Abstract

The Protein Biochemistry Program works to understand the molecular mechanisms that lead to normal and pathological mineralization of extracellular matrices, particularly bones and teeth. Our working hypothesis is that the addition/modification of specific noncollagenous proteins and in the case of bone and dentin, specific changes in the collagen matrix lead to an orderly mineralization of these important tissues. Furthermore, inappropriate expression or accumulation of some of these proteins may lead to pathologies that affect significant numbers of patients. Our objectives are to directly perform structure/function studies on several of the more likely candidate gene products and to make reagents such as antisera, cDNA probes and purified proteins available to colleagues around the world.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of Dental & Craniofacial Research (NIDCR)
Type
Intramural Research (Z01)
Project #
1Z01DE000074-24
Application #
2572229
Study Section
Special Emphasis Panel (BRB)
Project Start
Project End
Budget Start
Budget End
Support Year
24
Fiscal Year
1996
Total Cost
Indirect Cost

  Institution

Name
National Institute of Dental & Craniofacial Research
Department
Type
DUNS #
City
State
Country
United States
Zip Code

  Publications

von Marschall, Zofia; Fisher, Larry W (2010) Dentin sialophosphoprotein (DSPP) is cleaved into its two natural dentin matrix products by three isoforms of bone morphogenetic protein-1 (BMP1). Matrix Biol 29:295-303
Jain, Alka; Fisher, Larry W; Fedarko, Neal S (2008) Bone sialoprotein binding to matrix metalloproteinase-2 alters enzyme inhibition kinetics. Biochemistry 47:5986-95
Inkson, Colette A; Ono, Mitsuaki; Kuznetsov, Sergei A et al. (2008) TGF-beta1 and WISP-1/CCN-4 can regulate each other's activity to cooperatively control osteoblast function. J Cell Biochem 104:1865-78
Adams, J; Fantner, G E; Fisher, L W et al. (2008) Molecular energy dissipation in nanoscale networks of Dentin Matrix Protein 1 is strongly dependent on ion valence. Nanotechnology 19:384008
Bellahcene, Akeila; Castronovo, Vincent; Ogbureke, Kalu U E et al. (2008) Small integrin-binding ligand N-linked glycoproteins (SIBLINGs): multifunctional proteins in cancer. Nat Rev Cancer 8:212-26
de Vega, Susana; Iwamoto, Tsutomu; Nakamura, Takashi et al. (2007) TM14 is a new member of the fibulin family (fibulin-7) that interacts with extracellular matrix molecules and is active for cell binding. J Biol Chem 282:30878-88
Ogbureke, Kalu U E; Nikitakis, Nikolaos G; Warburton, Gary et al. (2007) Up-regulation of SIBLING proteins and correlation with cognate MMP expression in oral cancer. Oral Oncol 43:920-32
Fantner, Georg E; Adams, Jonathan; Turner, Patricia et al. (2007) Nanoscale ion mediated networks in bone: osteopontin can repeatedly dissipate large amounts of energy. Nano Lett 7:2491-8
Ogbureke, Kalu U E; Fisher, Larry W (2007) SIBLING expression patterns in duct epithelia reflect the degree of metabolic activity. J Histochem Cytochem 55:403-9
Nam, Jeong-Seok; Suchar, Adam M; Kang, Mi-Jin et al. (2006) Bone sialoprotein mediates the tumor cell-targeted prometastatic activity of transforming growth factor beta in a mouse model of breast cancer. Cancer Res 66:6327-35

Showing the most recent 10 out of 38 publications