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Placental ecto-ATP diphosphohydrolase: its structural feature distinct from CD39, localization and inhibition on shear-induced platelet aggregation. 1998

K Makita, and T Shimoyama, and Y Sakurai, and H Yagi, and M Matsumoto, and N Narita, and Y Sakamoto, and S Saito, and Y Ikeda, and M Suzuki, and K Titani, and Y Fujimura
Department of the 2nd Internal Medicine of Nara Medical University, Japan.

Human placental ecto-ATP diphosphohydrolase (ATPDase), an 82 kDa single-chain glycoprotein, was purified to high specific activity using a specific murine monoclonal antibody MK33 (IgG1-kappa). Structurally, protein-based analysis showed this enzyme to be almost identical to that of CD39 lymphoid cell activation antigen deduced by cDNA sequencing (Maliszewski CR, et al, J Immunol 1994; 153:3574); but differing in the NH2-terminal amino acid sequence, suggesting that placental ecto-ATPDase is most likely an isoform of CD39 generated by alternative splicing of the pre-mRNA. Functionally, placental ecto-ATPDase totally inhibits the secondary platelet aggregation induced by agonists at a final concentration (f.c.) of 1 microgram/ml. The purified enzyme (1 microgram/ml, final), pre-incubated with washed platelets prior to alpha-thrombin stimulation, completely inhibits the activation of platelet glycoprotein (GP) IIb/IIIa, thereby blocking the binding of fibrinogen or von Willebrand factor to platelets. Further, under different shear stresses, the enzyme modulates platelet aggregation differently. Low shear stress-induced platelet aggregation is blocked by this enzyme in a dose-dependent manner and is totally blocked at f.c. 0.5 microgram/ml. Under high shear stress, however, this protein at a f.c. of 0.5 microgram/ml mediates almost complete disaggregation of platelets without affecting the initial aggregation. Using immunohistochemical analysis, this enzyme was observed to be localized at the syncytiotrophoblasts of placental microvilli and the endothelial cells (ECs) of the umbilical vein obtained at full-term normal delivery, but scarcely at the ECs of the umbilical artery.

UI MeSH Term Description Entries
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D010920 Placenta A highly vascularized mammalian fetal-maternal organ and major site of transport of oxygen, nutrients, and fetal waste products. It includes a fetal portion (CHORIONIC VILLI) derived from TROPHOBLASTS and a maternal portion (DECIDUA) derived from the uterine ENDOMETRIUM. The placenta produces an array of steroid, protein and peptide hormones (PLACENTAL HORMONES). Placentoma, Normal,Placentome,Placentas,Placentomes
D010974 Platelet Aggregation The attachment of PLATELETS to one another. This clumping together can be induced by a number of agents (e.g., THROMBIN; COLLAGEN) and is part of the mechanism leading to the formation of a THROMBUS. Aggregation, Platelet
D011247 Pregnancy The status during which female mammals carry their developing young (EMBRYOS or FETUSES) in utero before birth, beginning from FERTILIZATION to BIRTH. Gestation,Pregnancies
D005260 Female Females
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000251 Adenosine Triphosphatases A group of enzymes which catalyze the hydrolysis of ATP. The hydrolysis reaction is usually coupled with another function such as transporting Ca(2+) across a membrane. These enzymes may be dependent on Ca(2+), Mg(2+), anions, H+, or DNA. ATPases,Adenosinetriphosphatase,ATPase,ATPase, DNA-Dependent,Adenosine Triphosphatase,DNA-Dependent ATPase,DNA-Dependent Adenosinetriphosphatases,ATPase, DNA Dependent,Adenosinetriphosphatases, DNA-Dependent,DNA Dependent ATPase,DNA Dependent Adenosinetriphosphatases,Triphosphatase, Adenosine
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D001081 Apyrase A calcium-activated enzyme that catalyzes the hydrolysis of ATP to yield AMP and orthophosphate. It can also act on ADP and other nucleoside triphosphates and diphosphates. EC 3.6.1.5. ADPase,ATP-Diphosphatase,Adenosine Diphosphatase,ADP Phosphohydrolase,ATP Diphosphohydrolase,ATP-ADPase,ATP ADPase,ATP Diphosphatase,Diphosphatase, Adenosine,Diphosphohydrolase, ATP,Phosphohydrolase, ADP
D013314 Stress, Mechanical A purely physical condition which exists within any material because of strain or deformation by external forces or by non-uniform thermal expansion; expressed quantitatively in units of force per unit area. Mechanical Stress,Mechanical Stresses,Stresses, Mechanical

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