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{{Infobox_gene}}
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'''Ectonucleoside triphosphate diphosphohydrolase-1''' (gene: '''''ENTPD1'''''; protein: '''NTPDase1''') also known as '''CD39''' ('''C'''luster of '''D'''ifferentiation '''39'''), is a typical cell surface-located enzymes with an extracellularly facing catalytic site.<ref>{{cite web | title = Entrez Gene: ENTPD1 Ectonucleoside triphosphate diphosphohydrolase 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=953| accessdate = }}</ref><ref>{{cite journal | vauthors = Sévigny J, Levesque FP, Grondin G, Beaudoin AR | title = Purification of the blood vessel ATP diphosphohydrolase, identification and localisation by immunological techniques | journal = Biochimica et Biophysica Acta | volume = 1334 | issue = 1 | pages = 73–88 | date = Feb 1997 | pmid = 9042368 | doi=10.1016/s0304-4165(96)00079-7}}</ref><ref>{{cite journal | vauthors = Kaczmarek E, Koziak K, Sévigny J, Siegel JB, Anrather J, Beaudoin AR, Bach FH, Robson SC | title = Identification and characterization of CD39/vascular ATP diphosphohydrolase | journal = The Journal of Biological Chemistry | volume = 271 | issue = 51 | pages = 33116–22 | date = Dec 1996 | pmid = 8955160 | doi=10.1074/jbc.271.51.33116}}</ref> NTPDase1 is an [[ectonucleotidase]] that catalyse the hydrolysis of γ- and β-phosphate residues of triphospho- and diphosphonucleosides to the monophosphonucleoside derivative.<ref>{{cite journal | vauthors = Robson SC, Sévigny J, Zimmermann H | title = The E-NTPDase family of ectonucleotidases: Structure function relationships and pathophysiological significance | journal = Purinergic Signalling | volume = 2 | issue = 2 | pages = 409–30 | date = Jun 2006 | pmid = 18404480 | pmc = 2254478 | doi = 10.1007/s11302-006-9003-5 }}</ref><ref>{{cite journal | vauthors = Yegutkin GG | title = Nucleotide- and nucleoside-converting ectoenzymes: Important modulators of purinergic signalling cascade | journal = Biochimica et Biophysica Acta | volume = 1783 | issue = 5 | pages = 673–94 | date = May 2008 | pmid = 18302942 | doi = 10.1016/j.bbamcr.2008.01.024 }}</ref> For example, NTPDase1 hydrolyzes [[P2 receptor]] ligands, namely [[Adenosine triphosphate|ATP]], [[Adenosine diphosphate|ADP]], UTP and UDP with similar efficacy.<ref>{{cite journal | vauthors = Kukulski F, Lévesque SA, Lavoie EG, Lecka J, Bigonnesse F, Knowles AF, Robson SC, Kirley TL, Sévigny J | title = Comparative hydrolysis of P2 receptor agonists by NTPDases 1, 2, 3 and 8 | journal = Purinergic Signalling | volume = 1 | issue = 2 | pages = 193–204 | date = Jun 2005 | pmid = 18404504 | pmc = 2096530 | doi = 10.1007/s11302-005-6217-x }}</ref>  NTPDase1 can therefore affect P2 receptor activation and functions.<ref>{{cite journal | vauthors = Kukulski F, Lévesque SA, Sévigny J | title = Impact of ectoenzymes on p2 and p1 receptor signaling | journal = Advances in Pharmacology | volume = 61 | pages = 263–99 | date = 2011-01-01 | pmid = 21586362 | doi = 10.1016/B978-0-12-385526-8.00009-6 }}</ref>
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== See also ==
{{GNF_Protein_box
* [[Cluster of differentiation]]
| image =
| image_source =
| PDB =
| Name = Ectonucleoside triphosphate diphosphohydrolase 1
| HGNCid = 3363
| Symbol = ENTPD1
| AltSymbols =; ATPDase; CD39; NTPDase-1
| OMIM = 601752
| ECnumber = 
| Homologene = 20423
| MGIid = 102805
| GeneAtlas_image1 = PBB_GE_ENTPD1_209473_at_tn.png
| GeneAtlas_image2 = PBB_GE_ENTPD1_207691_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_ENTPD1_209474_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}}
| Process = {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0007596 |text = blood coagulation}} {{GNF_GO|id=GO:0019735 |text = antimicrobial humoral response}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 953
    | Hs_Ensembl = ENSG00000138185
    | Hs_RefseqProtein = NP_001767
    | Hs_RefseqmRNA = NM_001776
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 10
    | Hs_GenLoc_start = 97461526
    | Hs_GenLoc_end = 97619442
    | Hs_Uniprot = P49961
    | Mm_EntrezGene = 12495
    | Mm_Ensembl = ENSMUSG00000048120
    | Mm_RefseqmRNA = NM_009848
    | Mm_RefseqProtein = NP_033978
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 19
    | Mm_GenLoc_start = 40764473
    | Mm_GenLoc_end = 40794913
    | Mm_Uniprot = Q544U5
  }}
}}
'''Ectonucleoside triphosphate diphosphohydrolase 1''' ('''ENTPD1''') also known as '''CD39''' ('''C'''luster of '''D'''ifferentiation '''39'''), is a human [[gene]].<ref>{{cite web | title = Entrez Gene: ENTPD1 Ectonucleoside triphosphate diphosphohydrolase 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=953| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== References ==
{{PBB_Summary
{{reflist}}
| section_title =
| summary_text =
}}


==References==
== Further reading ==
{{reflist|2}}
 
==See also==
* [[Cluster of differentiation]]
 
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Maliszewski CR, Delespesse GJ, Schoenborn MA, Armitage RJ, Fanslow WC, Nakajima T, Baker E, Sutherland GR, Poindexter K, Birks C | title = The CD39 lymphoid cell activation antigen. Molecular cloning and structural characterization | journal = Journal of Immunology | volume = 153 | issue = 8 | pages = 3574–83 | date = Oct 1994 | pmid = 7930580 | doi =  }}
| citations =
* {{cite journal | vauthors = Christoforidis S, Papamarcaki T, Galaris D, Kellner R, Tsolas O | title = Purification and properties of human placental ATP diphosphohydrolase | journal = European Journal of Biochemistry / FEBS | volume = 234 | issue = 1 | pages = 66–74 | date = Nov 1995 | pmid = 8529670 | doi = 10.1111/j.1432-1033.1995.066_c.x }}
*{{cite journal | author=Maliszewski CR, Delespesse GJ, Schoenborn MA, ''et al.'' |title=The CD39 lymphoid cell activation antigen. Molecular cloning and structural characterization. |journal=J. Immunol. |volume=153 |issue= 8 |pages= 3574-83 |year= 1994 |pmid= 7930580 |doi=  }}
* {{cite journal | vauthors = Wang TF, Guidotti G | title = CD39 is an ecto-(Ca2+,Mg2+)-apyrase | journal = The Journal of Biological Chemistry | volume = 271 | issue = 17 | pages = 9898–901 | date = Apr 1996 | pmid = 8626624 | doi = 10.1074/jbc.271.17.9898 }}
*{{cite journal | author=Christoforidis S, Papamarcaki T, Galaris D, ''et al.'' |title=Purification and properties of human placental ATP diphosphohydrolase. |journal=Eur. J. Biochem. |volume=234 |issue= 1 |pages= 66-74 |year= 1996 |pmid= 8529670 |doi= }}
* {{cite journal | vauthors = Kaczmarek E, Koziak K, Sévigny J, Siegel JB, Anrather J, Beaudoin AR, Bach FH, Robson SC | title = Identification and characterization of CD39/vascular ATP diphosphohydrolase | journal = The Journal of Biological Chemistry | volume = 271 | issue = 51 | pages = 33116–22 | date = Dec 1996 | pmid = 8955160 | doi = 10.1074/jbc.271.51.33116 }}
*{{cite journal | author=Wang TF, Guidotti G |title=CD39 is an ecto-(Ca2+,Mg2+)-apyrase. |journal=J. Biol. Chem. |volume=271 |issue= 17 |pages= 9898-901 |year= 1996 |pmid= 8626624 |doi= }}
* {{cite journal | vauthors = Robson SC, Kaczmarek E, Siegel JB, Candinas D, Koziak K, Millan M, Hancock WW, Bach FH | title = Loss of ATP diphosphohydrolase activity with endothelial cell activation | journal = The Journal of Experimental Medicine | volume = 185 | issue = 1 | pages = 153–63 | date = Jan 1997 | pmid = 8996251 | pmc = 2196106 | doi = 10.1084/jem.185.1.153 }}
*{{cite journal | author=Kaczmarek E, Koziak K, Sévigny J, ''et al.'' |title=Identification and characterization of CD39/vascular ATP diphosphohydrolase. |journal=J. Biol. Chem. |volume=271 |issue= 51 |pages= 33116-22 |year= 1997 |pmid= 8955160 |doi= }}
* {{cite journal | vauthors = Gray IC, Fallowfield J, Ford S, Nobile C, Volpi EV, Spurr NK | title = An integrated physical and genetic map spanning chromosome band 10q24 | journal = Genomics | volume = 43 | issue = 1 | pages = 85–8 | date = Jul 1997 | pmid = 9226376 | doi = 10.1006/geno.1997.4809 }}
*{{cite journal | author=Robson SC, Kaczmarek E, Siegel JB, ''et al.'' |title=Loss of ATP diphosphohydrolase activity with endothelial cell activation. |journal=J. Exp. Med. |volume=185 |issue= 1 |pages= 153-63 |year= 1997 |pmid= 8996251 |doi= }}
* {{cite journal | vauthors = Makita K, Shimoyama T, Sakurai Y, Yagi H, Matsumoto M, Narita N, Sakamoto Y, Saito S, Ikeda Y, Suzuki M, Titani K, Fujimura Y | title = Placental ecto-ATP diphosphohydrolase: its structural feature distinct from CD39, localization and inhibition on shear-induced platelet aggregation | journal = International Journal of Hematology | volume = 68 | issue = 3 | pages = 297–310 | date = Oct 1998 | pmid = 9846014 | doi = 10.1016/S0925-5710(98)00080-2 }}
*{{cite journal | author=Gray IC, Fallowfield J, Ford S, ''et al.'' |title=An integrated physical and genetic map spanning chromosome band 10q24. |journal=Genomics |volume=43 |issue= 1 |pages= 85-8 |year= 1997 |pmid= 9226376 |doi= 10.1006/geno.1997.4809 }}
* {{cite journal | vauthors = Matsumoto M, Sakurai Y, Kokubo T, Yagi H, Makita K, Matsui T, Titani K, Fujimura Y, Narita N | title = The cDNA cloning of human placental ecto-ATP diphosphohydrolases I and II | journal = FEBS Letters | volume = 453 | issue = 3 | pages = 335–40 | date = Jun 1999 | pmid = 10405171 | doi = 10.1016/S0014-5793(99)00751-6 }}
*{{cite journal | author=Makita K, Shimoyama T, Sakurai Y, ''et al.'' |title=Placental ecto-ATP diphosphohydrolase: its structural feature distinct from CD39, localization and inhibition on shear-induced platelet aggregation. |journal=Int. J. Hematol. |volume=68 |issue= 3 |pages= 297-310 |year= 1999 |pmid= 9846014 |doi= }}
* {{cite journal | vauthors = Kittel A, Kaczmarek E, Sevigny J, Lengyel K, Csizmadia E, Robson SC | title = CD39 as a caveolar-associated ectonucleotidase | journal = Biochemical and Biophysical Research Communications | volume = 262 | issue = 3 | pages = 596–9 | date = Sep 1999 | pmid = 10471369 | doi = 10.1006/bbrc.1999.1254 }}
*{{cite journal | author=Matsumoto M, Sakurai Y, Kokubo T, ''et al.'' |title=The cDNA cloning of human placental ecto-ATP diphosphohydrolases I and II. |journal=FEBS Lett. |volume=453 |issue= 3 |pages= 335-40 |year= 1999 |pmid= 10405171 |doi= }}
* {{cite journal | vauthors = Koziak K, Kaczmarek E, Kittel A, Sévigny J, Blusztajn JK, Schulte Am Esch J, Imai M, Guckelberger O, Goepfert C, Qawi I, Robson SC | title = Palmitoylation targets CD39/endothelial ATP diphosphohydrolase to caveolae | journal = The Journal of Biological Chemistry | volume = 275 | issue = 3 | pages = 2057–62 | date = Jan 2000 | pmid = 10636909 | doi = 10.1074/jbc.275.3.2057 | first8 = O | last9 = Goepfert | last7 = Imai | last8 = Guckelberger | first9 = C | author6 = Schulte Am Esch J 2nd | first7 = M }}
*{{cite journal | author=Kittel A, Kaczmarek E, Sevigny J, ''et al.'' |title=CD39 as a caveolar-associated ectonucleotidase. |journal=Biochem. Biophys. Res. Commun. |volume=262 |issue= 3 |pages= 596-9 |year= 1999 |pmid= 10471369 |doi= 10.1006/bbrc.1999.1254 }}
* {{cite journal | vauthors = Dias Neto E, Correa RG, Verjovski-Almeida S, Briones MR, Nagai MA, da Silva W, Zago MA, Bordin S, Costa FF, Goldman GH, Carvalho AF, Matsukuma A, Baia GS, Simpson DH, Brunstein A, de Oliveira PS, Bucher P, Jongeneel CV, O'Hare MJ, Soares F, Brentani RR, Reis LF, de Souza SJ, Simpson AJ | title = Shotgun sequencing of the human transcriptome with ORF expressed sequence tags | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 97 | issue = 7 | pages = 3491–6 | date = Mar 2000 | pmid = 10737800 | pmc = 16267 | doi = 10.1073/pnas.97.7.3491 }}
*{{cite journal | author=Koziak K, Kaczmarek E, Kittel A, ''et al.'' |title=Palmitoylation targets CD39/endothelial ATP diphosphohydrolase to caveolae. |journal=J. Biol. Chem. |volume=275 |issue= 3 |pages= 2057-62 |year= 2000 |pmid= 10636909 |doi= }}
* {{cite journal | vauthors = Goepfert C, Imai M, Brouard S, Csizmadia E, Kaczmarek E, Robson SC | title = CD39 modulates endothelial cell activation and apoptosis | journal = Molecular Medicine | volume = 6 | issue = 7 | pages = 591–603 | date = Jul 2000 | pmid = 10997340 | pmc = 1949966 | doi =  }}
*{{cite journal  | author=Dias Neto E, Correa RG, Verjovski-Almeida S, ''et al.'' |title=Shotgun sequencing of the human transcriptome with ORF expressed sequence tags. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 7 |pages= 3491-6 |year= 2000 |pmid= 10737800 |doi=  }}
* {{cite journal | vauthors = Kittel A, Garrido M, Varga G | title = Localization of NTPDase1/CD39 in normal and transformed human pancreas | journal = The Journal of Histochemistry and Cytochemistry | volume = 50 | issue = 4 | pages = 549–56 | date = Apr 2002 | pmid = 11897808 | doi = 10.1177/002215540205000412 }}
*{{cite journal | author=Goepfert C, Imai M, Brouard S, ''et al.'' |title=CD39 modulates endothelial cell activation and apoptosis. |journal=Mol. Med. |volume=6 |issue= 7 |pages= 591-603 |year= 2001 |pmid= 10997340 |doi= }}
* {{cite journal | vauthors = Kaneider NC, Egger P, Dunzendorfer S, Noris P, Balduini CL, Gritti D, Ricevuti G, Wiedermann CJ | title = Reversal of thrombin-induced deactivation of CD39/ATPDase in endothelial cells by HMG-CoA reductase inhibition: effects on Rho-GTPase and adenosine nucleotide metabolism | journal = Arteriosclerosis, Thrombosis, and Vascular Biology | volume = 22 | issue = 6 | pages = 894–900 | date = Jun 2002 | pmid = 12067895 | doi = 10.1161/01.ATV.0000018305.95943.F7 }}
*{{cite journal | author=Adrian K, Bernhard MK, Breitinger HG, Ogilvie A |title=Expression of purinergic receptors (ionotropic P2X1-7 and metabotropic P2Y1-11) during myeloid differentiation of HL60 cells. |journal=Biochim. Biophys. Acta |volume=1492 |issue= 1 |pages= 127-38 |year= 2000 |pmid= 11004484 |doi=  }}
* {{cite journal | vauthors = Drosopoulos JH | title = Roles of Asp54 and Asp213 in Ca2+ utilization by soluble human CD39/ecto-nucleotidase | journal = Archives of Biochemistry and Biophysics | volume = 406 | issue = 1 | pages = 85–95 | date = Oct 2002 | pmid = 12234494 | doi = 10.1016/S0003-9861(02)00414-9 }}
*{{cite journal | author=Kittel A, Garrido M, Varga G |title=Localization of NTPDase1/CD39 in normal and transformed human pancreas. |journal=J. Histochem. Cytochem. |volume=50 |issue= 4 |pages= 549-56 |year= 2002 |pmid= 11897808 |doi= }}
* {{cite journal | vauthors = Krötz F, Sohn HY, Keller M, Gloe T, Bolz SS, Becker BF, Pohl U | title = Depolarization of endothelial cells enhances platelet aggregation through oxidative inactivation of endothelial NTPDase | journal = Arteriosclerosis, Thrombosis, and Vascular Biology | volume = 22 | issue = 12 | pages = 2003–9 | date = Dec 2002 | pmid = 12482826 | doi = 10.1161/01.ATV.0000043454.08172.51 }}
*{{cite journal | author=Kaneider NC, Egger P, Dunzendorfer S, ''et al.'' |title=Reversal of thrombin-induced deactivation of CD39/ATPDase in endothelial cells by HMG-CoA reductase inhibition: effects on Rho-GTPase and adenosine nucleotide metabolism. |journal=Arterioscler. Thromb. Vasc. Biol. |volume=22 |issue= 6 |pages= 894-900 |year= 2002 |pmid= 12067895 |doi= }}
* {{cite journal | vauthors = Rossatto ER, da Silva LB, Pereira GS, Bonan CD, Battastini AM, Ribeiro JP, Sarkis JJ | title = ATP diphosphohydrolase in human platelets from patients with coronary arteries heart disease | journal = Platelets | volume = 14 | issue = 1 | pages = 47–52 | date = Feb 2003 | pmid = 12623446 | doi = 10.1080/0953710021000062923 }}
*{{cite journal | author=Drosopoulos JH |title=Roles of Asp54 and Asp213 in Ca2+ utilization by soluble human CD39/ecto-nucleotidase. |journal=Arch. Biochem. Biophys. |volume=406 |issue= 1 |pages= 85-95 |year= 2002 |pmid= 12234494 |doi= }}
* {{cite journal | vauthors = Sørensen CE, Amstrup J, Rasmussen HN, Ankorina-Stark I, Novak I | title = Rat pancreas secretes particulate ecto-nucleotidase CD39 | journal = The Journal of Physiology | volume = 551 | issue = Pt 3 | pages = 881–92 | date = Sep 2003 | pmid = 12832497 | pmc = 2343304 | doi = 10.1113/jphysiol.2003.049411 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
* {{cite journal | vauthors = Sévigny J, Sundberg C, Braun N, Guckelberger O, Csizmadia E, Qawi I, Imai M, Zimmermann H, Robson SC | title = Differential catalytic properties and vascular topography of murine nucleoside triphosphate diphosphohydrolase 1 (NTPDase1) and NTPDase2 have implications for thromboregulation | journal = Blood | volume = 99 | issue = 8 | pages = 2801–9 | date = Apr 2002 | pmid = 11929769 | doi=10.1182/blood.v99.8.2801}}
*{{cite journal | author=Krötz F, Sohn HY, Keller M, ''et al.'' |title=Depolarization of endothelial cells enhances platelet aggregation through oxidative inactivation of endothelial NTPDase. |journal=Arterioscler. Thromb. Vasc. Biol. |volume=22 |issue= 12 |pages= 2003-9 |year= 2002 |pmid= 12482826 |doi= }}
*{{cite journal | author=Rossatto ER, da Silva LB, Pereira GS, ''et al.'' |title=ATP diphosphohydrolase in human platelets from patients with coronary arteries heart disease. |journal=Platelets |volume=14 |issue= 1 |pages= 47-52 |year= 2003 |pmid= 12623446 |doi= }}
*{{cite journal | author=Sørensen CE, Amstrup J, Rasmussen HN, ''et al.'' |title=Rat pancreas secretes particulate ecto-nucleotidase CD39. |journal=J. Physiol. (Lond.) |volume=551 |issue= Pt 3 |pages= 881-92 |year= 2004 |pmid= 12832497 |doi= 10.1113/jphysiol.2003.049411 }}
}}
{{refend}}
{{refend}}


==External links==
== External links ==
* {{MeshName|ENTPD1+protein,+human}}
* {{MeshName|ENTPD1+protein,+human}}


{{membrane-protein-stub}}
{{Clusters of differentiation}}
{{Clusters of differentiation}}
[[Category:Clusters of differentiation]]
[[Category:Clusters of differentiation]]
{{WikiDoc Sources}}
 
 
{{membrane-protein-stub}}

Latest revision as of 00:49, 27 October 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Ectonucleoside triphosphate diphosphohydrolase-1 (gene: ENTPD1; protein: NTPDase1) also known as CD39 (Cluster of Differentiation 39), is a typical cell surface-located enzymes with an extracellularly facing catalytic site.[1][2][3] NTPDase1 is an ectonucleotidase that catalyse the hydrolysis of γ- and β-phosphate residues of triphospho- and diphosphonucleosides to the monophosphonucleoside derivative.[4][5] For example, NTPDase1 hydrolyzes P2 receptor ligands, namely ATP, ADP, UTP and UDP with similar efficacy.[6] NTPDase1 can therefore affect P2 receptor activation and functions.[7]

See also

References

  1. ↑ "Entrez Gene: ENTPD1 Ectonucleoside triphosphate diphosphohydrolase 1".
  2. ↑ Sévigny J, Levesque FP, Grondin G, Beaudoin AR (Feb 1997). "Purification of the blood vessel ATP diphosphohydrolase, identification and localisation by immunological techniques". Biochimica et Biophysica Acta. 1334 (1): 73–88. doi:10.1016/s0304-4165(96)00079-7. PMID 9042368.
  3. ↑ Kaczmarek E, Koziak K, Sévigny J, Siegel JB, Anrather J, Beaudoin AR, Bach FH, Robson SC (Dec 1996). "Identification and characterization of CD39/vascular ATP diphosphohydrolase". The Journal of Biological Chemistry. 271 (51): 33116–22. doi:10.1074/jbc.271.51.33116. PMID 8955160.
  4. ↑ Robson SC, Sévigny J, Zimmermann H (Jun 2006). "The E-NTPDase family of ectonucleotidases: Structure function relationships and pathophysiological significance". Purinergic Signalling. 2 (2): 409–30. doi:10.1007/s11302-006-9003-5. PMC 2254478. PMID 18404480.
  5. ↑ Yegutkin GG (May 2008). "Nucleotide- and nucleoside-converting ectoenzymes: Important modulators of purinergic signalling cascade". Biochimica et Biophysica Acta. 1783 (5): 673–94. doi:10.1016/j.bbamcr.2008.01.024. PMID 18302942.
  6. ↑ Kukulski F, Lévesque SA, Lavoie EG, Lecka J, Bigonnesse F, Knowles AF, Robson SC, Kirley TL, Sévigny J (Jun 2005). "Comparative hydrolysis of P2 receptor agonists by NTPDases 1, 2, 3 and 8". Purinergic Signalling. 1 (2): 193–204. doi:10.1007/s11302-005-6217-x. PMC 2096530. PMID 18404504.
  7. ↑ Kukulski F, Lévesque SA, Sévigny J (2011-01-01). "Impact of ectoenzymes on p2 and p1 receptor signaling". Advances in Pharmacology. 61: 263–99. doi:10.1016/B978-0-12-385526-8.00009-6. PMID 21586362.

Further reading

  • Maliszewski CR, Delespesse GJ, Schoenborn MA, Armitage RJ, Fanslow WC, Nakajima T, Baker E, Sutherland GR, Poindexter K, Birks C (Oct 1994). "The CD39 lymphoid cell activation antigen. Molecular cloning and structural characterization". Journal of Immunology. 153 (8): 3574–83. PMID 7930580.
  • Christoforidis S, Papamarcaki T, Galaris D, Kellner R, Tsolas O (Nov 1995). "Purification and properties of human placental ATP diphosphohydrolase". European Journal of Biochemistry / FEBS. 234 (1): 66–74. doi:10.1111/j.1432-1033.1995.066_c.x. PMID 8529670.
  • Wang TF, Guidotti G (Apr 1996). "CD39 is an ecto-(Ca2+,Mg2+)-apyrase". The Journal of Biological Chemistry. 271 (17): 9898–901. doi:10.1074/jbc.271.17.9898. PMID 8626624.
  • Kaczmarek E, Koziak K, Sévigny J, Siegel JB, Anrather J, Beaudoin AR, Bach FH, Robson SC (Dec 1996). "Identification and characterization of CD39/vascular ATP diphosphohydrolase". The Journal of Biological Chemistry. 271 (51): 33116–22. doi:10.1074/jbc.271.51.33116. PMID 8955160.
  • Robson SC, Kaczmarek E, Siegel JB, Candinas D, Koziak K, Millan M, Hancock WW, Bach FH (Jan 1997). "Loss of ATP diphosphohydrolase activity with endothelial cell activation". The Journal of Experimental Medicine. 185 (1): 153–63. doi:10.1084/jem.185.1.153. PMC 2196106. PMID 8996251.
  • Gray IC, Fallowfield J, Ford S, Nobile C, Volpi EV, Spurr NK (Jul 1997). "An integrated physical and genetic map spanning chromosome band 10q24". Genomics. 43 (1): 85–8. doi:10.1006/geno.1997.4809. PMID 9226376.
  • Makita K, Shimoyama T, Sakurai Y, Yagi H, Matsumoto M, Narita N, Sakamoto Y, Saito S, Ikeda Y, Suzuki M, Titani K, Fujimura Y (Oct 1998). "Placental ecto-ATP diphosphohydrolase: its structural feature distinct from CD39, localization and inhibition on shear-induced platelet aggregation". International Journal of Hematology. 68 (3): 297–310. doi:10.1016/S0925-5710(98)00080-2. PMID 9846014.
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External links


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