(OH)2D3. The rapid effect of 1alpha ,25(OH)2D3 also involved the 1,25-mVDR. Moreover, arachidonic acid was found to stimulate PKC when added directly to isolated matrix vesicles. These results indicate that matrix vesicle PKC is regulated by 1alpha ,25(OH)2D3 at three levels: 1) during matrix vesicle biogenesis; 2) through direct action on the membrane; and 3) through production of other factors such as arachidonic acid.

* This research was supported by United States Public Health Service Grants DE-08603 and DE-05937 and the Center for the Enhancement of the Biology/Biomaterials Interface at University of Texas Health Science Center at San Antonio.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: Dept. of Orthopaedics, MSC 7774, The University of Texas Health Science Center at San Antonio, 7703 Floyd Curl Dr., San Antonio, TX 78229-3900. Tel.: 210-567-6326; Fax: 210-567-6295; E-mail: BoyanB@uthscsa.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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