A heparin binding protein whose expression increases during differentiation of embryonal carcinoma cells to parietal endoderm cells: cDNA cloning and sequence analysis.
A heparin binding protein whose expression increases during differentiation of embryonal carcinoma cells to parietal endoderm cells: cDNA cloning and sequence analysis.
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一种肝素结合蛋白，其表达在胚胎癌细胞向壁内胚层细胞分化过程中增加：cDNA克隆和序列分析。
DOI：
10.1093/oxfordjournals.jbchem.a123197
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发表时间：
1990
影响因子：
2.7
通讯作者：
T. Muramatsu
中科院分区：
文献类型：
--
作者：
T. Furukawa;M. Ozawa;R. Huang;T. Muramatsu
从畸胎瘤OTT 6050的λ gt 11表达文库中分离的cDNA克隆指定了分子量约为44，000的糖蛋白。新的糖蛋白被称为肝素结合蛋白-44（HBP-44），因为它被吸收到肝素-琼脂糖柱上，并被含有1.5 M NaCl的缓冲液洗脱。HBP-44 mRNA在PYS-2壁内胚层细胞和肾脏中强烈表达，并且在F9胚胎癌细胞向壁内胚层细胞分化期间RNA水平增加约10倍。从cDNA序列，HBP-44的结论是富含带电荷的氨基酸，和大片段的蛋白质似乎形成α-螺旋。认为该蛋白通过N-末端区域中存在的疏水氨基酸簇锚定至膜。事实上，HBP-44的N末端序列与脱唾液酸糖蛋白受体同源，后者通过N末端区域锚定在膜上。此外，HBP-44的N-末端区域的一部分与亮氨酸拉链结构域同源。HBP-44与肌球蛋白重链等结构蛋白除N-末端区域外，其余区域均具有同源性。我们认为HBP-44被挤出质膜，与肝素和相关分子相互作用，并参与质膜与基底膜的相互作用。
A cDNA clone isolated from a lambda gt11 expression library of teratocarcinoma OTT6050 specifies for a glycoprotein with a molecular weight of about 44,000. The new glycoprotein was termed heparin binding protein-44 (HBP-44), since it was absorbed to a heparin-agarose column and was eluted from it by a buffer containing 1.5 M NaCl. HBP-44 mRNA was intensely expressed in PYS-2 parietal endoderm cells and in the kidney, and the RNA level increased about 10-fold during differentiation of F9 embryonal carcinoma cells to parietal endoderm cells. From the cDNA sequence, HBP-44 was concluded to be rich in charged amino acids, and large segments of the protein appeared to form alpha-helixes. The protein was considered to be anchored to the membrane by a cluster of hydrophobic amino acids present in the N-terminal region. Indeed, the N-terminal sequence of HBP-44 was homologous to asialoglycoprotein receptor, which is anchored to the membrane by the N-terminal region. Furthermore, a portion of the N-terminal region of HBP-44 was homologous to the leucine zipper domain. Except for the N-terminal region, HBP-44 had over-all homology with structural proteins such as myosin heavy chain. We propose that HBP-44 is extruded from plasma membranes and interacts with heparin and related molecules and that it is involved in the interactions of plasma membranes with basement membranes.