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.
Keywords
Matrix metalloproteinases - angiogenesis - invasiveness - chemoresistance - tumour-stroma
interaction