CHARACTERIZATION OF A NATURAL INHIBITOR OF THE INSULIN-RECEPTOR TYROSINE KINASE - CDNA CLONING, PURIFICATION, AND ANTI-MITOGENIC ACTIVITY
CHARACTERIZATION OF A NATURAL INHIBITOR OF THE INSULIN-RECEPTOR TYROSINE KINASE - CDNA CLONING, PURIFICATION, AND ANTI-MITOGENIC ACTIVITY
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DOI：
10.1016/0092-8674(89)90098-6
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发表时间：
1989-08-25
期刊：
影响因子：
64.5
通讯作者：
LECAM, A
中科院分区：
文献类型：
--
作者：
AUBERGER, P;FALQUERHO, L;LECAM, A
利用cDNA序列推导出大鼠肝细胞分泌的磷酸化n -糖蛋白（pp63）前体的氨基酸序列。该多肽（Mr = 40,586）富含半胱氨酸和脯氨酸，并含有三个潜在的n -糖基化位点。单个pp63 mRNA种(.apprx。通过亲和层析纯化的pp63抑制胰岛素受体酪氨酸激酶和受体自磷酸化，它在正常肝细胞中发现，但在肝癌细胞中没有发现。只有磷酸化形式的蛋白质是有活性的。此外，pp63在FaO细胞中拮抗胰岛素的促生长作用，但不影响激素介导的酪氨酸转氨酶诱导的这些细胞中氨基酸运输能力的增加。
Amino acid sequence of the precursor of the phosphorylated N-glycoprotein (pp63) secreted by rat hepatocytes was deduced from the cDNA sequence. This polypeptide (Mr = 40,586) was rich in both cysteine and proline and contained three potential N-glycosylation sites. A single pp63 mRNA species (.apprx. 2000 bp), found in normal hepatocytes but not in FaO hepatoma cells, appeared to result from transcription of a single gene, pp63 purified by affinity chromatography inhibited insulin receptor tyrosine kinase and receptor autophosphorylation. Only the phosphorylated form of the protein was active. In addition, pp63 antagonized the growth-promoting action of insulin in FaO cells but did not affect hormone-mediated increase in amino acid transport capacity of tryrosine aminotransferase induction in these cells.