TY - JOUR
T1 - The cDNA cloning of human placental ecto-ATP diphosphohydrolases I and II
AU - Matsumoto, Masanori
AU - Sakurai, Yoshihiko
AU - Kokubo, Tetsuro
AU - Yagi, Hideo
AU - Makita, Kaori
AU - Matsui, Taei
AU - Titani, Koiti
AU - Fujimura, Yoshihiro
AU - Narita, Nobuhiro
N1 - Funding Information:
This work was supported by Research Grants from the Ministry of Health and Welfare of Japan for Cardiovascular Disease (8A-1), from the Japanese Ministry of Education Culture and Science (to Y.F. and K.T.), and from Fujita Health University. The authors also thank Dr. Daniel Mrozek for editing the manuscript.
PY - 1999/6/25
Y1 - 1999/6/25
N2 - 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.
AB - 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.
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U2 - 10.1016/S0014-5793(99)00751-6
DO - 10.1016/S0014-5793(99)00751-6
M3 - Article
C2 - 10405171
AN - SCOPUS:0032812571
SN - 0014-5793
VL - 453
SP - 335
EP - 340
JO - FEBS Letters
JF - FEBS Letters
IS - 3
ER -