Purification and NH2-terminal amino acid sequence of guinea pig tumor-secreted vascular permeability factor.
Purification and NH2-terminal amino acid sequence of guinea pig tumor-secreted vascular permeability factor.
复制标题
DOI：
--
复制
发表时间：
1990-03
期刊：
影响因子：
11.2
通讯作者：
D. Senger;D. Connolly;L. Water;Joseph;Feder;H. Dvorak
中科院分区：
文献类型：
--
作者：
D. Senger;D. Connolly;L. Water;Joseph;Feder;H. Dvorak
啮齿动物和人类肿瘤细胞系分泌一种有效的血管通透性因子（VPF），其引起血浆蛋白的微血管通透性的快速和显著增加，而不引起肥大细胞脱粒或内皮细胞损伤或不刺激炎性细胞浸润[D. R. Senger，S. J. Galli，A. M.德沃夏克角A. Perruzzi，V.S. Harvey和H. F.德沃夏克科学（Wash）DC），219：983-985，1983; D. R.森格角A. Perruzzi，J. Feder和H.F.德沃夏克癌症研究所，46：5629-5632，1986]。VPF现在已经从豚鼠肿瘤细胞培养基中纯化到同质;它是一种Mr 34，000 - 43，000的蛋白质，并且已经推导出NH 2-末端氨基酸序列。用对应于天然蛋白质氨基酸残基1-24的合成肽来产生兔抗体，该抗体结合豚鼠肿瘤细胞分泌的所有血管通透性增加活性，并在免疫印迹上染色纯化的VPF。这些发现确定了该NH 2-末端氨基酸序列源自渗透性因子。同源性搜索发现，VPF的NH 2-末端序列和数据库序列之间没有身份或密切的相似性，表明VPF是从其他蛋白质的序列数据是不同的。特别是，肿瘤分泌的VPF和其他介质的血管通透性增加，包括血浆和腺激肽释放酶之间没有发现序列相似性。
Rodent and human tumor cell lines secrete a potent vascular permeability factor (VPF) which causes a rapid and substantial increase in microvascular permeability to plasma proteins without causing mast cell degranulation, or endothelial cell damage or without exciting an inflammatory cell infiltrate [D. R. Senger, S. J. Galli, A. M. Dvorak, C. A. Perruzzi, V. S. Harvey, and H. F. Dvorak. Science (Wash. DC), 219: 983-985, 1983; D. R. Senger, C. A. Perruzzi, J. Feder, and H.F. Dvorak. Cancer Res., 46: 5629-5632, 1986]. VPF now has been purified to homogeneity from guinea pig tumor cell culture medium; it is a Mr 34,000-43,000 protein, and a NH2-terminal amino acid sequence has been derived. A synthetic peptide corresponding to amino acid residues 1-24 of the native protein was used to raise rabbit antibodies which bind all of the vessel permeability-increasing activity secreted by guinea pig tumor cells and which stain purified VPF on immunoblots. These findings establish that this NH2-terminal amino acid sequence was derived from the permeability factor. Homology searches found no identity or close similarity between VPF NH2-terminal sequence and database sequences, indicating that VPF is distinct from other proteins for which sequence data are available. In particular, no sequence similarity was found between tumor-secreted VPF and other mediators of increased vessel permeability including plasma and glandular kallikreins.