NOVEL METALLOPROTEINASE INHIBITORS--ROLE IN TUMOR INVASION AND METASTASIS

我们已经分离并表征了一种新的 金属蛋白酶组织抑制因子家族(TIMP家族)成员 我们称之为TIMP-2。TIMP-2与潜伏形式的特异性结合 72 kDa的IV型胶原酶。活化酶的抑制 以1：1摩尔化学计量比发生。TIMP-2含有12个半胱氨酸残基， 其位置与初级的相比是高度保守的 TIMP-1的结构。我们已经获得了一个1.0kB的cDNA克隆，该克隆编码 支持TIMP-2的。该克隆编码194个氨基酸的成熟TIMP-2 分子和一个由26个氨基酸组成的信号肽。最近的研究集中在 重组TIMP-2的生产及其转录调控 TIMP-2转录水平。

We have isolated and characterized the complete primary structure of a new member of the tissue inhibitor of metalloproteinase family (TIMP family) which we refer to as TIMP-2. TIMP-2 binds specifically to the latent form of the 72 kDa type IV collagenase. Inhibition of the activated enzyme occurs with 1:1 molar stoichiometry. TIMP-2 contains 12 cysteine residues, the positions of which are highly conserved when compared with the primary structure of TIMP-1. We have obtained a 1.0 kB cDNA clone which encodes for the pro-TIMP-2. This clone encodes for a 194 amino acid mature TIMP-2 molecule and a 26 amino acid signal peptide. Recent studies have focused on the production of recombinant TIMP-2 and transcriptional regulation of the TIMP-2 transcript levels.