PRIMARY STRUCTURE OF HUMAN CORTICOSTEROID BINDING GLOBULIN, DEDUCED FROM HEPATIC AND PULMONARY CDNAS, EXHIBITS HOMOLOGY WITH SERINE PROTEASE INHIBITORS
PRIMARY STRUCTURE OF HUMAN CORTICOSTEROID BINDING GLOBULIN, DEDUCED FROM HEPATIC AND PULMONARY CDNAS, EXHIBITS HOMOLOGY WITH SERINE PROTEASE INHIBITORS
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DOI：
10.1073/pnas.84.15.5153
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发表时间：
1987-08-01
影响因子：
11.1
通讯作者：
BARDIN, CW
中科院分区：
文献类型：
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作者：
HAMMOND, GL;SMITH, CL;BARDIN, CW
我们已经分离和测序的皮质类固醇结合球蛋白（CBG）的cDNA制备从人类肝脏和肺的mRNAs。我们的研究结果表明，CBG mRNA在肝脏中相对丰富，但也存在于肺，睾丸和肾脏。肝CBG cDNA含有405个氨基酸（Mr 45，149）多肽的开放阅读框架。这包括在人CBG的已知NH-2-末端序列之前的22个残基的主要疏水性前导序列。因此，我们预测成熟蛋白质由383个氨基酸组成，是Mr 42，646的多肽。第二个，在框架内，72个碱基对顺反子的未知意义之间存在的TAA终止密码子CBG和可能的聚腺苷酸化信号（AATAAA）位于聚腺苷酸化位点前16个核苷酸。成熟CBG的推导氨基酸序列包含两个半胱氨酸残基和用于连接六个可能的N-连接低聚糖链的共有序列。人肺和肝CBG cDNA的序列在所提出的前导序列中仅相差一个核苷酸，我们将其归因于点突变。在CBG和其它类固醇结合蛋白之间没有发现序列同源性，但是在CBG和α 1-抗胰蛋白酶的氨基酸序列之间存在显著的相似性，并且这延伸到丝氨酸蛋白酶抑制剂（丝氨酸蛋白酶抑制剂）超家族的其它成员。
We have isolated and sequenced cDNAs for corticosteroid binding globulin (CBG) prepared from human liver and lung mRNAs. Our results indicate that CBG mRNA is relatively abundant in the liver but is also present in the lung, testis, and kidney. The liver CBG cDNA contains an open reading frame for a 405-amino acid (Mr 45, 149) polypeptide. This includes a predominantly hydrophobic, leader sequence of 22 residues that precedes the known NH-2-terminal sequence of human CBG. We therefore, predict that the mature protein is composed of 383 amino acids and is a polypeptide of Mr 42,646. A second, in-frame, 72-base-pair cistron of unknown significance exists between the TAA termination codon for CBG and a possible polyadenylation signal (AATAAA) located 16 nucleotides before the poladenylylation site. The deduced amino acid sequence of mature CBG contains two cysteine residues and consensus sequences for the attachment of six possible N-linked oligosaccharide chains. The sequences of the human lung and liver CBG cDNAs differ by only one nucleotide within the proposed leader sequence, and we attribute this to a point mutation. No sequence homology was found between CBG and other steroid binding proteins, but there is a remarkable similarity between the amino acid sequences of CBG and of .alpha.1-antitrypsin, and this extends to other members of the serpin (serine protease inhibitor) superfamily.