Cleaved bovine prolactin-related protein-I stimulates vascular endothelial cell proliferation
Cleaved bovine prolactin-related protein-I stimulates vascular endothelial cell proliferation
复制标题
DOI：
10.1016/j.mce.2010.03.008
复制
发表时间：
2010-07-29
影响因子：
4.1
通讯作者：
Hashizume, Kazuyoshi
中科院分区：
文献类型：
--
作者：
Ushizawa, Koichi;Takahashi, Toru;Hashizume, Kazuyoshi
催乳素相关蛋白-I（PRP 1）是牛的非经典催乳素（PRL）/生长激素家族的成员。然而，它的功能仍然未知。PRL，当被组织蛋白酶D和基质金属蛋白酶（MMP）切割时，导致切割的N-末端16 kDa片段（16 K-PRL），其在人类和啮齿动物中具有抗血管生成特性。我们研究了牛PRP 1类似活性的可能性。PRP 1（通常为33 kDa）被组织蛋白酶（CTS）裂解。MMPs和牛子叶条件培养基（BCCM），主要产生26 kDa的N末端片段。两种特异性酶家族，CTS和MMPs切割完整的PRP 1，BCCM也含有PRP 1切割活性。在使用牛脑血管内皮细胞的细胞增殖测定中检查切割的PRP 1的促或抗血管生成的生物活性。切割的PRP 1在体外使内皮细胞增殖。切割的PRP 1的内皮细胞增殖活性可能在特定的牛胎盘血管生成中共享。(C)2010爱思唯尔爱尔兰有限公司版权所有。
Prolactin-related protein-I (PRP1) is a member of a non-classical prolactin (PRL)/growth hormone family in cattle. However, its function is still unknown. PRL, when cleaved by cathepsin D and matrix metalloproteinases (MMPs), resulted in cleaved N-terminal 16 kDa fragments (16K-PRL) that have antiangiogenetic properties in human and rodents. We examined the possibility of similar activity of bovine PRP1. PRP1 (normally 33 kDa) was cleaved by cathepsins (CTSs). MMPs, and bovine cotyledonary-conditioned medium (BCCM), and generated mainly 26 kDa N-terminal fragments. Two specific enzyme families, CTSs and MMPs cleaved intact PRP1, and BCCM also contained PRP1 cleavage activity. Bioactivity for pro- or anti-angiogenesis of the cleaved PRP1 was examined in a cell proliferation assay using bovine brain vascular endothelial cells. The cleaved PRP1 proliferated the endothelial cells in vitro. The endothelial cell proliferation activity of cleaved PRP1 may be shared in specific bovine placentomal angiogenesis. (C) 2010 Elsevier Ireland Ltd. All rights reserved.