The cDNA cloning of human placental ecto‐ATP diphosphohydrolases I and II 1

FEBS Letters

Yagi, Hideo¹  Kokubo, Tetsuro⁴  Makita, Kaori¹  Fujimura, Yoshihiro³  Sakurai, Yoshihiko³  Narita, Nobuhiro¹  Titani, Koiti²  Matsumoto, Masanori¹  Matsui, Taei² 

[1] Second Department of Internal Medicine, Nara Medical University, Kashihara, Nara 634-8522 Japan;Institute for Comprehensive Medical Science, Fujita Health University, Toyoake, Aichi 470-1192, Japan;Department of Blood Transfusion Medicine, Nara Medical University, Kashihara, Nara 634-8522, Japan;Division of Gene Function in Animals, Nara Institute of Science and Technology, Takayama, Ikoma, Nara 630-0101, Japan

关键词: Ecto-ATP diphosphohydrolase;    Placenta;    cDNA cloning;   

DOI  :  10.1016/S0014-5793(99)00751-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The cDNA clones of two isoforms (enzymes I and II) of human placental ecto-ATP diphosphohydrolases have been isolated based on the N-terminal amino acid (aa) sequence of the immunopurified 82 kDa protein and characterized. The cDNA clone encoding enzyme I consists of 2081 nucleotides and the predicted enzyme I consists of 517 aa residues. Enzyme I has a 5′-UTR and an N-terminal 11 aa sequence that differ from CD39, but the rest of the sequence is the same as CD39. The hydropathy plot indicated that enzyme I has two hydrophobic regions near the N- and C-termini of the molecule. In contrast, enzyme II consists of 1814 nucleotides and the predicted protein consists of 306 aa residues. The sequence of 1–1018 nucleotides of enzyme II is identical to that of enzyme I, but the 1019–1814 nucleotide sequence is different from both enzyme I and CD39. The hydropathy plot indicated that enzyme II has one hydrophobic region near the N-terminus, suggesting that enzyme II is also anchored to the cell membrane. It is, however, likely that some of enzyme II exists as a soluble form in plasma, possibly after proteolytic processing.

【 授权许可】

Unknown