scholarly journals Adenylate kinase 1 overexpression increases locomotor activity in medaka fish

PLoS ONE ◽  
2022 ◽  
Vol 17 (1) ◽  
pp. e0257967
Author(s):  
Michiyo Maruyama ◽  
Yuko Furukawa ◽  
Masato Kinoshita ◽  
Atsushi Mukaiyama ◽  
Shuji Akiyama ◽  
...  
Keyword(s):  
Locomotor Activity ◽  
Energy Balance ◽  
Adenylate Kinase ◽  
Adenine Nucleotide ◽  
Energy Regulation ◽  
Medaka Fish ◽  
Temperature Dependent ◽  
Cellular Energy ◽  
And Function ◽  
Adenylate Kinase 1

Maintenance of the energy balance is indispensable for cell survival and function. Adenylate kinase (Ak) is a ubiquitous enzyme highly conserved among many organisms. Ak plays an essential role in energy regulation by maintaining adenine nucleotide homeostasis in cells. However, its role at the whole organism level, especially in animal behavior, remains unclear. Here, we established a model using medaka fish (Oryzias latipes) to examine the function of Ak in environmental adaptation. Medaka overexpressing the major Ak isoform Ak1 exhibited increased locomotor activity compared to that of the wild type. Interestingly, this increase was temperature dependent. Our findings suggest that cellular energy balance can modulate locomotor activity.

scholarly journals Adenylate kinase 1 overexpression increases locomotor activity in medaka fish

2021 ◽  
Author(s):  
Michiyo Maruyama ◽  
Yuko Furukawa ◽  
Masato Kinoshita ◽  
Atsushi Mukaiyama ◽  
Shuji Akiyama ◽  
...  
Keyword(s):  
Locomotor Activity ◽  
Energy Balance ◽  
Adenylate Kinase ◽  
Adenine Nucleotide ◽  
Energy Regulation ◽  
Medaka Fish ◽  
Temperature Dependent ◽  
Cellular Energy ◽  
And Function ◽  
Adenylate Kinase 1

Maintenance of the energy balance is indispensable for cell survival and function. Adenylate kinase (Ak) is a ubiquitous enzyme highly conserved among many organisms. Ak plays an essential role in energy regulation by maintaining adenine nucleotide homeostasis in cells. However, its role at the whole organism level, especially in animal behavior, remains unclear. Here, we established a model using medaka fish (Oryzias latipes) to examine the function of Ak in environmental adaptation. Medaka overexpressing the major Ak isoform Ak1 exhibited increased locomotor activity compared to that of the wild type. Interestingly, this increase was temperature dependent. Our findings suggest that cellular energy balance can modulate locomotor activity.

scholarly journals Purine-Metabolizing Ectoenzymes Control IL-8 Production in Human Colon HT-29 Cells

2014 ◽  
Vol 2014 ◽  
pp. 1-10 ◽  
Author(s):  
Fariborz Bahrami ◽  
Filip Kukulski ◽  
Joanna Lecka ◽  
Alain Tremblay ◽  
Julie Pelletier ◽  
...  
Keyword(s):  
Adenylate Kinase ◽  
Adenine Nucleotide ◽  
Inflammatory Diseases ◽  
Cancer Cell Line ◽  
Human Colon ◽  
Nucleotide Metabolism ◽  
Poly I:C ◽  
Intestinal Epithelial ◽  
And Function ◽  
Ht 29

Interleukin-8 (IL-8) plays key roles in both chronic inflammatory diseases and tumor modulation. We previously observed that IL-8 secretion and function can be modulated by nucleotide (P2) receptors. Here we investigated whether IL-8 release by intestinal epithelial HT-29 cells, a cancer cell line, is modulated by extracellular nucleotide metabolism. We first identified that HT-29 cells regulated adenosine and adenine nucleotide concentration at their surface by the expression of the ectoenzymes NTPDase2, ecto-5′-nucleotidase, and adenylate kinase. The expression of the ectoenzymes was evaluated by RT-PCR, qPCR, and immunoblotting, and their activity was analyzed by RP-HPLC of the products and by detection ofPiproduced from the hydrolysis of ATP, ADP, and AMP. In response to poly (I:C), with or without ATP and/or ADP, HT-29 cells released IL-8 and this secretion was modulated by the presence of NTPDase2 and adenylate kinase. Taken together, these results demonstrate the presence of 3 ectoenzymes at the surface of HT-29 cells that control nucleotide levels and adenosine production (NTPDase2, ecto-5′-nucleotidase and adenylate kinase) and that P2 receptor-mediated signaling controls IL-8 release in HT-29 cells which is modulated by the presence of NTPDase2 and adenylate kinase.

scholarly journals Subtle Role for Adenylate Kinase 1 in Maintaining Normal Basal Contractile Function and Metabolism in the Murine Heart

2021 ◽  
Vol 12 ◽  
Author(s):  
Sevasti Zervou ◽  
Debra J. McAndrew ◽  
Hannah J. Whittington ◽  
Hannah A. Lake ◽  
Kyung Chan Park ◽  
...  
Keyword(s):  
Functional Recovery ◽  
Adenylate Kinase ◽  
Citrate Synthase ◽  
Contractile Function ◽  
Adenine Nucleotide ◽  
Ex Vivo ◽  
Adenine Nucleotides ◽  
Contractile Reserve ◽  
Adenylate Kinase 1

AimsAdenylate kinase 1 (AK1) catalyses the reaction 2ADP ↔ ATP + AMP, extracting extra energy under metabolic stress and promoting energetic homeostasis. We hypothesised that increased AK1 activity would have negligible effects at rest, but protect against ischaemia/reperfusion (I/R) injury.Methods and ResultsCardiac-specific AK1 overexpressing mice (AK1-OE) had 31% higher AK1 activity (P = 0.009), with unchanged total creatine kinase and citrate synthase activities. Male AK1-OE exhibited mild in vivo dysfunction at baseline with lower LV pressure, impaired relaxation, and contractile reserve. LV weight was 19% higher in AK1-OE males due to higher tissue water content in the absence of hypertrophy or fibrosis. AK1-OE hearts had significantly raised creatine, unaltered total adenine nucleotides, and 20% higher AMP levels (P = 0.05), but AMP-activated protein kinase was not activated (P = 0.85). 1H-NMR revealed significant differences in LV metabolite levels compared to wild-type, with aspartate, tyrosine, sphingomyelin, cholesterol all elevated, whereas taurine and triglycerides were significantly lower. Ex vivo global no-flow I/R, caused four-of-seven AK1-OE hearts to develop terminal arrhythmia (cf. zero WT), yet surviving AK1-OE hearts had improved functional recovery. However, AK1-OE did not influence infarct size in vivo and arrhythmias were only observed ex vivo, probably as an artefact of adenine nucleotide loss during cannulation.ConclusionModest elevation of AK1 may improve functional recovery following I/R, but has unexpected impact on LV weight, function and metabolite levels under basal resting conditions, suggesting a more nuanced role for AK1 underpinning myocardial energy homeostasis and not just as a response to stress.

Structure of contact sites between the outer and inner mitochondrial membranes investigated by HVEM tomography

1996 ◽  
Vol 54 ◽  
pp. 966-967
Author(s):  
C.A. Mannella ◽  
K.F. Buttle ◽  
K.A. O‘Farrell ◽  
A. Leith ◽  
M. Marko
Keyword(s):  
Liver Mitochondrion ◽  
Adenine Nucleotide ◽  
Protein Complexes ◽  
Mitochondrial Membranes ◽  
Electron Microscopic ◽  
Contact Sites ◽  
Transmission Electron ◽  
Precursor Proteins ◽  
Membrane Contacts ◽  
And Function

Early transmission electron microscopy of plastic-embedded, thin-sectioned mitochondria indicated that there are numerous junctions between the outer and inner membranes of this organelle. More recent studies have suggested that the mitochondrial membrane contacts may be the site of protein complexes engaged in specialized functions, e.g., import of mitochondrial precursor proteins, adenine nucleotide channeling, and even intermembrane signalling. It has been suggested that the intermembrane contacts may be sites of membrane fusion involving non-bilayer lipid domains in the two membranes. However, despite growing interest in the nature and function of intramitochondrial contact sites, little is known about their structure.We are using electron microscopic tomography with the Albany HVEM to determine the internal organization of mitochondria. We have reconstructed a 0.6-μm section through an isolated, plasticembedded rat-liver mitochondrion by combining 123 projections collected by tilting (+/- 70°) around two perpendicular tilt axes. The resulting 3-D image has confirmed the basic inner-membrane organization inferred from lower-resolution reconstructions obtained from single-axis tomography.

P1, P5-Bis-(5′-adenosyl)pentaphosphate: Is this Adenylate Kinase Inhibitor Substrate for Mitochondrial Processes?

1977 ◽  
Vol 32 (9-10) ◽  
pp. 786-791 ◽  
Author(s):  
Josef Köhrle ◽  
Joachim Lüstorff ◽  
Eckhard Schlimme
Keyword(s):  
Adenylate Kinase ◽  
Kinase Inhibitor ◽  
Adenine Nucleotide ◽  
Nucleoside Diphosphate Kinase ◽  
Liver Mitochondria ◽  
Inhibitory Effect ◽  
Rat Liver Mitochondria ◽  
Intermembrane Space ◽  
Rabbit Muscle ◽  
Inner Mitochondrial Membrane

Abstract 1. P1, P5-Bis-(5′-adenosyl)pentaphosphate (Ap5A) inhibits “soluble” adenylate kinase even when this enzyme is an integral part of the complete mitochondrion. The Ki is 10-5м , i. e. about two orders of magnitude higher than the inhibitor constants determined for the purified adenylate kinase of rabbit muscle and an enzyme preparation separated from the mitochondrial intermembrane space. The weaker inhibitory effect is due to a lower accessibility of the enzyme.2. As to be expected Ap5A which is of the “multisubstrate analogue”-type does not affect mito­ chondrial nucleoside diphosphate kinase.3. Though Ap5A owns the structural elements of both ATP and ADP it is not a substrate of the adenine nucleotide carrier, i.e. neither it is exchanged across the inner mitochondrial membrane nor specifically bound.4. Ap5A is not metabolized by rat liver mitochondria.

Immunization with recombinant schistosome adenylate kinase 1 partially protects mice against Schistosoma japonicum infection

2017 ◽  
Vol 116 (6) ◽  
pp. 1665-1674 ◽  
Author(s):  
Yanru Gao ◽  
Xiaoshan Zhou ◽  
Huan Wang ◽  
Rong Liu ◽  
Qing Ye ◽  
...  
Keyword(s):  
Schistosoma Japonicum ◽  
Adenylate Kinase ◽  
Adenylate Kinase 1

PMR4-dependent cell wall depositions are a consequence but not the cause of temperature-induced autoimmunity

2021 ◽  
Author(s):  
Giuliana Hessler ◽  
Stephan Michael Portheine ◽  
Eva-Maria Gerlach ◽  
Tim Lienemann ◽  
Gerald Koch ◽  
...  
Keyword(s):  
Cell Wall ◽  
Immune System ◽  
Severe Damage ◽  
Temperature Dependent ◽  
Callose Synthase ◽  
Ambient Temperatures ◽  
Point Of No Return ◽  
Dependent Cell ◽  
And Function ◽  
Reduced Temperature

Abstract Plants possess a well-balanced immune system that is required for defense against pathogen infections. In autoimmune mutants or necrotic crosses, an intrinsic temperature-dependent imbalance leads to constitutive immune activation, resulting in severe damage or even death of plants. Recently, cell wall depositions were described as one of the symptoms following induction of the autoimmune phenotype in Arabidopsis saul1-1 mutants. However, the regulation and function of these depositions remained unclear. Here, we show that cell wall depositions, containing lignin and callose, were a common autoimmune feature and were deposited in proportion to the severity of the autoimmune phenotype at reduced ambient temperatures. When plants were exposed to reduced temperature for periods insufficient to induce an autoimmune phenotype, the cell wall depositions were not present. After low temperature intervals, sufficient to induce autoimmune responses, cell wall depositions correlated with a point of no return in saul1-1 autoimmunity. Although cell wall depositions were largely abolished in saul1-1 pmr4-1 double mutants lacking SAUL1 and the callose synthase gene GSL5/PMR4, their phenotype remained unchanged compared to that of the saul1-1 single mutant. Our data showed that cell wall depositions generally occur in autoimmunity, but appear not to be the cause of autoimmune phenotypes.

scholarly journals Amylin/Calcitonin Receptor–Mediated Signaling in POMC Neurons Influences Energy Balance and Locomotor Activity in Chow-Fed Male Mice

Diabetes ◽  
2020 ◽  
Vol 69 (6) ◽  
pp. 1110-1125 ◽  
Author(s):  
Bernd Coester ◽  
Christina Koester-Hegmann ◽  
Thomas A. Lutz ◽  
Christelle Le Foll
Keyword(s):  
Locomotor Activity ◽  
Energy Balance ◽  
Calcitonin Receptor ◽  
Male Mice

scholarly journals Synphilin-1 Interacts with AMPK and Increases AMPK Phosphorylation

2020 ◽  
Vol 21 (12) ◽  
pp. 4352 ◽  
Author(s):  
Tianxia Li ◽  
Jingnan Liu ◽  
Gongbo Guo ◽  
Bo Ning ◽  
Xueping Li ◽  
...  
Keyword(s):  
Energy Balance ◽  
Cultured Cells ◽  
Energy Status ◽  
Glutathione S Transferase ◽  
Cellular Functions ◽  
Ampk Signaling ◽  
Cellular Energy ◽  
Downstream Signaling ◽  
Compound C ◽  
Ampk Phosphorylation

A role for the cytoplasmic protein synphilin-1 in regulating energy balance has been demonstrated recently. Expression of synphilin-1 increases ATP levels in cultured cells. However, the mechanism by which synphilin-1 alters cellular energy status is unknown. Here, we used cell models and biochemical approaches to investigate the cellular functions of synphilin-1 on the AMP-activated protein kinase (AMPK) signaling pathway, which may affect energy balance. Overexpression of synphilin-1 increased AMPK phosphorylation (activation). Moreover, synphilin-1 interacted with AMPK by co-immunoprecipitation and GST (glutathione S-transferase) pull-down assays. Knockdown of synphilin-1 reduced AMPK phosphorylation. Overexpression of synphilin-1 also altered AMPK downstream signaling, i.e., a decrease in acetyl CoA carboxylase (ACC) phosphorylation, and an increase in p70S6K phosphorylation. Treatment of compound C (an AMPK inhibitor) reduced synphilin-1 binding with AMPK. In addition, compound C diminished synphilin-1-induced AMPK phosphorylation, and the increase in cellular ATP (adenosine triphosphate) levels. Our results demonstrated that synphilin-1 couples with AMPK, and they exert mutual effects on each other to regulate cellular energy status. These findings not only identify novel cellular actions of synphilin-1, but also provide new insights into the roles of synphilin-1 in regulating energy currency, ATP.

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