Ectodomain shedding of cystinyl aminopeptidase from human placental membranes.
Ectodomain shedding of cystinyl aminopeptidase from human placental membranes.
复制标题
胱氨酰氨肽酶从人胎盘膜上脱落的胞外域。
作者：
L. Ofner;N. Hooper
半胱氨酸氨基肽酶（CAP; EC 3.4.11.3）是胎盘膜的一种完整蛋白，在妊娠期间也以可溶性形式存在于母体血清中。发现CAP在一个温度和时间依赖的过程中从人胎盘膜脱落。经Triton X-114相分离和高速离心鉴定，CAP的释放形态为亲水性。羟肟酸类化合物marimastat和BB3103可抑制CAP的胞外结构域脱落。CAP蛋白脱落的抑制谱与血管紧张素转换酶的释放的抑制谱不同，暗示不同的锌金属分泌酶参与了这两种蛋白的脱落。这些结果有助于我们理解在某些妊娠相关疾病（如先兆子痫）中观察到的血清CAP水平降低的机制。
Cystinyl aminopeptidase (CAP; EC 3.4.11.3) is an integral protein of the placental membrane that is also found in a soluble form in maternal serum during pregnancy. CAP was found to be shed from human placental membranes in a temperature- and time-dependent process. The released form of CAP was hydrophilic as assessed by phase separation in Triton X-114 and high-speed centrifugation. This ectodomain shedding of CAP was inhibited by the hydroxamic acid-based compounds marimastat and BB3103. The inhibition profile for the shedding of CAP was distinct to that for the release of angiotensin converting enzyme, implicating the involvement of distinct zinc metallosecretases in the shedding of these two proteins. These results have implications for our understanding of the mechanism underlying the reduction in serum levels of CAP observed in certain pregnancy-related disorders, such as pre-eclampsia.
DOI：
10.1210/jcem.78.2.8106636
发表时间：
1994-02
期刊：
The Journal of clinical endocrinology and metabolism
影响因子：
--
作者：
A M Germain;J. Smith;M. Casey;P. MacDonald
通讯作者：
A M Germain;J. Smith;M. Casey;P. MacDonald
影响因子：
56.9
作者：
Peschon, JJ;Slack, JL;Black, RA
通讯作者：
Black, RA