Encyclopedia of Cancer

Living Edition
| Editors: Manfred Schwab

Secreted Protein Acidic and Rich in Cysteine

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DOI: https://doi.org/10.1007/978-3-642-27841-9_5212-2
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Synonyms

BM-40; Osteonectin; SPARC

Definition

Secreted protein acidic and rich in cysteine (SPARC) belongs to a group of nonstructural proteins of the extracellular matrix (ECM), termed matricellular proteins, which modulate interactions between cells and their environment. It is expressed in developing and remodeling tissues and regulates cell attachment, deposition of ECM, matrix mineralization, and angiogenesis.

Characteristics

SPARC is a counter-adhesive protein that induces cell rounding, inhibits cell spreading, and mediates focal adhesion disassembly and the reorganization of actin stress fibers. In several cell types, it delays cell cycle in G1phase. It is the main noncollagenous component of the bone, where binding of SPARC to collagen can induce deposition of calcium. However, inhibition of hydroxylapatite crystallization suggests that SPARC prevents matrix mineralization rather than inducing it. SPARC also regulates the production, assembly, and organization of ECM, and...

Keywords

Focal Adhesion Kinase Endothelial Cell Spreading Tumor Suppressor Gene RASSF1A Identify Tumor Suppressor Gene Induce Cell Rounding 
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

  1. Chlenski A, Cohn SL (2010) Modulation of matrix remodeling by SPARC in neoplastic progression. Semin Cell Dev Biol 21(1):55-65Google Scholar
  2. Framson PE, Sage EH (2004) SPARC and tumor growth: where the seed meets the soil? J Cell Biochem 92:679–690CrossRefPubMedGoogle Scholar
  3. Lane TF, Sage EH (1994) The biology of SPARC, a protein that modulates cell-matrix interactions. FASEB J 8:163–173PubMedGoogle Scholar

See Also

  1. (2012) AKT. In: Schwab M (ed) Encyclopedia of Cancer, 3rd edn. Springer Berlin Heidelberg, p 115. doi: 10.1007/978-3-642-16483-5_163Google Scholar
  2. (2012) Basic Fibroblast Growth Factor. In: Schwab M (ed) Encyclopedia of Cancer, 3rd edn. Springer Berlin Heidelberg, p 349. doi: 10.1007/978-3-642-16483-5_539Google Scholar
  3. (2012) EF-Hand. In: Schwab M (ed) Encyclopedia of Cancer, 3rd edn. Springer Berlin Heidelberg, pp 1210-1211. doi: 10.1007/978-3-642-16483-5_1818Google Scholar
  4. (2012) Matricellular Proteins. In: Schwab M (ed) Encyclopedia of Cancer, 3rd edn. Springer Berlin Heidelberg, p 2182. doi: 10.1007/978-3-642-16483-5_3550Google Scholar
  5. (2012) Microenvironment. In: Schwab M (ed) Encyclopedia of Cancer, 3rd edn. Springer Berlin Heidelberg, p 2296. doi: 10.1007/978-3-642-16483-5_3720Google Scholar
  6. (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
  7. (2012) TGF-β. In: Schwab M (ed) Encyclopedia of Cancer, 3rd edn. Springer Berlin Heidelberg, p 3661. doi: 10.1007/978-3-642-16483-5_5753Google Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 2014

Authors and Affiliations

  1. 1.Department of Pediatrics, Section of Hematology/OncologyUniversity of ChicagoChicagoUSA