Considering the critical interface between tumor cells and stromal cells in the search for targets for anticancer therapy.
In this issue of Cancer Cell, a paper by Lynch et al. demonstrates how the careful study of changes that occur at the interface between tumor cells and stromal cells led to the discovery of a new function for matrix metalloproteinase-7 (MMP-7) in the formation of osteolytic lesions in prostate cancer. The data suggest that MMP-7 inhibition could be a therapeutic target in prostate cancer.
Blavier
Laurence
L
Division of Hematology-Oncology, Department of Pediatrics, Keck School of Medicine, University of Southern California, Los Angeles, California 90027, USA.
Declerck
Yves A
YA
D000818:Animals; D002352:Carrier Proteins / Q000378:metabolism; D015870:Gene Expression; D008297:Male; D020783:Matrix Metalloproteinase 7 / Q000235:genetics / Q000378:metabolism*; D008562:Membrane Glycoproteins / Q000378:metabolism; D051379:Mice; D008954:Models, Biological; D010010:Osteoclasts / Q000378:metabolism / Q000473:pathology; D010014:Osteolysis / Q000209:etiology / Q000378:metabolism / Q000473:pathology; D011471:Prostatic Neoplasms / Q000150:complications / Q000378:metabolism / Q000628:therapy*; D053245:RANK Ligand; D051381:Rats; D053246:Receptor Activator of Nuclear Factor-kappa B; D017154:Stromal Cells / Q000378:metabolism*
D002352:Carrier Proteins; D008562:Membrane Glycoproteins; D053245:RANK Ligand; D053246:Receptor Activator of Nuclear Factor-kappa B; C505687:Tnfrsf11a protein, mouse; C505689:Tnfsf11 protein, mouse; D020783:Matrix Metalloproteinase 7