This program combines the technologies of protein structural and physical chemistry, cell biology, molecular biology and genetics, and clinical investigation to elucidate the contributions of bone proteins to bone structure/function. The integrated program aims at identifying and characterizing bone proteins. This knowledge will be utilized in three fashions: 1) to provide tools to identify cells involved in bone synthesis and to prove their regulation at both the protein and nucleic acid level. 2) to develop an appreciation of the contribution of collagenous and noncollagenous proteins in providing the structural/functional qualities of bone. 3) to evaluate the utility of knowledge of the blood and urine levels of bone proteins and their fragments in the evaluation of normal and abnormal skeletal function. The research program proposed brings together experienced laboratories directed by seasoned investigators who have demonstrated ability to work together. It is hoped the concerted research effort will provide fundamental insights into bone biology and also the technology to combat osteoporosis and other major diseases of bone formation.

Agency
National Institute of Health (NIH)
Institute
National Institute on Aging (NIA)
Type
Research Program Projects (P01)
Project #
5P01AG008777-04
Application #
2050392
Study Section
Aging Review Committee (AGE)
Project Start
1991-06-01
Project End
1996-05-31
Budget Start
1994-06-01
Budget End
1995-05-31
Support Year
4
Fiscal Year
1994
Total Cost
Indirect Cost
Name
University of Vermont & St Agric College
Department
Biochemistry
Type
Schools of Medicine
DUNS #
066811191
City
Burlington
State
VT
Country
United States
Zip Code
05405
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Bini, A; Mann, K G; Kudryk, B J et al. (1999) Noncollagenous bone matrix proteins, calcification, and thrombosis in carotid artery atherosclerosis. Arterioscler Thromb Vasc Biol 19:1852-61
Fanburg, J C; Rosenberg, A E; Weaver, D L et al. (1997) Osteocalcin and osteonectin immunoreactivity in the diagnosis of osteosarcoma. Am J Clin Pathol 108:464-73
Xie, R L; Long, G L (1996) Elements within the first 17 amino acids of human osteonectin are responsible for binding to type V collagen. J Biol Chem 271:8121-5
Xie, R L; Long, G L (1995) Role of N-linked glycosylation in human osteonectin. Effect of carbohydrate removal by N-glycanase and site-directed mutagenesis on structure and binding of type V collagen. J Biol Chem 270:23212-7
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Carlson, C S; Tulli, H M; Jayo, M J et al. (1993) Immunolocalization of noncollagenous bone matrix proteins in lumbar vertebrae from intact and surgically menopausal cynomolgus monkeys. J Bone Miner Res 8:71-81