The broad objectives of this research are to characterize rat bone non- collagenous proteins that are made and secreted by osteoblasts and are found in the calcified matrix of bone and to determine their functions. The fundamental hypothesis on which these studies is based is that these NCPs are involved in the formation of bone. The recent demonstration that two of the bone matrix proteins are cell attachment proteins while others are growth factors indicate that some of the bone NPCs have activities relating to cells. The specific objectives of this research are: 1) to use antibodies against bone matrix proteins as markers to study osteoblast differentiation, 2) to determine the nature, location and biosynthesis of the post-translational modifications of osteopontin, a phosphorylated cell attachment protein, 3) to identify and characterize putative proteins linking osteopontin to the organic matrix of bone (type I collagen) 4) to continue studies on the characterization, biosynthesis and immunolocalization of newly discovered bone matrix NCPs. These studies will advance our knowledge of the fundamental biochemical mechanisms involved in osteogenesis. This fundamental knowledge will be useful in understanding the basic causes of certain genetic and systemic diseases that affect bone.

Agency
National Institute of Health (NIH)
Institute
National Institute of Arthritis and Musculoskeletal and Skin Diseases (NIAMS)
Type
Research Project (R01)
Project #
5R01AR039273-06
Application #
3159271
Study Section
General Medicine B Study Section (GMB)
Project Start
1987-06-01
Project End
1995-05-31
Budget Start
1992-06-01
Budget End
1993-05-31
Support Year
6
Fiscal Year
1992
Total Cost
Indirect Cost
Name
University of Texas Health Science Center Houston
Department
Type
Schools of Dentistry
DUNS #
City
Houston
State
TX
Country
United States
Zip Code
77225
Razzouk, S; Brunn, J C; Qin, C et al. (2002) Osteopontin posttranslational modifications, possibly phosphorylation, are required for in vitro bone resorption but not osteoclast adhesion. Bone 30:40-7
Liu, R; Li, W; Karin, N J et al. (2000) Ribozyme ablation demonstrates that the cardiac subtype of the voltage-sensitive calcium channel is the molecular transducer of 1, 25-dihydroxyvitamin D(3)-stimulated calcium influx in osteoblastic cells. J Biol Chem 275:8711-8
French, M M; Smith, S E; Akanbi, K et al. (1999) Expression of the heparan sulfate proteoglycan, perlecan, during mouse embryogenesis and perlecan chondrogenic activity in vitro. J Cell Biol 145:1103-15
Devoll, R E; Li, W; Woods, K V et al. (1999) Osteopontin (OPN) distribution in premalignant and malignant lesions of oral epithelium and expression in cell lines derived from squamous cell carcinoma of the oral cavity. J Oral Pathol Med 28:97-101
Thalmann, G N; Sikes, R A; Devoll, R E et al. (1999) Osteopontin: possible role in prostate cancer progression. Clin Cancer Res 5:2271-7
Farach-Carson, M C; Ridall, A L (1998) Dual 1,25-dihydroxyvitamin D3 signal response pathways in osteoblasts: cross-talk between genomic and membrane-initiated pathways. Am J Kidney Dis 31:729-42
Safran, J B; Butler, W T; Farach-Carson, M C (1998) Modulation of osteopontin post-translational state by 1, 25-(OH)2-vitamin D3. Dependence on Ca2+ influx. J Biol Chem 273:29935-41
Snyder, W R; Hoover, J; Khoury, R et al. (1997) Effect of agents used in perforation repair on osteoblastic cells. J Endod 23:158-61
Devoll, R E; Pinero, G J; Appelbaum, E R et al. (1997) Improved immunohistochemical staining of osteopontin (OPN) in paraffin-embedded archival bone specimens following antigen retrieval: anti-human OPN antibody recognizes multiple molecular forms. Calcif Tissue Int 60:380-6
Neame, P J; Butler, W T (1996) Posttranslational modification in rat bone osteopontin. Connect Tissue Res 35:145-50

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