Prostatic acid phosphatase degrades lysophosphatidic acid in seminal plasma
Prostatic acid phosphatase degrades lysophosphatidic acid in seminal plasma
复制标题
DOI：
10.1016/j.febslet.2004.06.083
复制
发表时间：
2004-07-30
期刊：
影响因子：
3.5
通讯作者：
Arai, H
中科院分区：
文献类型：
--
作者：
Tanaka, M;Kishi, Y;Arai, H
溶血磷脂酸（LPA）是一种具有多种生物活性的脂质介质，可在包括人精浆在内的各种生物体液中检测到。由于其细胞增殖刺激和抗凋亡活性，LPA已涉及一些癌症如卵巢癌和前列腺癌的进展。在这里，我们表明，前列腺酸性磷酸酶，这是一种非特异性磷酸酶，并已牵连在前列腺癌的进展，失活LPA在人类精浆。人类精浆含有一种LPA合成酶lysoPLD（将溶血磷脂转化为LPA并负责血清中LPA的产生）及其主要底物溶血磷脂酰胆碱。在血清中，LPA在37 ℃孵育期间积累。然而，在精浆中，LPA没有积累。这种差异是由一个强大的LPA降解活性的存在解释。LPA与精浆孵育导致LPA的消失和伴随的甘油单酯的积累，表明LPA被精浆中存在的磷酸酶活性降解。当精浆在磷酸酶抑制剂原钒酸钠存在下孵育时，LPA积累，表明LPA在流体中产生和降解。LPA-磷酸酶活性的生化表征确定了两个磷酸酶活性在人精浆。通过Western印迹分析结合几个柱层析，揭示了主要的活性是相同的前列腺酸性磷酸酶。目前的研究表明，活跃的LPA代谢精浆中，并指出LPA信号在男性性器官，包括前列腺癌的可能作用。(C)2004年由Elsevier B. V.代表欧洲生物化学学会联合会出版。
Lysophosphatidic acid (LPA) is a lipid mediator with multiple biological activities and is detected in various biological fluids, including human seminal plasma. Due to its cell proliferation stimulatory and anti-apoptotic activities, LPA has been implicated in the progression of some cancers such as ovarian cancer and prostate cancer. Here, we show that prostatic acid phosphatase, which is a non-specific phosphatase and which has been implicated in the progression of prostate cancer, inactivates LPA in human seminal plasma. Human seminal plasma contains both an LPA-synthetic enzyme, lysoPLD, which converts lysophospholipids to LPA and is responsible for LPA production in serum, and its major substrate, lysophosphatidylcholine. In serum, LPA accumulated during incubation at 37 degreesC. However, in seminal plasma, LPA did not accumulate. This discrepancy is explained by the presence of a strong LPA-degrading activity. Incubation of LPA with seminal plasma resulted in the disappearance of LPA and an accompanying accumulation of monoglyceride showing that LPA is degraded by phosphatase activity present in the seminal plasma. When seminal plasma was incubated in the presence of a phosphatase inhibitor, sodium orthovanadate, LPA accumulated, indicating that LPA is produced and degraded in the fluid. Biochemical characterization of the LPA-phosphatase activity identified two phosphatase activities in human seminal plasma. By Western blotting analysis in combination with several column chromatographies, the major activity was revealed to be identical to prostatic acid phosphatase. The present study demonstrates active LPA metabolism in seminal plasma and indicates the possible role of LPA signaling in male sexual organs including prostate cancer. (C) 2004 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.