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The primary structure of a cell-binding bone sialoprotein.
Open accessAbstract
We have determined the amino acid sequence of rat bone sialoprotein (BSP). The sequence deduced from a 1974-base pair cDNA encodes a protein of 320 residues, including a 16-residues long signal peptide. The mature BSP has a molecular mass of 33,600 and contains predominantly glutamic acid and glycine residues, which constitute 32% of all residues. The glutamic acid residues are typically distributed in clusters of up to 10 consecutive residues. The tissue distribution of BSP mRNA suggests that the protein may be a unique product of cells in bone tissue. BSP contains an Arg-Gly-Asp sequence, which presumably is responsible for its cell binding properties (Oldberg, A., Franzén, A., Heinegård, D., Pierschbacher, M., and Ruoslahti, E. (1988) J. Biol. Chem. 263, 19433-19436).
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Cited by
Beresford, J. N., Bennett, J. H., Devlin, C., Leboy, P. S., & Owen, M. E. (1992) · Journal of Cell Science · doi:10.1242/jcs.102.2.341 · Cited by 836
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George, A., & Veis, A. (2008) · Chemical Reviews · doi:10.1021/cr0782729 · Cited by 745
Structure and Biological Role of Vitronectin
Preissner, K. T. (1991) · Annual Review of Cell Biology · doi:10.1146/annurev.cb.07.110191.001423 · Cited by 486
Qin, C., Baba, O., & Butler, W. T. (2004) · Critical Reviews in Oral Biology & Medicine · doi:10.1177/154411130401500302 · Cited by 439
Mizuno, M., Fujisawa, R., & Kuboki, Y. (2000) · Journal of Cellular Physiology · doi:10.1002/1097-4652(200008)184:2<207::aid-jcp8>3.0.co;2-u · Cited by 384
Metadata
- Authors
- Oldberg, A., Franzén, A., & Heinegård, D.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1988-12
- Volume
- 263
- Issue
- 36
- Pages
- 19430-19432
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1493047535
- Cited by
- 383
- References
- 0
- FWCI
- 15.80
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Oldberg, A., Franzén, A., & Heinegård, D. (1988). The primary structure of a cell-binding bone sialoprotein. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(19)77651-0
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