Identification and Characterization of Human and Mouse Ovastacin A NOVEL METALLOPROTEINASE SIMILAR TO HATCHING ENZYMES FROM ARTHROPODS, BIRDS, AMPHIBIANS, AND FISH

摘要: We have cloned and characterized human mouse ovary cDNAs encoding a new protein of the astacin family metalloproteinases, called ovastacin because its predominant expression in ovarian tissues. Human ovastacins exhibit same domain organization as other astacins, including signal sequence, propeptide, metalloproteinase domain. However, show an additional C-terminal about 150 amino acids with no similarity to ancillary domains present equivalent region most astacins. Northern blot analysis tissues cell lines revealed that is only detected at significant levels leukemia lymphoma cells different origin. In addition, RT-PCR demonstrated expressed ovary, unfertilized oocytes, 1.5-day-postcoitum preimplantation embryos. Further studies showed superovulation caused dramatic increase ovastacin, indicating production this enzyme under hormonal regulation. was Escherichia coli purified recombinant hydrolyzed synthetic substrates used for assaying metalloproteinases. These activities were abolished by inhibitors but not classes proteases. On basis these results, we suggest could play mammals physiological function similar performed hatching proteases evolutionary distant species from arthropods fish.