Effect of metallothioneins on transformation of gelatinase A from human fibroblast WI-38 cells.
The effect of metallothioneins (MTs) on gelatinase A activity was investigated. The collagenolytic activity of gelatinase A from human fibroblast WI-38 cells was enhanced by the addition of MTs. This enhancement may be caused by the transformation of the inactive 62 kDa intermediate species of gelatinase A to the 59 kDa active enzyme. This enhancement was also observed in the conditioned medium of WI-38 cells exposed to heavy metals, but intracellular 72 kDa pro-gelatinase A did not change. Furthermore, degradation of gelatinase A occurred in the reaction between gelatinase A with substrate and MTs. Our results suggest that MTs may be an endogenous activator of gelatinase A, and may provide a host factor in cancer metastasis.
Haga
A
A
Department of Public Health, Gifu Pharmaceutical University, Gifu, Japan.
Nagase
H
H
Kito
H
H
Sato
T
T
D000818:Animals; D002460:Cell Line; D017077:Culture Media, Conditioned; D004789:Enzyme Activation / Q000187:drug effects; D005347:Fibroblasts / Q000187:drug effects* / Q000201:enzymology; D005780:Gelatin / Q000378:metabolism; D018093:Gelatinases / Q000187:drug effects* / Q000378:metabolism; D006801:Humans; D008297:Male; D020778:Matrix Metalloproteinase 2; D008666:Metalloendopeptidases / Q000187:drug effects* / Q000378:metabolism; D008668:Metallothionein / Q000302:isolation & purification / Q000494:pharmacology*; D051381:Rats; D017208:Rats, Wistar
D017077:Culture Media, Conditioned; D005780:Gelatin; D008668:Metallothionein; D018093:Gelatinases; D008666:Metalloendopeptidases; D020778:Matrix Metalloproteinase 2