Beckner M E, Krutzsch H C, Stracke M L, Williams S T, Gallardo J A, Liotta L A
Laboratory of Pathology, National Cancer Institute, NIH, Bethesda, Maryland 20892, USA.
Cancer Res. 1995 May 15;55(10):2140-9.
A novel immunoglobulin-type protein expressed in blood vessels has been identified. The cDNA for AAMP (angio-associated, migratory cell protein) was first isolated from a human melanoma cell line during a search for motility-associated cell surface proteins. Upon analysis of the tissue distribution of AAMP, it was found to be expressed strongly in endothelial cells, cytotrophoblasts, and poorly differentiated colon adenocarcinoma cells found in lymphatics. The sequence of AAMP predicts a protein (M(r) 49,000) with distant identity (25%) to known proteins. It contains immunoglobulin-like domains [one with multiple homologies to deleted in colon carcinoma (DCC) protein], the WD40 repeat motif, and a heparin-binding consensus sequence. A 1.6-kilobase mRNA transcript of AAMP is detected in tissue culture cell lines and tissues. Affinity-purified polyclonal antibodies, anti-recombinant AAMP, and anti-peptide 189 (AAMP derived) recognize a M(r) 52,000 protein in human tissue and cellular extracts. The protein size is in keeping with the mRNA and predicted sequence. The AAMP-derived peptide, P189, contains a heparin-binding domain (dissociation constant, 14 pmol) and mediates heparin-sensitive cell adhesion. The shared expression of AAMP in endothelial cells, trophoblasts, and tumor cells implies a common function in migrating cells.
一种在血管中表达的新型免疫球蛋白型蛋白已被鉴定出来。AAMP（血管相关迁移细胞蛋白）的cDNA最初是在寻找与运动相关的细胞表面蛋白过程中，从一种人类黑色素瘤细胞系中分离得到的。对AAMP的组织分布进行分析后发现，它在内皮细胞、细胞滋养层细胞以及淋巴管中发现的低分化结肠腺癌细胞中强烈表达。AAMP的序列预测其编码的蛋白分子量为49,000，与已知蛋白有较远的同源性（25%）。它包含免疫球蛋白样结构域[其中一个与结肠癌缺失蛋白（DCC）有多个同源性]、WD40重复基序以及一个肝素结合共有序列。在组织培养细胞系和组织中可检测到1.6千碱基的AAMP mRNA转录本。亲和纯化的多克隆抗体、抗重组AAMP抗体以及抗肽189（源自AAMP）可识别在人类组织和细胞提取物中分子量为52,000的蛋白。该蛋白大小与mRNA和预测序列相符。源自AAMP的肽P189包含一个肝素结合结构域（解离常数为14皮摩尔），并介导肝素敏感的细胞黏附。AAMP在内皮细胞、滋养层细胞和肿瘤细胞中的共同表达意味着其在迁移细胞中具有共同功能。
