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The Thrombospondins
Open accessAbstract
Thrombospondins are evolutionarily conserved, calcium-binding glycoproteins that undergo transient or longer-term interactions with other extracellular matrix components. They share properties with other matrix molecules, cytokines, adaptor proteins, and chaperones, modulate the organization of collagen fibrils, and bind and localize an array of growth factors or proteases. At cell surfaces, interactions with an array of receptors activate cell-dependent signaling and phenotypic outcomes. Through these dynamic, pleiotropic, and context-dependent pathways, mammalian thrombospondins contribute to wound healing and angiogenesis, vessel wall biology, connective tissue organization, and synaptogenesis. We overview the domain organization and structure of thrombospondins, key features of their evolution, and their cell biology. We discuss their roles in vivo, associations with human disease, and ongoing translational applications. In many respects, we are only beginning to appreciate the important roles of these proteins in physiology and pathology.
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Cites
Platelet α-granules: Basic biology and clinical correlates
Blair, P., & Flaumenhaft, R. (2009) · Blood Reviews · doi:10.1016/j.blre.2009.04.001 · Cited by 1,157
Eroglu, Ç., Allen, N. J., Susman, M. W., O'Rourke, N. A., Park, C. Y., Özkan, E., Chakraborty, C., Mulinyawe, S. B., Annis, D. S., Huberman, A. D., et al. (2009) · Cell · doi:10.1016/j.cell.2009.09.025 · Cited by 893
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Barros, C. S., Franco, S. J., & Muller, U. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a005108 · Cited by 506
Isenberg, J. S., Romeo, M. J., Yu, C., Yu, C. K., Nghiem, K., Monsale, J., Rick, M. E., Wink, D. A., Frazier, W. A., & Roberts, D. D. (2008) · Blood · doi:10.1182/blood-2007-06-098392 · Cited by 205
Thrombospondin Plays a Vital Role in the Immune Privilege of the Eye
Zamiri, P., Masli, S., Kitaichi, N., Taylor, A. W., & Streilein, J. W. (2005) · Investigative Opthalmology & Visual Science · doi:10.1167/iovs.04-0362 · Cited by 143
Wang, S., Wu, Z., Sorenson, C. M., Lawler, J., & Sheibani, N. (2003) · Developmental Dynamics · doi:10.1002/dvdy.10412 · Cited by 133
Self-citationSun, J., Hopkins, B. D., Tsujikawa, K., Perruzzi, C., Adini, I., Swerlick, R., Bornstein, P., Lawler, J., & Benjamin, L. E. (2009) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.01246.2008 · Cited by 56
Self-citationNarizhneva, N. V., Byers-Ward, V. J., Quinn, M. J., Zidar, F. J., Plow, E. F., Topol, E. J., & Byzova, T. V. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m311090200 · Cited by 47 · cited 2×
“Nevertheless, biochemical and cellular analyses of the N700S and A387P SNPs of TSP-1 and TSP-4, respectively, have identified effects on calcium binding, protein conformation, and interactions with cells and ECM components of the vessel wall and platelet clot (Stenina et al. 2003, 2005; Narizhneva et al. 2004; Carlson…”
BackgroundEnhanced proangiogenic signaling in thrombospondin-1-deficient retinal endothelial cells
Wang, Y., Wang, S., & Sheibani, N. (2006) · Microvascular Research · doi:10.1016/j.mvr.2006.02.004 · Cited by 34
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Glover, J. D., Wells, K. L., Matthäus, F., Painter, K. J., Ho, W., Riddell, J., Johansson, J. A., Ford, M. J., Jahoda, C. A. B., Klika, V., et al. (2017) · PLOS Biology · doi:10.1371/journal.pbio.2002117 · Cited by 155
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Zhong, S., & Khalil, R. A. (2019) · Biochemical Pharmacology · doi:10.1016/j.bcp.2019.03.033 · Cited by 119
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Inoue, M., Jiang, Y., Barnes, R. H., Tokunaga, M., Martinez-Santibañez, G., Geletka, L., Lumeng, C. N., Buchner, D. A., & Chun, T.-H. (2013) · Endocrinology · doi:10.1210/en.2013-1587 · Cited by 85
Cheng, C., Lau, S. K. M., & Doering, L. C. (2016) · Molecular Brain · doi:10.1186/s13041-016-0256-9 · Cited by 84
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Cui, J., & Zhang, J. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23169253 · Cited by 77
Contreras-Ruiz, L., Ryan, D. S., Sia, R. K., Bower, K. S., Dartt, D. A., & Masli, S. (2014) · Ophthalmology · doi:10.1016/j.ophtha.2014.01.033 · Cited by 58
Masli, S., Sheibani, N., Cursiefen, C., & Zieske, J. (2014) · Current Eye Research · doi:10.3109/02713683.2013.877936 · Cited by 54
Rupareliya, V. P., Singh, A. A., Butt, A. M., A, H., & Kumar, H. (2023) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2023.176048 · Cited by 29
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Simon, L. S., Keshav, V., Baharozian, C., Masli, S., & Lee, H. J. (2021) · Graefe's Archive for Clinical and Experimental Ophthalmology · doi:10.1007/s00417-021-05121-3 · Cited by 5
Metadata
- Authors
- Adams, J. C., & Lawler, J.
- Venue
- Cold Spring Harbor Perspectives in Biology
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2011-08-29
- Volume
- 3
- Issue
- 10
- Pages
- a009712-a009712
- ISSN
- 1943-0264 (ISSN-L)
- OpenAlex
- W4211045489
- Cited by
- 457
- References
- 9
- Type
- posted content
- Language
- en
- Open access
- bronze
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