Human kallikrein hK2 has low kininogenase activity while prostate-specific antigen (hK3) has none

被引:25
作者
Deperthes, D
Marceau, F
Frenette, G
Lazure, C
Tremblay, RR
Dubé, JY [1 ]
机构
[1] CHUL, Res Ctr, Hormonal Bioregulat Lab, St Foy, PQ G1V 4G2, Canada
[2] Univ Laval, St Foy, PQ G1V 4G2, Canada
[3] Hotel Dieu, Res Ctr, Quebec City, PQ, Canada
[4] Clin Res Inst Montreal, Montreal, PQ H2W 1R7, Canada
来源
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY | 1997年 / 1343卷 / 01期
基金
英国医学研究理事会;
关键词
kallikrein; bradykinin; kininogen; seminal plasma;
D O I
10.1016/S0167-4838(97)00135-0
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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. (C) 1997 Elsevier Science B.V.
引用
收藏
页码:102 / 106
页数:5
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