The fundamental question of how cells of bones and teeth assemble and mineralize their respective matrices in such a coordinated and superbly biofunctional way is still largely unanswered. The Protein Chemistry Unit has been performing a variety of experiments and collaborations to help determine the structure-function relationship of several of the more interesting noncollagenous proteins. Publications fall into four general categories. 1) Two closely related proteoglycans, decorin and biglycan, continued to be central to our interests. Advances have included work on the biglycan knock-out mouse, partial characterization of the human biglycan promoter as well as localization of the endocytosis domain of human decorin to Leu125-Val230. 2) Continued work on the gene structure of the enamel protein, tuftelin. 3) Advances in the understanding of McCune-Albright syndrome including data indicating that the disease directly affects the osteogenic lineage. Furthermore we have aided in the development of an implantation model of the disease. 4) Finally we have continued our exploration of the possible role of bone sialoprotein in osteotropic cancers. With our colleagues, we have shown that BSP is an interesting marker for breast, lung, thyroid and prostate cancers.

Agency
National Institute of Health (NIH)
Institute
National Institute of Dental & Craniofacial Research (NIDCR)
Type
Intramural Research (Z01)
Project #
1Z01DE000074-26
Application #
6104528
Study Section
Special Emphasis Panel (CSDB)
Project Start
Project End
Budget Start
Budget End
Support Year
26
Fiscal Year
1998
Total Cost
Indirect Cost
Name
National Institute of Dental & Craniofacial Research
Department
Type
DUNS #
City
State
Country
United States
Zip Code
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
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
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
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

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