The Stability of Chicken Nucleoside Triphosphate Diphosphohydrolase 8 Requires Both of Its Transmembrane Domains

Biochemistry ◽  
2010 ◽  
Vol 49 (1) ◽  
pp. 134-146 ◽  
Author(s):  
Cheryl S. Li ◽  
Yonghee Lee ◽  
Aileen F. Knowles
Keyword(s):  
Transmembrane Domains ◽  
Nucleoside Triphosphate ◽  
Nucleoside Triphosphate Diphosphohydrolase ◽  
The Stability

scholarly journals NTPDase1 Modulates Smooth Muscle Contraction in Mice Bladder by Regulating Nucleotide Receptor Activation Distinctly in Male and Female

Biomolecules ◽  
2021 ◽  
Vol 11 (2) ◽  
pp. 147
Author(s):  
Romuald Brice Babou Kammoe ◽  
Gilles Kauffenstein ◽  
Julie Pelletier ◽  
Bernard Robaye ◽  
Jean Sévigny
Keyword(s):  
Smooth Muscle ◽  
Ex Vivo ◽  
Smooth Muscle Contraction ◽  
Receptor Activation ◽  
Nucleoside Triphosphate ◽  
Nucleotide Receptors ◽  
Nerve Terminals ◽  
Wild Type ◽  
Nucleoside Triphosphate Diphosphohydrolase ◽  
Bladder Contraction

Nucleotides released by smooth muscle cells (SMCs) and by innervating nerve terminals activate specific P2 receptors and modulate bladder contraction. We hypothesized that cell surface enzymes regulate SMC contraction in mice bladder by controlling the concentration of nucleotides. We showed by immunohistochemistry, enzymatic histochemistry, and biochemical activities that nucleoside triphosphate diphosphohydrolase-1 (NTPDase1) and ecto-5′-nucleotidase were the major ectonucleotidases expressed by SMCs in the bladder. RT-qPCR revealed that, among the nucleotide receptors, there was higher expression of P2X1, P2Y1, and P2Y6 receptors. Ex vivo, nucleotides induced a more potent contraction of bladder strips isolated from NTPDase1 deficient (Entpd1−/−) mice compared to wild type controls. The strongest responses were obtained with uridine 5′-triphosphate (UTP) and uridine 5′-diphosphate (UDP), suggesting the involvement of P2Y6 receptors, which was confirmed with P2ry6−/− bladder strips. Interestingly, this response was reduced in female bladders. Our results also suggest the participation of P2X1, P2Y2 and/or P2Y4, and P2Y12 in these contractions. A reduced response to the thromboxane analogue U46619 was also observed in wild type, Entpd1−/−, and P2ry6−/− female bladders showing another difference due to sex. In summary, NTPDase1 modulates the activation of nucleotide receptors in mouse bladder SMCs, and contractions induced by P2Y6 receptor activation were weaker in female bladders.

scholarly journals Role of Ca2+ in Mediating Plant Responses to Extracellular ATP and ADP

2018 ◽  
Vol 19 (11) ◽  
pp. 3590 ◽  
Author(s):  
Greg Clark ◽  
Stanley Roux
Keyword(s):  
Cytosolic Calcium ◽  
Defense Responses ◽  
Receptor Activation ◽  
Extracellular Atp ◽  
Extracellular Nucleotides ◽  
Nucleoside Triphosphate ◽  
Plant Responses ◽  
Downstream Signaling ◽  
Nucleoside Triphosphate Diphosphohydrolase

Among the most recently discovered chemical regulators of plant growth and development are extracellular nucleotides, especially extracellular ATP (eATP) and extracellular ADP (eADP). Plant cells release ATP into their extracellular matrix under a variety of different circumstances, and this eATP can then function as an agonist that binds to a specific receptor and induces signaling changes, the earliest of which is an increase in the concentration of cytosolic calcium ([Ca2+]cyt). This initial change is then amplified into downstream-signaling changes that include increased levels of reactive oxygen species and nitric oxide, which ultimately lead to major changes in the growth rate, defense responses, and leaf stomatal apertures of plants. This review presents and discusses the evidence that links receptor activation to increased [Ca2+]cyt and, ultimately, to growth and diverse adaptive changes in plant development. It also discusses the evidence that increased [Ca2+]cyt also enhances the activity of apyrase (nucleoside triphosphate diphosphohydrolase) enzymes that function in multiple subcellular locales to hydrolyze ATP and ADP, and thus limit or terminate the effects of these potent regulators.

Leishmania infantum amastigote nucleoside triphosphate diphosphohydrolase 1 (NTPDase 1): Its inhibition as a new insight into mode of action of pentamidine

2019 ◽  
Vol 200 ◽  
pp. 1-6 ◽  
Author(s):  
Ana Carolina Ribeiro Gomes Maia ◽  
Gabriane Nascimento Porcino ◽  
Michelle Lima Detoni ◽  
Leonardo Ramos Quellis ◽  
Nayara Braga Emídio ◽  
...  
Keyword(s):  
Mode Of Action ◽  
Leishmania Infantum ◽  
Nucleoside Triphosphate ◽  
Nucleoside Triphosphate Diphosphohydrolase ◽  
Insight Into

scholarly journals Label-free assay based on immobilized capillary enzyme reactor of Leishmania infantum nucleoside triphosphate diphosphohydrolase ( Lic NTPDase-2-ICER-LC/UV)

2016 ◽  
Vol 1008 ◽  
pp. 98-107 ◽  
Author(s):  
Luana Magalhães ◽  
Arthur Henrique Cavalcante de Oliveira ◽  
Raphael de Souza Vasconcellos ◽  
Christiane Mariotini-Moura ◽  
Rafaela de Cássia Firmino ◽  
...  
Keyword(s):  
Leishmania Infantum ◽  
Nucleoside Triphosphate ◽  
Label Free ◽  
Enzyme Reactor ◽  
Nucleoside Triphosphate Diphosphohydrolase
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