Tanaka H, Hojo K, Yoshida H, Yoshioka T, Sugita K
Department of Microbiology, Shionogi Research Laboratories, Shionogi & Co., Ltd., Osaka, Japan.
Biochem Biophys Res Commun. 1993 Feb 15;190(3):732-40. doi: 10.1006/bbrc.1993.1110.
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.
我们在源自小鼠鳞状细胞癌的转移性肿瘤细胞系SN-H的培养上清液中检测到一种强大的明胶酶活性。通过明胶酶谱法估计该明胶酶的相对分子量为105 kDa。我们已克隆了这种明胶酶的cDNA，并确定了3160 bp的序列。从翻译后的氨基酸序列来看，半胱氨酸残基的位置和功能域结构与人类92 kDa明胶酶高度同源。这两个cDNA之间的核苷酸和氨基酸序列同源性分别为75%和72%。将该cDNA转染到表达载体中导致产生了105 kDa的明胶酶，从而证实该cDNA具有功能。
