Apyrase from pea stems: Isolation, purification, characterization and identification of a NTPase from the cytoskeleton fraction of pea stem tissue

Shibata, Koichi; Morita, Yae; Abe, Shunnosuke; Stanković, Bratislav; Davies, Eric

doi:10.1016/s0981-9428(99)00102-3

Cited by 38 publications

(46 citation statements)

References 26 publications

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“…The model considered above assumes that MT is suppressed by apyrase (ATP diphosphohydralase), providing ATP and UTP hydrolysis to yield di-and monophosphonucleosides [46]. However, we failed to detect any significant action of 2 U/ml apyrase on MT of pressurized mesenteric arteries (data not shown).…”

Section: Discussionmentioning

confidence: 72%

Myogenic tone in mouse mesenteric arteries: evidence for P2Y receptor-mediated, Na+, K+, 2Cl− cotransport-dependent signaling

Кольцова

Maximov

Kotelevtsev

et al. 2009

Purinergic Signalling

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This study examines the action of agonists and antagonists of P2 receptors on mouse mesenteric artery contractions and the possible involvement of these signaling pathways in myogenic tone (MT) evoked by elevated intraluminal pressure. Both ATP and its non-hydrolyzed analog α,β-ATP triggered transient contractions that were sharply decreased in the presence of NF023, a potent antagonist of P2X 1 receptors. In contrast, UTP and UDP elicited sustained contractions which were suppressed by MRS2567, a selective antagonist of P2Y 6 receptors. Inhibition of Na + , K + , 2Cl − cotransport (NKCC) with bumetanide led to attenuation of contractions in UTP-but not ATPtreated arteries. Both UTP-induced contractions and MT were suppressed by MRS2567 and bumetanide but were insensitive to NF023. These data implicate a P2Y 6 -mediated, NKCC-dependent mechanism in MT of mesenteric arteries. The action of heightened intraluminal pressure on UTP release from mesenteric arteries and its role in the triggering of P2Y 6 -mediated signaling should be examined further.

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Section: Discussionmentioning

confidence: 72%

Myogenic tone in mouse mesenteric arteries: evidence for P2Y receptor-mediated, Na+, K+, 2Cl− cotransport-dependent signaling

Кольцова

Maximov

Kotelevtsev

et al. 2009

Purinergic Signalling

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“…We describe morphological and physiological characteristics, and gene expression pattern in rth1 mutant. We revealed that RTH1 encodes an enzyme apyrase that can hydrolyze NTPs and/or diphosphates (Shibata et al 1999) and that apyrase is a key gene for root hair elongation and plant growth in rice. …”

Section: Introductionmentioning

confidence: 99%

Molecular cloning of a root hairless gene rth1 in rice

et al. 2009

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Root hairs, projections from the epidermal cells of the roots, are contributing to water and nutrient uptake and anchorage to the soil. To better understand genetic control of root hair formation in rice, we analyzed root hairless 1 (rth1) mutant that was induced by NaN 3 treatment. SEM observation showed that in rth1 plants, root hair elongation was abolished after the formation of bulge. High-resolution mapping using 2,088 segregants revealed three predicted genes in a 38-kb candidate interval on chromosome 7. Sequences comparison of the three genes between wild-type Oochikara and rth1 detected a nucleotide substitution only in apyrase (OsAPY). This nucleotide substitution (G → A) lies in the junction between the third intron and the forth exon, and results in the splicing anomaly to the rth1 cDNA sequence. Transgenic plants with introduced OsAPY allele restored normal root hairs and plant growth, showing a complementation of rth1 phenotype. We concluded that the root hairless phenotype of rth1 is caused by a mutation of OsAPY. OsAPY appears to be an important gene for root hair elongation and plant growth in rice.

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“…3.6.1.5) is an enzyme which hydrolyzes ATP and ADP along with other nucleoside tri-and/or di-phosphates into monophosphates, by a one-step reaction (Shibata et al 1999). It is widely distributed in both animal and plant tissues and can be classified as an endo-apyrase or ecto-apyrase based on the localization and biochemical characteristics (Plesner 1995;Komoszynski & Wojtczak 1996).…”

Section: Introductionmentioning

confidence: 99%

“…In plants, this enzyme has been characterized from potato (Solanum tuberosum; Kalckar 1944;Molnar & Lorand 1961;Kettlun et al 1982), and various legumes, such as Glycine max (soya; Day et al 2000), Medicago truncatula (barrel medic; Cohn et al 2001), and Pisum sativum (pea; Hsieh et al 2000). It has been identified from various plant tissues and has multiple cellular locations, such as the cytoskeleton (Shibata et al 1999), filamentous structures associated with ribosomes, nuclei (Shibata et al 2002), chromatin (Matsumoto et al 1984), nuclear membrane (Tong et al 1993), the outer surface of the cytoplasmic membrane, the cell wall (Thomas et al 1999) and in the Golgi (Dunkley et al 2004;Chiu et al 2012;Parsons et al 2012;Schiller et al 2012). These findings suggest that apyrase in plants may be involved in diverse functions and signalling inside and outside the cells.…”

Section: Introductionmentioning

confidence: 99%

“…NTP/dNTP pools are important in the cells undergoing division where transcription, gene duplication, and assembly/disassembly of the cytoskeleton proteins occur. In another experiment, PsAPY1, an endo-apyrase protein, was isolated from the pea nuclei and cytoskeleton, and was hypothesized to play a role in cytoskeleton associated mRNA transport, cytoskeleton-based cellular metabolism and cytoskeleton-related signal transduction and transportation (Shibata et al 1999(Shibata et al , 2002. It was shown that PsAPY1 was localized in the cell wall, the nucleus, and around the filamentous structures in the cytoplasm of 5-day-old pea seedlings.…”

Section: Introductionmentioning

confidence: 99%

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Expression pattern of PsAPY1 during apical hook development in pea

2014

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Apyrase (ATP diphosphohydrolase, EC 3.6.1.5) catalyzes hydrolysis of nucleoside tri-and di-phosphates to nucleoside monophosphates and orthophosphates. In the present study, the spatio-temporal expression of an apyrase gene (PsAPY1) in pea (Pisum sativum L. var. Alaska), was investigated during early stages of apical hook development using nonradioactive mRNA in-situ hybridization. During the formation of apical hook; at 45 hours after sowing (HAS), expression of PsAPY1 was obvious in epidermis and vascular bundle. By 60 HAS, the apical hook was completely formed. At this stage, transcript accumulation became higher than at the previous stage and expression was also visible in the cortex tissues of the developing hook. However, at 78 HAS, the curvature of the hook was reduced and hook was in the process of opening. At this time, expression of PsAPY1 was visible in all the above-mentioned tissues although the level of expression was slightly lower than at the previous stage (60 HAS). Apical hook formation provides a unique mechanism of protection for delicate shoot meristem in dicot plants. Its establishment is orchestrated by differential elongation rates of cells within the structure. The expression pattern of a gene provides essential information concerning the likely appearance and localization of its encoded protein and this helps to understand the mechanism of development of plant cells and tissues. Higher expression of PsAPY1 during the process of hook development indicates its essential role in the process of formation and maintenance of hook curvature and thus aids in protection of delicate shoot meristem.

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Apyrase from pea stems: Isolation, purification, characterization and identification of a NTPase from the cytoskeleton fraction of pea stem tissue

Cited by 38 publications

References 26 publications

Myogenic tone in mouse mesenteric arteries: evidence for P2Y receptor-mediated, Na+, K+, 2Cl− cotransport-dependent signaling

Myogenic tone in mouse mesenteric arteries: evidence for P2Y receptor-mediated, Na+, K+, 2Cl− cotransport-dependent signaling

Molecular cloning of a root hairless gene rth1 in rice

Expression pattern of PsAPY1 during apical hook development in pea

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