| dc.description.abstract |
The present study demonstrates that a unique isoform of matrix metalloproteinase (MMP)-2 present in human follicular fluid (FF) can be processed selectively by human oviducal fluid (OF). A gelatin zymogram of untreated FF showed distinct 88-, 84- and 62-kDa gelatinases. Treatment of FF with EDTA resulted in the appearance of 110-kDa gelatinase (GA110). Most gelatinases, except for the 88- and 84-kDa gelatinases, were abolished by pretreatment with EDTA or phenanthroline, but not by pretreatment with a serine/threonine protease inhibitor. When EDTA-pretreated FF was mixed with OF, the GA110 of the FF was specifically reduced. The reduction in GA110 was dependent upon the amount of OF protein and the incubation period after mixing. Treatment of FF with aminophenylmercuric acetate reduced GA110 activity, but this reduction was accompanied by a concomitant increase of 62-kDa gelatinase activity. Anti-human MMP-2 antibody strongly reacted with both GA110 and 62-kDa gelatinases of FF, but only GA110 immunoreactivity was abolished when FF was mixed with OF. The results suggest that the GA110 of FF is an MMP-2 isoform that can be processed selectively by OF. |
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