Encyclopedia of Cancer

Living Edition
| Editors: Manfred Schwab

Thrombospondin

Living reference work entry
DOI: https://doi.org/10.1007/978-3-642-27841-9_5796-2

Definition

Thrombospondins (TSPs, THBSs) are a family of multidomain, calcium-binding, extracellular glycoproteins which are synthesized, secreted, and incorporated into the extracellular matrix of a variety of normal and transformed cells of both mesenchymal and epithelial origins.

Characteristics

Classification

Five distinct forms of thrombospondin have been identified, TSP-1, -2, -3, -4, and -5 (cartilage oligomeric matrix protein, COMP). The TSPs fall into two subgroups, termed A and B, according to their oligomerization status and molecular architecture. Subgroup A includes TSP-1 and TSP-2, which form homotrimers. Subgroup B includes TSP-3, TSP-4, and TSP-5/COMP, which form homopentamers. All five members contain the type 2 repeats, the type 3 repeats, and a highly conserved C-terminal domain. The type 2 repeats are similar to the epidermal growth factor repeats, the type 3 repeats comprise a contiguous set of calcium-binding sites, and the C-terminal domain is involved in cell...

Keywords

Endothelial Cell Migration Vascular Endothelial Growth Factor Endothelial Cell Apoptosis Metronomic Chemotherapy Cartilage Oligomeric Matrix Protein 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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References

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  3. Lawler J, Detmar M (2004) Tumor progression: the effects of thrombospondin-1 and -2. Int J Biochem Cell Biol 36:1038–1045CrossRefPubMedGoogle Scholar
  4. Ren B, Yee KO, Lawler J et al (2006) Regulation of tumor angiogenesis by thrombospondin-1. Biochim Biophys Acta 1765:178–188PubMedGoogle Scholar

See Also

  1. (2012) Extracellular Matrix. In: Schwab M (ed) Encyclopedia of Cancer, 3rd edn. Springer Berlin Heidelberg, p 1362. doi:10.1007/978-3-642-16483-5_2067Google Scholar
  2. (2012) FAS. In: Schwab M (ed) Encyclopedia of Cancer, 3rd edn. Springer Berlin Heidelberg, p 1379. doi:10.1007/978-3-642-16483-5_2121Google Scholar
  3. (2012) Integrin. In: Schwab M (ed) Encyclopedia of Cancer, 3rd edn. Springer Berlin Heidelberg, p 1884. doi:10.1007/978-3-642-16483-5_3084Google Scholar
  4. (2012) JUN. In: Schwab M (ed) Encyclopedia of Cancer, 3rd edn. Springer Berlin Heidelberg, p 1929. doi:10.1007/978-3-642-16483-5_3186Google Scholar
  5. (2012) Knock-Out Mouse. In: Schwab M (ed) Encyclopedia of Cancer, 3rd edn. Springer Berlin Heidelberg, p 1957. doi:10.1007/978-3-642-16483-5_3239Google Scholar
  6. (2012) Mimetic Peptide. In: Schwab M (ed) Encyclopedia of Cancer, 3rd edn. Springer Berlin Heidelberg, p 2318. doi:10.1007/978-3-642-16483-5_3749Google Scholar
  7. (2012) P53. In: Schwab M (ed) Encyclopedia of Cancer, 3rd edn. Springer Berlin Heidelberg, p 2747. doi:10.1007/978-3-642-16483-5_4331Google Scholar
  8. (2012) SMAD. In: Schwab M (ed) Encyclopedia of Cancer, 3rd edn. Springer Berlin Heidelberg, p 3440. doi:10.1007/978-3-642-16483-5_5360Google Scholar
  9. (2012) Tumor Vessel Density. In: Schwab M (ed) Encyclopedia of Cancer, 3rd edn. Springer Berlin Heidelberg, p 3807. doi:10.1007/978-3-642-16483-5_6060Google Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 2015

Authors and Affiliations

  1. 1.Duke PathologyDuke University School of MedicineDurhamUSA