NDLI: Functional analysis of expression of human ecto-nucleoside triphosphate diphosphohydrolase-1 and/or ecto-5'-nucleotidase in pig endothelial cells.

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Immunohistochemical and functional analysis of ectonucleoside triphosphate diphosphohydrolase 1 (CD39) and ecto-5'-nucleotidase (CD73) in pig aortic valves.

Functional analysis of expression of human ecto-nucleoside triphosphate diphosphohydrolase-1 and/or ecto-5'-nucleotidase in pig endothelial cells.

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Functional analysis of expression of human ecto-nucleoside triphosphate diphosphohydrolase-1 and/or ecto-5'-nucleotidase in pig endothelial cells.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	De Giorgi, M. Pelikant-Malecka, I. Sielicka, A. Slominska, E. M. Giovannoni, R. Cinti, A. Cerrito, M. G. Lavitrano, M. Smolenski, R. T.
Description	Country affiliation: Italy Author Affiliation: De Giorgi M ( a Department of Surgery and Translational Medicine , University of Milano-Bicocca , Milano , Italy.)
Abstract	Adenine nucleosides and nucleotides are important signaling molecules involved in control of key mechanisms of xenotransplant rejection. Extracellular pathway that converts ATP and ADP to AMP, and AMP to adenosine mainly mediated by ecto-nucleoside triphosphate diphosphohydrolase 1, (ENTPD1 or CD39) and ecto-5'-nucleotidase (E5NT or CD73) respectively, is considered as important target for xenograft protection. To clarify feasibility of combined expression of human ENTPD1 and E5NT and to study its functional effect we transfected pig endothelial cell line (PIEC) with both genes together. To do this we have produced a dicistronic construct bearing F2A sequence in frame between human E5NT and human ENTPD1 coding sequences. PIEC cells were mock-transfected as transfection control or transfected with plasmids encoding human ENTPD1 or human E5NT. PIEC cells were exposed to 50 µM ATP or 50 µM ADP or 50 µM AMP. Conversion of extracellular substrates into products (ATP/ADP/AMP/adenosine) was measured by HPLC in the media collected at specific time intervals. Following addition of AMP, production of adenosine in the medium of E5NT/ENTPD1- and E5NT- transfected cells increased to 14.2±1.1 and 24.5±3.4 µM respectively while it remained below 1 µM in controls and in ENTPD1-transfected cells. A marked increase of adenosine formation from ADP or ATP was observed only in E5NT/ENTPD1-transfected cells (11.7±0.1 and 5.7±2.2 µM respectively) but not in any other condition studied. This study indicates feasibility and functionality of combined expression of human E5NT and ENTPD1 in pig endothelial cells using F2A sequence bearing construct.
File Format	HTM / HTML
ISSN	15257770
Issue Number	4-6
Volume Number	33
e-ISSN	15322335
Journal	Nucleosides, Nucleotides and Nucleic Acids
Language	English
Publisher	Taylor & Francis
Publisher Date	2014-01-01
Publisher Place	United States
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Discipline Biochemistry 5'-nucleotidase Genetics Metabolism Antigens, Cd Apyrase Endothelial Cells Enzyme Assays Methods Adenine Nucleotides Adenosine Animals Gene Expression Humans Swine Transfection Journal Article Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Genetics Medicine Biochemistry Molecular Medicine

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Immunohistochemical and functional analysis of ectonucleoside triphosphate diphosphohydrolase 1 (CD39) and ecto-5'-nucleotidase (CD73) in pig aortic valves.

Expression and Characterization of Soluble and Membrane-bound Human Nucleoside Triphosphate Diphosphohydrolase 6 (CD39L2)

Ecto-nucleoside triphosphate diphosphohydrolase 1 (E-NTPDase1/CD39) regulates neutrophil chemotaxis by hydrolyzing released ATP to adenosine.

Enzymes that hydrolyze adenine nucleotides in lymphocytes and platelets of immunosuppressed rats.

Extracellular ATP Selectively Upregulates Ecto-Nucleoside Triphosphate Diphosphohydrolase 2 and Ecto-5′-Nucleotidase by Rat Cortical Astrocytes In Vitro

Specificity of the ecto-ATPase inhibitor ARL 67156 on human and mouse ectonucleotidases

Conserved lysine 79 is important for activity of ecto-nucleoside triphosphate diphosphohydrolase 3 (NTPDase3)

The structure of the nucleoside triphosphate diphosphohydrolases (NTPDases) as revealed by mutagenic and computational modeling analyses

Activities of enzymes that hydrolyze adenine nucleotides in lymphocytes from patients with rheumatoid arthritis.

Functional analysis of expression of human ecto-nucleoside triphosphate diphosphohydrolase-1 and/or ecto-5'-nucleotidase in pig endothelial cells.

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Functional analysis of expression of human ecto-nucleoside triphosphate diphosphohydrolase-1 and/or ecto-5'-nucleotidase in pig endothelial cells.