Urokinase plasminogen activator is necessary but not sufficient for prostate cancer cell invasion.

Invasion & metastasis Pub Date : 1995-01-01
D F Jarrard, N M Hansen, B Patai, D B Rukstalis
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Abstract

The expression and function of urokinase plasminogen activator (uPA), an extracellular protease, were examined in four established prostate cancer lines, and one uPA-transfected cell line. The cell lines exhibited variable efficiency in uPA transcription, translation and specific proteolytic activity. A statistically significant inhibition of Boyden chamber invasion by anti-uPA monoclonal antibodies was demonstrated in cell lines TSU-PR1 and PC3. This inhibition suggests a direct role for uPA in the invasion of prostate cancer. However, variable processing of uPA mRNA, protein and proteolytic activity make prediction of in vitro invasion of prostate cancer difficult. Stable transfection experiments suggest that the proteolytic cascade generated by a cell is multiform and solitary alterations in uPA may not modify the proteolytic capability for invasion.

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尿激酶纤溶酶原激活剂对前列腺癌细胞的侵袭是必要的,但不是充分的。
尿激酶纤溶酶原激活剂(uPA)是一种细胞外蛋白酶,我们检测了4株前列腺癌细胞系和1株uPA转染细胞系的表达和功能。这些细胞系在uPA转录、翻译和特异性蛋白水解活性方面表现出不同的效率。在细胞系TSU-PR1和PC3中,抗upa单克隆抗体对Boyden室侵袭有显著的抑制作用。这种抑制表明uPA在前列腺癌的侵袭中起直接作用。然而,uPA mRNA、蛋白和蛋白水解活性的变化使得预测前列腺癌的体外侵袭变得困难。稳定转染实验表明,细胞产生的蛋白水解级联是多种形式的,uPA的单独改变可能不会改变入侵的蛋白水解能力。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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