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Literature summary for 3.4.24.7 extracted from

  • Packard, B.Z.; Artym, V.V.; Komoriya, A.; Yamada, K.M.
    Direct visualization of protease activity on cells migrating in three-dimensions (2009), Matrix Biol., 28, 3-10.
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
analysis detection of localized extracellular sites of protease activity by use of fluorescent biosensor rhodamine 6G-labeled KDP-6-aminohexanoic acid-GPLGIAGIG-6-aminohexanoic acid-PKGY. Protease activity is localized at the polarized leading edge of migrating tumor cells rather than further back on the cell body. The path of proteolytic cleavage by a migrating cell can be visualized in 2- and 3-dimensional matrices. Probe can be used to determine inhibitor concentrations needed to suppress cell-surface protease activity Homo sapiens
medicine protease activity is localized at the polarized leading edge of migrating tumor cells rather than further back on the cell body. Activity is essential for cell migration in native cross-linked but not pepsin-treated collagen matrices Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
additional information not inhibitory: tissue inhibitor of matrix metalloproteinase-1 Homo sapiens
tissue inhibitor of matrix metalloproteinase-2 0.1 microM, inhibits both protease activity and migration in a 3-dimensional cross-linked collagen matrix Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
HT-1080 cell
-
Homo sapiens
-
PC-3 cell
-
Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
rhodamine 6G-labeled KDP-6-aminohexanoic acid-GPLGIAGIG-6-aminohexanoic acid-PKGY + H2O fluorescent biosensor, substrate for matrix metalloproteinases MMP-2, MMP-9, MMP-14 Homo sapiens rhodamine 6G-labeled KDP-6-aminohexanoic acid-GPLG + IAGIG-6-aminohexanoic acid-PKGY
-
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