Regulation of ADAMTS-2 by 1,25-dihydroxyvitaminD3 in osteoblastic cells.

Cited 0 time in Web of Science Cited 0 time in Scopus

Lee, Seungbok; Jeon, Eun-Young; Kim, Hyun-Man

Issue Date
Korean Acadamy of Oral Biology
International Journal of Oral Biology. 31:93-98
Biosynthetic processing of fibrillar procollagens is
essential for producing mature collagen monomers that
polymerize into fibrils by a self-assembly process. The
metalloproteinase ADAMTS-2 is the major enzyme that
processes the N-propeptide of type I procollagen in the skin
and also of type II and type III procollagens. Mutations in
the ADAMTS-2 gene cause dermatospraxis in animals and
Ehlers-Danlos syndrome VIIC in humans, both of which
are characterized by the accumulation of type I pN-collagen
and the formation of abnormal collagen fibrils in the skin.
Despite its importance in procollagen processing, little is
known about the regulation of ADAMTS-2 expression.
Here, we demonstrate that ADAMTS-2 can be regulated by
1,25-dihydroxyvitamin D3, an inducer of type I procollagen
synthesis. This steroid hormone induced ADAMTS-2
mRNA ~3-fold in MG-63 human osteosarcoma cells and
MC3T3-E1 murine osteoblastic cells. This induction was
dose- and time-dependent in MG-63 cells. In contrast,
secreted ADAMTS-2 protein was increased only 1.4-fold with
1,25-dihydroxyvitamin D3. Finally, 1,25-dihydroxyvitamin
D3 in the presence of ascorbate increased levels of secreted
ADAMTS-2 1.9-fold over ascorbate treatment alone, which
did not appreciably change ADAMTS-2 expression. These
data indicate that the regulation of ADAMTS-2 is coupled
with the synthesis of type I procollagen through 1,25-
dihydroxyvitamin D3 signaling and may involve translational
or posttranslational control.
Files in This Item:
Appears in Collections:
College of Dentistry/School of Dentistry (치과대학/치의학대학원)Dept. of Dentistry (치의학과)Journal Papers (저널논문_치의학과)
  • mendeley

Items in S-Space are protected by copyright, with all rights reserved, unless otherwise indicated.