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Osteoactivin acts as downstream mediator of BMP-2 effects on osteoblast function.

Authors
Abdelmagid-SM; Barbe-MF; Arango-Hisijara-I; Owen-TA; Popoff-SN; Safadi-FF
Source
J Cell Physiol 2007 Jan; 210(1):26-37
NIOSHTIC No.
20041716
Abstract
Our laboratory previously showed that osteoactivin (OA) is a novel, osteoblast-related glycoprotein that plays a role in osteoblast differentiation and function. The purpose of this study was to examine the regulation of OA expression by BMP-2 and the role OA plays as a downstream mediator of BMP-2 effects in osteoblast function. Using primary osteoblast cultures, we tested different doses of BMP-2 on the regulation of OA expression during osteoblast development. To test whether Smad-1 signaling is responsible for BMP-2 regulation of OA expression, osteoblast cultures were transfected with Smad1 siRNA, treated with 50 ng/ml of BMP-2 and analyzed by Western blot. BMP-2 treatment increased OA mRNA and protein expression in a dose-dependent manner and this upregulation was blocked in Smad1 siRNA transfected cultures. We next examined whether the role of OA as a downstream mediator of BMP-2 effects on osteoblast differentiation and matrix mineralization. Osteoblast cultures were transfected with OA antisense oligonucleotides and treated with 50 ng/ml of BMP-2. Cultures transfected with OA antisense oligonucleotides and treated with BMP-2 showed a reduction of OA expression associated with a significant reduction in early and late differentiation markers induced by BMP-2. Therefore, OA acts, at least in part, as a downstream mediator of BMP-2 effects on osteoblast differentiation and matrix mineralization. Our findings suggest that BMP-2 regulates OA expression through the Smad1 signaling pathway. Our data also emphasize that OA protein acts as a downstream mediator of BMP-2 effects on osteoblast differentiation and function.
Keywords
Animals; Glycoproteins; Tissue-culture; Bone-structure; Proteins; Genetics; Metabolism; Pharmacology; Drug-interaction; Dose-response; Cytology; Osteogenesis; Laboratory-animals
Contact
Dr. Fayez F. Safadi, Associate Professor, Department of Anatomy and Cell Biology, Temple University School of Medicine, 3400 North Broad Street, Philadelphia, PA 19140
CODEN
JCLLAX
Publication Date
20070101
Document Type
Journal Article
Email Address
fsafadi@temple.edu
Funding Type
Cooperative Agreement
Fiscal Year
2007
NTIS Accession No.
NTIS Price
Identifying No.
Cooperative-Agreement-Number-U01-OH-008599
Issue of Publication
1
ISSN
0021-9541
Source Name
Journal of Cellular Physiology
State
PA; CT
Performing Organization
Temple University, Philadelphia, Pennsylvania
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