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Biochem Biophys Res Commun. 1993 Feb 15;190(3):732-40.

Molecular cloning and expression of the mouse 105-kDa gelatinase cDNA.

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Department of Microbiology, Shionogi Research Laboratories, Shionogi & Co., Ltd., Osaka, Japan.


We have detected a potent gelatinolytic activity in the culture supernatant of a metastatic tumor line, SN-H, derived from a murine squamous cell carcinoma. The relative molecular weight of the gelatinase was estimated as 105-kDa by gelatin zymography. We have cloned the cDNA of this gelatinase and the 3160-bp sequence has been determined. From the translated amino acid sequence, the positions of the cysteine residues and the functional domain structure are highly homologous to the human 92-kDa gelatinase. The nucleotide and amino acid sequence homology between these two cDNAs are 75% and 72%, respectively. Transfection of the cDNA in an expression vector resulted in production of the 105-kDa gelatinase, thus confirming that this cDNA is functional.

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