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evolution
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CG5276 belongs to another family of calcium-activated nucleotidases. CG5276 may represent an apyrase related to calcium-activated nucleotidases
evolution
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GS52 is a member of the NTPDase/apyrase family
evolution
the capy gene is most likely an ancestral feature that has been lost from most apicomplexan genomes except Cryptosporidium, Neospora and Toxoplasma
evolution
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the enzyme is a member of the E-NTPDase family
evolution
the enzyme is a member of the eukaryotic NTPDase family
evolution
nucleoside triphosphate diphosphohydrolases (NTPDases) belong to the GDA1/CD39 protein superfamily, E-NTPDase family. Existence of several isoforms with different specificities with respect to divalent cations (magnesium, calcium, manganese, and zinc) and substrates
evolution
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the enzyme belongs to the APY gene family
evolution
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the enzyme belongs to the NTPDase family
evolution
the seven member Arabidopsis apyrase family contains representatives in each clade and are clustered into the AtAPY1-2 clade I (GDA1-like), the AtAPY3-6 (clade II) and AtAPY7 in clade III. Isozymes AtAPY3, AtAPY4, and AtAPY5 occur as recurrent tandem duplications and share 68% identity, all three are expressed during Arabidopsis thaliana development with AtAPY3 predominately in the roots and both AtAPY4/AtAPY5 in the vegetative rosette. The protein structure of the seven Arabidopsis apyrase proteins outline the apyrase conserved domain GDA1_CD39 and predicted transmembrane helices
evolution
the seven member Arabidopsis apyrase family contains representatives in each clade and are clustered into the AtAPY1-2 clade I (GDA1-like), the AtAPY3-6 (clade II) and AtAPY7 in clade III. The clade I (GDA-like) Arabidopsis members (AtAPY1 andAtAPY2) form a distinct clade with the other characterized plant apyrases, human apyrases and the yeast GDA1 enzyme. The protein structure of the seven Arabidopsis apyrase proteins outline the apyrase conserved domain GDA1_CD39 and predicted transmembrane helices
evolution
the seven member Arabidopsis apyrase family contains representatives in each clade and are clustered into the AtAPY1-2 clade I (GDA1-like), the AtAPY3-6 (clade II) and AtAPY7 in clade III. The protein structure of the seven Arabidopsis apyrase proteins outline the apyrase conserved domain GDA1_CD39 and predicted transmembrane helices
malfunction
a soluble truncated mutant NTPDase8, lacking the extracellular domain, shows 85% reduced activity compared to the full-length membrane-bound enzyme. Also activity of the soluble chicken NTPDase8 decreases with time in a temperature-dependent manner as a result of inactivation by ATP, ADP, and phosphate, in contrast to the wild-type full-length enzyme
malfunction
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suppression of apyrase expression affects the regulation of stomatal aperture
malfunction
the inactivated, functionally disrupted enzyme is not active in stimulating nodulation
malfunction
downregulation of NTPDase3 expression in MIN-6 cells inhibits extracellular ATP hydrolysis and insulin secretion
malfunction
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single knockout mutants of isoforms APY6 and 7 display a minor change in pollen exine pattern without obvious change in fertility, while double knockout mutants of APY6 and 7 display severe defects in pollen exine pattern, deformed pollen shape and reduced male fertility
malfunction
the excessive levels of extracellular ATP in the enzyme knockout animals desensitize the P2X receptors associated with nerve fibers, thereby depressing taste responses
malfunction
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the suppression of isoforms APY1 and APY2 blocks growth in Arabidopsis thaliana. The basal halves of apyrase-suppressed hypocotyls contain considerably lower free indole-3-acetic acid levels when compared with wild type plants, and disrupted auxin transport in the apyrase-suppressed roots is reflected by their significant morphological abnormalities, such as unusual root hair distribution and meristematic disorganization. A critical step connecting apyrase suppression to growth suppression is the inhibition of polar auxin transport
malfunction
apy2 single knockout roots show increased skewing compared with wild-type roots when grown on phytagel
malfunction
immunochemical and genetic suppression of AtAPY1 and AtAPY2 results in an increase in extracellular ATP
malfunction
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infection with bovine herpesvirus type 5 (BoHV-5) strain SV-507/99 leads to a decrease in ectonucleotidase activity in synaptosomes from the cerebral cortex of infected rabbits, whereas an increased ectonucleotidase activity in synaptosomes from the hippocampus is observed. On day 7 p.i., NTPDase activity (ATP and ADP hydrolysis) are decreased in synaptosomes from the cerebral cortex of rabbits infected with BoHV-5 in relation to the control group. BoHV-5 replication results in changes in ectonucleotidase activity in the brain, which may contribute to the neurological signs commonly observed in the disease herpetic meningoencephalitis
malfunction
the primary roots of seedlings overexpressing APY1 show less skewing than wild-type plants. Plants suppressed in their expression of APY1 show more skewing than wild-type plants. The primary roots of apy1 single knockout (APY1 KO) seedlings (Ws background) exhibit increased rightward skewing and have an HGI that is significantly higher than that of wild-type roots. The apy1 single knockout roots show increased skewing compared with wild-type roots when grown on phytagel. Treatment of R2-4A seedlings with estradiol induces 70% suppression of APY1 expression in the null background of APY2 and results in shortened roots with swollen root tips. Apy1 mutant roots show altered cell file rotation. Phenotypes, overview
malfunction
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under cold stress, PeAPY2-overexpressing transgenic plants maintain plasma membrane integrity and show reduced cold-elicited electrolyte leakage compared with wild-type plants. These responses probably result from efficient plasma membrane repair via vesicular trafficking. Transgenic plants show accelerated endocytosis and exocytosis during cold stress and recovery. Low doses of extracellular ATP accelerate vesicular trafficking, but high extracellular ATP inhibit trafficking and reduce cell viability. Cold stress causes significant increases in root medium extracellular ATP. Under these conditions, PeAPY2-overexpressing transgenic lines show greater control of extracellular ATP levels than wild-type plants
metabolism
plasma membrane-bound NTPDases, namely NTPDase1/CD39, NTPDase2/CD39L1, and NTPDase8, represent the major liver ectonucleotidase activities
metabolism
roles of the Arabidopsis thaliana apyrase family in regulating endomembrane NDP/NMP homoeostasis, overview. The AtAPY1-6 Arabidopsis thaliana enzymes all exhibit classic apyrase-like NTPase and/or NDPases activities, with an absence of NMP activity
metabolism
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plasma membrane-bound NTPDases, namely NTPDase1/CD39, NTPDase2/CD39L1, and NTPDase8, represent the major liver ectonucleotidase activities
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physiological function
apyrase plays a role in growth and development of tissues, for example, lateral roots
physiological function
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ectoapyrase and extracellular nucleotides play a significant role in regulating cotton fiber growth
physiological function
the recombinant protein inhibits ADP- and collagen-induced platelet aggregation. Thus, this salivary protein plays an important role in the blood-feeding process in Phlebotomus duboscqi
physiological function
antibodies directed against CApy block Cryptosporidium parvum sporozoite invasion of HCT-8 cells
physiological function
apyrases can inhibit platelet activation by depletion of adenosine diphosphate
physiological function
ecto-apyrase is an extracellular nucleoside triphosphate diphosphohydrolase that modulates the nucleotide concentration in the extracellular matrix. Ecto-apyrase controls the concentration of extracellular nucleotides. GS52 activity stimulates root nodulation, the inactivated enzyme is not effective
physiological function
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ecto-nucleoside triphosphate diphosphohydrolases, E-NTPDases, regulate the concentration of extracellular nucleotides, signaling molecules that play a role in the pathogenesis of hepatic fibrosis. Up-regulation of Entpd3 mRNA expression modulates the extracellular concentration of nucleotides/nucleosides and affect P2-receptor signaling differently in quiescent-like cells and may play a role in the regulation of hepatic stellate cell functions
physiological function
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expression of the two apyrase isozymes in Arabidopsis thaliana, APY1 and APY2, is strongly correlated with cell growth and secretory activity. Ectoapyrases and extracellular nucleotides play key roles in regulating stomatal functions, overview
physiological function
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important role for the Glycine max ecto-apyrase GS52 in rhizobial root hair infection and root nodule formation
physiological function
nucleoside triphosphate diphosphohydrolases are a physiologically important class of membrane-bound ectonucleotidases responsible for the regulation of extracellular levels of nucleotides
physiological function
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unlike NT5E-1, NT5E-2 seems to play a specific role in male reproduction since it is expressed more strongly in males than in females and is expressed specifically in testis
physiological function
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apyrase enzyme blocks abscisic acid-induced stomatal closure
physiological function
isoform APY1 exerts its growth and developmental effects by possibly regulating glycosylation reactions in the Golgi
physiological function
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isoforms APY6 and AtAPY7 play an important role in exine development of pollen grains, possibly through regulating the production of key polysaccharides needed for proper assembly of the exine layer
physiological function
pharmacological inhibition by ARL 67156 or gene silencing of the endogenous ecto-nucleoside triphosphate diphosphohydrolase isoform 2 results in a 25% reduction in both ATP hydrolysis and ADP formation. NTPDase2 hydrolyzes ATP and generates sustainable ADP levels. Knocking down NTPDase2 potentiates the nanomolar ATP-induced intracellular calcium increase
physiological function
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the basal halves of apyrase-suppressed hypocotyls contain considerably lower free indole-3-acetic acid levels when compared with wild type plants, and disrupted auxin transport in the apyrase-suppressed roots is reflected by their significant morphological abnormalities, such as unusual root hair distribution and meristematic disorganization
physiological function
the enzyme blocks platelet aggregation and supports blood flow
physiological function
the enzyme modulates insulin secretion by controlling activation of purinergic receptors
physiological function
the enzyme modulates insulin secretion by controlling activation of purinergic receptors
physiological function
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apyrase and extracellular ATP play crucial roles in mediating plant growth and defense responses. Cold stress causes significant increases in root medium extracellular ATP
physiological function
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apyrase decreases microglial ramification and surveillance. Applying the ATPase apyrase, an enzyme which hydrolyzes ATP and ADP, reduces microglial process ramification and surveillance in acutely prepared postnatal day (P)12 rat hippocampal slices, suggesting that ambient ATP/ADP maintains microglial surveillance. But attempting to raise the level of ATP/ADP by blocking the endogenous ecto-ATPase (termed NTPDase1/CD39), which also hydrolyzes ATP/ADP, does not affect the cells' ramification or surveillance, nor their membrane currents, which respond to even small rises of extracellular [ATP] or [ADP] with the activation of K+ channels. This indicates a lack of detectable ambient ATP/ADP and ecto-ATPase activity, contradicting the results with apyrase. Contamination of commercially available apyrase by a high K+ concentration reduces ramification and surveillance by depolarizing microglia. Exposure to the same K+ concentration (without apyrase added) reduced ramification and surveillance as with apyrase. Dialysis of apyrase to remove K+ retains its ATP-hydrolyzing activity but abolishes the microglial depolarization and decrease of ramification produced by the undialyzed enzyme. Microglia are very sensitive to increases of extracellular ATP concentration, to which they respond by activating P2Y12 receptor-gated THIK-1 K+ channels, generating an outward K+ current which leads to a hyperpolarization of their membrane
physiological function
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apyrases, which directly regulate intra- and extracellular ATP homeostasis, play a pivotal role in the regulation of various stress adaptations in mammals, bacteria and plants
physiological function
biochemical analysis of AtAPY4 results in the lowest NDPase activates measured, exhibiting a substrate preference for CTP. But even with this reduced NDPase activity, the isozyme's localization to the Golgi lumen probably assists in the positive complementation phenotype in Saccharomyces cerevisiae DELTAgda1DELTAynd1 dKO. The Arabidopsis apyrases family members have possible roles in regulating endomembrane NDP/NMP (nucleoside monophosphate) homoeostasis
physiological function
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BjAPY2 is closely associated with the expansion of stems but not of leaves in the tuber mustard. Cloning and analysis of the promoter region of BjAPY2 reveal that there are several types of motifs in the promoter region, including the light and temperature responsive elements suggesting that BjAPY2 might play an important role during the stem expansion of the tuber mustard
physiological function
both AtAPY1 and AtAPY2 have been shown to play numerous physiological roles in pollen development, vegetative growth and stomata opening/closure. AtAPY1 and AtAPY2 function as plant endo-apyrases and are necessary for lumenal glycosylation. The Arabidopsis apyrases family members have possible roles in regulating endomembrane NDP/NMP (nucleoside monophosphate) homoeostasis. AtAPY 1 and AtAPY2 are able to function as internal Golgi lumenal NDPases
physiological function
differential effect of apyrase treatment and hCD39 overexpression on chronic renal fibrosis after ischemia-reperfusion injury (IRI), overview. Hydrolysis of ATP to adenosine diphosphate (ADP) by the ectonucleotidase CD39 (ENTPDase1) is an important step in reducing the proinflammatory effects of ATP CD39 also hydrolyses ADP to adenosine monophosphate (AMP), which is subsequently converted to adenosine by CD73 (5' ectonucleotidase). Augmenting CD39 activity is a potential therapy to improve both short- and long-term outcomes of IRI by reducing the extracellular concentration of proinflammatory ATP and promoting adenosine generation. hCD39 transgene expression in CD39Tg mice (C57BL/6 wild-type expressing human CD39) reduces ischemia-induced acute renal injury, but exacerbates chronic renal injury. Apyrase does not modify baseline ATP, ADP, AMP, adenosine or inosine levels, but reduces ATP, ADP, and AMP levels during ischemia. Apyrase attenuates the increase in A2BR mRNA levels at week 4 post-IRI
physiological function
ecto-nucleoside triphosphate diphosphohydrolase1 (NTPDase1, CD39) is a major ectonucleotidase that hydrolyzes proinflammatory ATP via ADP to AMP, which is subsequently converted by ecto-5'-nucleotidase (CD73) to immunosuppressive adenosine
physiological function
ectoapyrases (ect-NTPDases) function to decrease levels of extracellular ATP and ADP in animals and plants. Ectopic expression of a pea ectoapyrase, psNTP9, enhances growth in Arabidopsis thaliana seedlings and the overexpression of the two Arabidopsis apyrases most closely related to psNTP9 enhances auxin transport and growth in Arabidopsis thaliana. Ectopic expression of psNTP9 can promote a more extensive root system architecture (RSA) in Arabidopsis thaliana. Transgenic Arabidopsis thaliana seedlings have longer primary roots, more lateral roots, and more and longer root hairs than wild-type plants. Transcriptomic analyses reveal gene expression changes in the transgenic plants that help account for their enhanced RSA and improved drought tolerance
physiological function
ectoapyrases (ecto-NTPDases) function to decrease levels of extracellular ATP and ADP in animals and plants. Ectopic expression of a pea ectoapyrase, psNTP9, enhances growth in Arabidopsis thaliana seedlings and the overexpression of the two Arabidopsis apyrases most closely related to psNTP9 enhances auxin transport and growth in Arabidopsis thaliana. Ectopic expression of psNTP9 can promote a more extensive root system architecture (RSA) in Arabidopsis thaliana. Transgenic Arabidopsis thaliana seedlings have longer primary roots, more lateral roots, and more and longer root hairs than wild-type plants. Transcriptomic analyses reveal gene expression changes in the transgenic plants that help account for their enhanced RSA and improved drought tolerance
physiological function
ectoapyrases (ecto-NTPDases) function to decrease levels of extracellular ATP and ADP in animals and plants. Ectopic expression of a pea ectoapyrase, psNTP9, enhances growth in Arabidopsis thaliana seedlings. Ectopic expression of psNTP9 can promote a more extensive root system architecture (RSA) in Arabidopsis thaliana. Transgenic Arabidopsis thaliana seedlings have longer primary roots, more lateral roots, and more and longer root hairs than wild-type plants. Transgenic Glycine max plants show improved RSA, growth and seed yield, and supports higher survival in response to drought
physiological function
isozyme AtAPY6 is able to complement the growth defect phenotype of the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant, demonstrating that the enzyme is also able to function as internal Golgi lumenal NDPases. Analysis of atapy6 mutants indicate a minor role in pollen development associated with abnormal exine patterning. An endoapyrase role for AtAPY6. The Arabidopsis apyrases family members have possible roles in regulating endomembrane NDP/NMP (nucleoside monophosphate) homoeostasis
physiological function
modulation of root skewing in Arabidopsis thaliana by apyrases and extracellular ATP. Skewing is induced by touch stimuli which the roots experience as they grow along the surface. Touch stimuli also induce the release of extracellular ATP (eATP) into the plant's extracellular matrix, and two apyrases (NTPDases) in Arabidopsis thaliana, APY1 and APY2, can help regulate the concentration of eATP. Exogenous application of ATP or ATPgammaS also increases skewing in wild-type roots, which can be blocked by co-incubation with a purinergic receptor antagonist. APY1 and, to a lesser extent, APY2 help control root skewing in Arabidopsis thaliana, and application of extracellular nucleotides also affects this directional growth response of roots. Treatment with ATP and ATPgammaS increases root skewing. Blocking auxin transport with 1-N-naphthylphthalamic acid (NPA) also increases root skewing
physiological function
mosquitoes infected by sporozoites, the infectious stage of malaria, bite more frequently than uninfected mosquitoes. One of the mechanisms underlying this behavioural change appears to be that the sporozoites decrease the activity of apyrase, an ADP-degrading enzyme that helps the mosquitoes to locate blood. Using the parasite Plasmodium berghei and the mosquito Anopheles gambiae, it is confirmed that sporozoite infection alters the hostseeking behaviour of mosquitoes by making them more likely to refeed after a first blood meal, and that apyrase activity is one of the mechanisms of the increased biting persistence and motivation of infectious mosquitoes. Apyrase activity decreases as the sporozoite load increases, and mosquitoes with lower apyrase activity take up less blood
physiological function
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occlusion of vein grafts (VGs) after bypass surgery due to thrombosis and intimal hyperplasia (IH) is a major clinical problem. Apyrases are enzymes that scavenge extracellular ATP and ADP and promote adenosine formation at sites of vascular injury and hence have potential to inhibit vein graft pathology. Recombinant soluble apyrase APT102 inhibits thrombosis and intimal hyperplasia in vein grafts without adversely affecting hemostasis or re-endothelialization. Effects of recombinant soluble human apyrase, APT102, on platelets, smooth muscle cells (SMCs), and endothelial cells (ECs) in vitro and thrombosis and IH in murine VGs from C57BL/6J male mice, overview. While potently inhibiting ADP-induced platelet aggregation and VG thrombosis, APT102 does not impair surgical hemostasis. APT102 does not directly inhibit SMC or EC proliferation, but significantly attenuates the effects of ATP on SMC and EC proliferation. APT102 significantly inhibits SMC migration, but does not inhibit EC migration, which may be mediated, at least in part, by inhibition of SMC, but not EC, migration by adenosine. At 4 weeks after surgery, IH is significantly less in VGs of APT102-treated mice than in control VGs. APT102 significantly inhibit cell proliferation in VGs, but does not inhibit re-endothelialization
physiological function
the Arabidopsis apyrases family members have possible roles in regulating endomembrane NDP/NMP (nucleoside monophosphate) homoeostasis
physiological function
Arabidopsis thaliana ecotype Columbia, CS907
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ectoapyrases (ecto-NTPDases) function to decrease levels of extracellular ATP and ADP in animals and plants. Ectopic expression of a pea ectoapyrase, psNTP9, enhances growth in Arabidopsis thaliana seedlings and the overexpression of the two Arabidopsis apyrases most closely related to psNTP9 enhances auxin transport and growth in Arabidopsis thaliana. Ectopic expression of psNTP9 can promote a more extensive root system architecture (RSA) in Arabidopsis thaliana. Transgenic Arabidopsis thaliana seedlings have longer primary roots, more lateral roots, and more and longer root hairs than wild-type plants. Transcriptomic analyses reveal gene expression changes in the transgenic plants that help account for their enhanced RSA and improved drought tolerance
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physiological function
Arabidopsis thaliana ecotype Columbia, CS907
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ectoapyrases (ect-NTPDases) function to decrease levels of extracellular ATP and ADP in animals and plants. Ectopic expression of a pea ectoapyrase, psNTP9, enhances growth in Arabidopsis thaliana seedlings and the overexpression of the two Arabidopsis apyrases most closely related to psNTP9 enhances auxin transport and growth in Arabidopsis thaliana. Ectopic expression of psNTP9 can promote a more extensive root system architecture (RSA) in Arabidopsis thaliana. Transgenic Arabidopsis thaliana seedlings have longer primary roots, more lateral roots, and more and longer root hairs than wild-type plants. Transcriptomic analyses reveal gene expression changes in the transgenic plants that help account for their enhanced RSA and improved drought tolerance
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additional information
influence of transmembrane helix dynamics on activity is achieved by coupling to a domain motion. Active site structure of NTPDase1, overview, closure movement in NTPDases
additional information
immune sera that recognize specifically the B domain of NTPDase 1 are produced against synthetic peptides (LbB1LJ (residues 82-103, RERFKRIEPGLSSFATDQEGAK) and LbB2LJ (residues 102-121, AKQSLAGLLRFAEKAVPRSY) synthetic peptides belong to the N- and C-terminal portions, respectively) derived from this domain. The polyclonal antibodies have effective anti-leishmanial effect, reducing significantly in vitro promastigotes growth (21-25%), an antiproliferative effect is also demonstrated by immune sera produced against recombinant r-pot B domain, and two other synthetic peptides (potB1LJ and potB2LJ). In addition, using these biomolecules in ELISA technique, IgG1 and IgG2 subclasses reactivities of either healthy dogs or infected by Leishmania infantum and classified clinically as asymptomatic, oligosymptomatic and symptomatic are tested. The peptides have have high identity with their Leishmnia infantum NTPDase 1 counterparts. Analysis of distinct IgG1 and IgG2 seropositivities patterns suggest antibody subclasses binding epitopes along B domain for protection against infection, indicating this domain as a tool for prophylactic and immunotherapeutic investigations
additional information
immune sera that recognize specifically the B domain of NTPDase 1 are produced against synthetic peptides (LbB1LJ and LbB2LJ) derived from this domain. The polyclonal antibodies have effective anti-leishmanial effect, reducing significantly in vitro promastigotes growth (21-25%), an antiproliferative effect is also demonstrated by immune sera produced against recombinant r-pot B domain, and two other synthetic peptides (potB1LJ and potB2LJ). The LbB1LJ (residues 82-103, RERFKRIEPGLSSFATDQEGAK) and LbB2LJ (residues 102-121, AKQSLAGLLRFAEKAVPRSY) synthetic peptides belong to the N- and C-terminal portions, respectively, from conserved B domain (82-121) of Leishmania braziliensis NTPDase 1 (UniProt ID A4H7X3), and have high identity with their Leishmnia infantum NTPDase 1 counterparts. In addition, using these biomolecules in ELISA technique, IgG1 and IgG2 subclasses reactivities of either healthy dogs or infected by Leishmania infantum and classified clinically as asymptomatic, oligosymptomatic and symptomatic are tested. Analysis of distinct IgG1 and IgG2 seropositivities patterns suggest antibody subclasses binding epitopes along B domain for protection against infection, indicating this domain as a tool for prophylactic and immunotherapeutic investigations
additional information
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the transcript abundance of seven intrinsic Arabidopsis apyrase genes, AtAPY1, AtAPY2, AtAPY3, AtAPY4, AtAPY5, AtAPY6, and AtAPY7, is not altered by the overexpression of exogenous PeAPY2
additional information
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immune sera that recognize specifically the B domain of NTPDase 1 are produced against synthetic peptides (LbB1LJ and LbB2LJ) derived from this domain. The polyclonal antibodies have effective anti-leishmanial effect, reducing significantly in vitro promastigotes growth (21-25%), an antiproliferative effect is also demonstrated by immune sera produced against recombinant r-pot B domain, and two other synthetic peptides (potB1LJ and potB2LJ). The LbB1LJ (residues 82-103, RERFKRIEPGLSSFATDQEGAK) and LbB2LJ (residues 102-121, AKQSLAGLLRFAEKAVPRSY) synthetic peptides belong to the N- and C-terminal portions, respectively, from conserved B domain (82-121) of Leishmania braziliensis NTPDase 1 (UniProt ID A4H7X3), and have high identity with their Leishmnia infantum NTPDase 1 counterparts. In addition, using these biomolecules in ELISA technique, IgG1 and IgG2 subclasses reactivities of either healthy dogs or infected by Leishmania infantum and classified clinically as asymptomatic, oligosymptomatic and symptomatic are tested. Analysis of distinct IgG1 and IgG2 seropositivities patterns suggest antibody subclasses binding epitopes along B domain for protection against infection, indicating this domain as a tool for prophylactic and immunotherapeutic investigations
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