Deperthes D, Marceau F, Frenette G, Lazure C, Tremblay R R, Dubé J Y
Laboratory of Hormonal Bioregulation, CHUL Research Center and Laval University, Sainte-Foy, Quebec, Canada.
Biochim Biophys Acta. 1997 Nov 14;1343(1):102-6. doi: 10.1016/s0167-4838(97)00135-0.
In the present paper, we determined the kinin-releasing activity of human prostatic kallikrein hK2 and compared it to one of the kallikreins hK1 and prostate specific antigen (hK3). Kinin-like substances active on the rabbit jugular vein were progressively produced when nanomolar concentrations of hK2 were incubated with heated plasma. However in these experiments, hK1 appeared much more potent than hK2 while hK3 was totally inactive. When hK2 was incubated with purified high molecular weight kininogen, several peptides were generated as shown by the analysis on C18 reverse-phase HPLC. Kinin activity was localized exclusively in a small peak having an elution time identical to that of bradykinin while the only important peak obtained with hK1 corresponded to Lys-bradykinin. Finally, the rate of kinin production of hK2 was found to be more than a thousandfold lower than that of hK1. These experiments show that kallikreins hK2 has only a low kininogenase activity. However, it is not excluded that some of the peptides produced by hK2 action could have other types of biological activity.
在本论文中，我们测定了人前列腺激肽释放酶hK2的激肽释放活性，并将其与激肽释放酶之一hK1以及前列腺特异性抗原（hK3）进行比较。当纳摩尔浓度的hK2与加热的血浆一起孵育时，对兔颈静脉有活性的类激肽物质会逐渐产生。然而，在这些实验中，hK1似乎比hK2更具活性，而hK3则完全无活性。当hK2与纯化的高分子量激肽原一起孵育时，通过C18反相高效液相色谱分析表明产生了几种肽。激肽活性仅定位在一个洗脱时间与缓激肽相同的小峰中，而用hK1得到的唯一重要峰对应于赖氨酰缓激肽。最后，发现hK2的激肽产生速率比hK1低一千多倍。这些实验表明，激肽释放酶hK2仅具有低激肽原酶活性。然而，不排除hK2作用产生的一些肽可能具有其他类型的生物活性。
