Thromb Haemost 2005; 93(02): 199-204
DOI: 10.1160/TH04-08-0536
Theme Issue Article
Schattauer GmbH

Roles of the multifunctional glycoprotein, emmprin (basigin; CD147), in tumour progression

Li Yan
1   Oncology, Centocor Inc, Radnor, Pennsylvania, USA
,
Stanley Zucker
2   Research and Medicine, Veterans Affairs Medical Center, Northport, New York, USA
,
Bryan P. Toole
3   Cell Biology and Anatomy, Medical University of South Carolina, Charleston, South Carolina, USA
› Author Affiliations
Financial support: Original work in this article was supported by NIH grant CA 79866 (BPT).
Further Information

Publication History

Received 23 August 2004

Accepted after revision 21 January 2004

Publication Date:
11 December 2017 (online)

Summary

Emmprin (basigin;CD147) is a widely distributed cell surface glycoprotein that belongs to the Ig superfamily and is highly enriched on the surface of malignant tumour cells. Emmprin is involved in numerous physiological and pathological systems and exhibits several molecular and cellular characteristics, but a major function of emmprin is stimulation of synthesis of several matrix metalloproteinases. In tumours, emmprin most likely stimulates matrix metalloproteinase production in stromal fibroblasts and endothelial cells as well as in tumour cells themselves by a mechanism involving homophilic interactions between emmprin molecules on apposing cells or on neighbouring cells after membrane vesicle shedding. Membrane-associated cofactors, including caveolin-1 and annexin II, regulate emmprin activity. Emmprin induces angiogenesis via stimulation of VEGF production, invasiveness via stimulation of matrix metalloproteinase production and multidrug resistance via hyaluronan-mediated up-regulation of ErbB2 signaling and cell survival pathway activities. Although the detailed mechanisms whereby it regulates these numerous phenomena are not yet known, it is clear that emmprin is a major mediator of malignant cell behavior.

 
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