NTPDase family in zebrafish: Nucleotide hydrolysis, molecular identification and gene expression profiles in brain, liver and heart

Rosemberg, Denis B.; Rico, Eduardo Pacheco; Langoni, Andrei Silveira; Spinelli, Jonathan Tesch; Pereira, Talita Carneiro Brandão; Dias, Renato Dutra; Souza, Diogo O.; Bonan, Carla Denise; Bogo, Maurı́cio Reis

doi:10.1016/j.cbpb.2009.11.005

Cited by 58 publications

(29 citation statements)

References 54 publications

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“…Homologues of the mammalian ecto-forms of the ENTPDase family are found in Xenopus [185] and zebrafish [186]. Interestingly, these enzymes are missing in the Drosophila and Caenorhabditis elegans genome.…”

Section: Phylogenetic Relationshipmentioning

confidence: 99%

Cellular function and molecular structure of ecto-nucleotidases

Zimmermann

Zebisch

Sträter

2012

Purinergic Signalling

891

922

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Ecto-nucleotidases play a pivotal role in purinergic signal transmission. They hydrolyze extracellular nucleotides and thus can control their availability at purinergic P2 receptors. They generate extracellular nucleosides for cellular reuptake and salvage via nucleoside transporters of the plasma membrane. The extracellular adenosine formed acts as an agonist of purinergic P1 receptors. They also can produce and hydrolyze extracellular inorganic pyrophosphate that is of major relevance in the control of bone mineralization. This review discusses and compares four major groups of ectonucleotidases: the ecto-nucleoside triphosphate diphosphohydrolases, ecto-5′-nucleotidase, ecto-nucleotide pyrophosphatase/phosphodiesterases, and alkaline phosphatases. Only recently and based on crystal structures, detailed information regarding the spatial structures and catalytic mechanisms has become available for members of these four ecto-nucleotidase families. This permits detailed predictions of their catalytic mechanisms and a comparison between the individual enzyme groups. The review focuses on the principal biochemical, cell biological, catalytic, and structural properties of the enzymes and provides brief reference to tissue distribution, and physiological and pathophysiological functions.

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Section: Phylogenetic Relationshipmentioning

confidence: 99%

Cellular function and molecular structure of ecto-nucleotidases

Zimmermann

Zebisch

Sträter

2012

Purinergic Signalling

891

922

View full text Add to dashboard Cite

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“…Each of the NTPDases had a distinct expression pattern during embryogenesis suggest-ing that they have different functions in this process [118]. Rosemberg et al [119] reported that the NTPDase7 gene is absent in zebrafish, while there are three NTPase2 and two NTPDase5 paralogs. Gene expression of the seven NTPDases in zebrafish brain, liver, and heart was analyzed by RT-PCR.…”

Section: Intracellular Ntpdasesmentioning

confidence: 99%

“…Thus, the contribution by the NTPDases could not be quantified. No effort was made to determine the protein expression of the seven NTPDases in the three zebrafish tissues [119].…”

Section: Intracellular Ntpdasesmentioning

confidence: 99%

The GDA1_CD39 superfamily: NTPDases with diverse functions

Knowles

2011

Purinergic Signalling

145

117

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The first comprehensive review of the ubiquitous "ecto-ATPases" by Plesner was published in 1995. A year later, a lymphoid cell activation antigen, CD39, that had been cloned previously, was shown to be an ecto-ATPase. A family of proteins, related to CD39 and a yeast GDPase, all containing the canonical apyrase conserved regions in their polypeptides, soon started to expand. They are now recognized as members of the GDA1_CD39 protein family. Because proteins in this family hydrolyze nucleoside triphosphates and diphosphates, a unifying nomenclature, nucleoside triphosphate diphopshohydrolases (NTPDases), was established in 2000. Membrane-bound NTPDases are either located on the cell surface or membranes of intracellular organelles. Soluble NTPDases exist in the cytosol and may be secreted. In the last 15 years, molecular cloning and functional expression have facilitated biochemical characterization of NTPDases of many organisms, culminating in the recent structural determination of the ecto-domain of a mammalian cell surface NTPDase and a bacterial NTPDase. The first goal of this review is to summarize the biochemical, mutagenesis, and structural studies of the NTPDases. Because of their ability in hydrolyzing extracellular nucleotides, the mammalian cell surface NTPDases (the ecto-NTPDases) which regulate purinergic signaling have received the most attention. Less appreciated are the functions of intracellular NTPDases and NTPDases of other organisms, e.g., bacteria, parasites, Drosophila, plants, etc. The second goal of this review is to summarize recent findings which demonstrate the involvement of the NTPDases in multiple and diverse physiological processes: pathogen-host interaction, plant growth, eukaryote cell protein and lipid glycosylation, eye development, and oncogenesis.

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“…Specific entpd1, entpd2, entpd2a.1, entpd2a.2, entpd3, nt5e, and ada1 primers were designed and used as described previously by our group [40][41][42]. The well known adenosine receptor sequences (ADORA) from human and mouse were used as queries to search homologous zebrafish protein-related sequences.…”

Section: Primer Design and Rt-pcr Experimentsmentioning

confidence: 99%

Acute Restraint Stress in Zebrafish: Behavioral Parameters and Purinergic Signaling

et al. 2011

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Despite the extensive knowledge about the effects of acute restraint stress (ARS) in rodents, zebrafish research is still elementary in this field, and the consequences of stress on purinergic system are unclear. Therefore, we evaluated the effects of ARS on behavior, biochemical, and molecular parameters in zebrafish brain. Animals were submitted to a 90 min ARS protocol and tested for anxiety levels, exploratory behavior, and memory performance. Furthermore, we analyzed ectonucleotidase and adenosine deaminase activities and their gene expression profile, as well as transcription of adenosine receptors. ARS increased anxiety, but did not impair locomotion or cognition. ARS significantly increased ATP hydrolysis, decreased cytosolic ADA activity, and changed the entpd and adora gene expression. In conclusion, ARS disturbed zebrafish behavior, and we hypothesize that the augmentation in adenosine-mediated signaling may be a strategy to reestablish homeostasis and normal behavior after a stressful event.

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NTPDase family in zebrafish: Nucleotide hydrolysis, molecular identification and gene expression profiles in brain, liver and heart

Cited by 58 publications

References 54 publications

Cellular function and molecular structure of ecto-nucleotidases

Cellular function and molecular structure of ecto-nucleotidases

The GDA1_CD39 superfamily: NTPDases with diverse functions

Acute Restraint Stress in Zebrafish: Behavioral Parameters and Purinergic Signaling

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