ライフサイエンスコーパス: E-NTPDase

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1 E-NTPDase antagonists reduced transcription of IL-2 mRNA

2 E-NTPDases are extracellular enzymes that hydrolyze nucl

3 mouse homologue that has been designated as E-NTPDase 8.

4 Human ecto-ATPase (E-NTPDase 2) and chicken ecto-ATP-diphosphohydrolase (E-

5 In contrast to the chicken E-NTPDase 8, the human E-NTPDase 8 hydrolyzes MgADP poor

6 HEK293 cells differ from that of the chicken E-NTPDase 8.

7 -nucleoside triphosphate dephosphohydrolase (E-NTPDase) with specificity for nucleotide diphosphates

8 ween structure and function of the different E-NTPDases, existence of liver ecto-ATPDase isoforms in

9 2) and chicken ecto-ATP-diphosphohydrolase (E-NTPDase 8) are cell surface nucleotidases with two tra

10 nucleoside triphosphate diphosphohydrolase (E-NTPDase) family.

11 hat the CD39L2 gene encodes an extracellular E-NTPDase.

12 side triphosphate diphosphohydrolase family (E-NTPDase).

13 ry structures, enzymatic properties of human E-NTPDase 8 expressed in HEK293 cells differ from that o

14 ell as in determining the structure of human E-NTPDase 8.

15 t to detergent inhibition, the soluble human E-NTPDase 8 ECD displays greater activity with Ca nucleo

16 The soluble human E-NTPDase 8 which was secreted into the culture media of

17 The human E-NTPDase 8 has similar topology as the avian and mouse

18 ntrast to the chicken E-NTPDase 8, the human E-NTPDase 8 hydrolyzes MgADP poorly and is inhibited by

19 the extracellular domain (ECD) of the human E-NTPDase 8 was constructed.

20 of the transmembranous domains of the human E-NTPDase 8.

21 The human E-NTPDase gene family currently consists of five reporte

22 has similar topology as the avian and mouse E-NTPDase 8 but has fewer potential N-glycosylation site

23 exacerbation and explored the expression of E-NTPDase 1, 2, 3, and 8, and E-NPP1, 2, and 3, in their

24 that are also present in other cell surface E-NTPDases.

25 Here we report that E-NTPDase activity is up-regulated within 15 min of T ce

26 cDNAs with high homology with members of the E-NTPDase family that encode predicted proteins of 495,

27 NK cells and CD8(+) T cells as well as their E-NTPDase activity.

28 ate that (1) the C- and N-termini of the two E-NTPDases encompassing the two transmembranous domains

29 ne if the transmembranous domains of the two E-NTPDases mediate their respective responses to deterge

30 curs in the extracellular domains of the two E-NTPDases responds differently to conformational constr

31 2 shows characteristic features of a typical E-NTPDase, but with a much higher degree of specificity

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