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- W2034124119 abstract "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." @default.
- W2034124119 created "2016-06-24" @default.
- W2034124119 creator A5043717687 @default.
- W2034124119 creator A5064660101 @default.
- W2034124119 creator A5085036412 @default.
- W2034124119 date "2005-01-01" @default.
- W2034124119 modified "2023-10-15" @default.
- W2034124119 title "Roles of the multifunctional glycoprotein, emmprin (basigin; CD147), in tumour progression" @default.
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- W2034124119 doi "https://doi.org/10.1160/th04-08-0536" @default.
- W2034124119 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/15711733" @default.
- W2034124119 hasPublicationYear "2005" @default.
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