Proteases associated with invadopodia, and their role in degradation of extracellular matrix.
Metastasizing cancer cells invade the extracellular matrix using plasma membrane protrusions (invadopodia) that contact and dissolve the matrix. Evidence suggests that membrane-associated proteases, 170-kD gelatinase (seprase) and Gelatinase A, exert their mechanisms of action on invadopodia. Potential roles that other metallo- and serine-types of membrane proteases, including membrane-type matrix metalloprotease, meprin, dipeptidyl peptidase IV, fibroblast activation protein alpha and guanidinobenzoatase, play in the cell surface proteolysis are also discussed. It is proposed that formation of a structurally and functionally linked protease complex on invadopodia allows the invasion of cancer cells into the extracellular matrix.
Chen
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Department of Cell Biology, Georgetown University School of Medicine, Washington, D.C. 20007, USA.
D000818:Animals; D018819:Dipeptidyl Peptidase 4 / Q000378:metabolism; D010450:Endopeptidases / Q000378:metabolism*; D004789:Enzyme Activation; D005109:Extracellular Matrix / Q000201:enzymology*; D018093:Gelatinases / Q000378:metabolism; D006801:Humans; D020778:Matrix Metalloproteinase 2; D053504:Matrix Metalloproteinases, Membrane-Associated; D008565:Membrane Proteins / Q000378:metabolism; D008666:Metalloendopeptidases / Q000378:metabolism; D008970:Molecular Weight; D009361:Neoplasm Invasiveness; D009362:Neoplasm Metastasis / Q000473:pathology*; D012697:Serine Endopeptidases / Q000378:metabolism; D008625:Tiopronin / Q000378:metabolism; D000099167:Fibroblast Activation Protein Alpha
D018819:Dipeptidyl Peptidase 4; D010450:Endopeptidases; D018093:Gelatinases; D020778:Matrix Metalloproteinase 2; D053504:Matrix Metalloproteinases, Membrane-Associated; D008565:Membrane Proteins; D008666:Metalloendopeptidases; D012697:Serine Endopeptidases; D008625:Tiopronin; D000099167:Fibroblast Activation Protein Alpha