DEGRADATION OF ADENINE NUCLEOTIDES IN THE MUSCLE OF THE DUNGENESS CRAB (CANCER MAGISTER) AND KING CRAB (PARALITHODES CAMTSCHATICA) DURING STORAGE AND COOKING

1969 ◽  
Vol 32 (1) ◽  
pp. 1-3 ◽  
Author(s):  
H. S. Groninger ◽  
K. R. Brandt
Keyword(s):  
Adenine Nucleotide ◽  
Adenine Nucleotides ◽  
Adenosine Monophosphate ◽  
Adenosine Diphosphate ◽  
Heat Processing ◽  
Minor Role ◽  
Dungeness Crab ◽  
Cancer Magister ◽  
King Crab ◽  
Before And After

The adenine nucleotide content of king and Dungeness crab was determined on muscle before and after storage and on heat-processed or cooked crab meat. As a result of both storage and heat processing, adenosine triphosphate (ATP) and adenosine diphosphate (ADP) are degraded to adenosine monophosphate (AMP) and inosine and hypoxanthine. Only small amounts of inosine monophosphate (IMP) are found in cooked crabmeat. Flavor evaluation of IMP-treated king crab showed that IMP plays only a minor role in the flavor of crab.

scholarly journals Studies on Human Erythrocyte Nucleotide Metabolism. II. Nonspherocytic Hemolytic Anemia, High Red Cell ATP, and Ribosephosphate Pyrophosphokinase (RPK, E.C. 2.7.6.1) Deficiency

Blood ◽  
1972 ◽  
Vol 39 (5) ◽  
pp. 674-684 ◽  
Author(s):  
William N. Valentine ◽  
Helen M. Anderson ◽  
Donald E. Paglia ◽  
Ernst R. Jaffé ◽  
Patricia N. Konrad ◽  
...  
Keyword(s):  
Hemolytic Anemia ◽  
Reduced Glutathione ◽  
Adenine Nucleotides ◽  
Adenosine Monophosphate ◽  
Adenosine Diphosphate ◽  
Blood Film ◽  
Nucleotide Metabolism ◽  
Glutathione Metabolism ◽  
Final Decision ◽  
Blood Samples

Abstract A 29-yr-old black woman was found to have a long-standing, nonspherocytic hemolytic disorder associated with a marked reduction in the activity of erythrocyte ribosephosphate pyrophosphokinase (RPK, PRPP synthetase, E.C. 2.7.6.1). Although the patient’s erythrocytes had about 50% of the average RPK activity of normal mature human erythrocytes, this level represented only about 20-30% of the activity in comparable reticulocyte-rich blood samples from patients with other types of hemolytic anemias. The concentrations of adenosine triphosphate adenosine diphosphate, adenosine monophosphate and, therefore, of total adenine nucleotides in her erythrocytes were markedly increased, even well above the levels in extracts of comparable reticulocyte-rich blood samples. ATPase activity was increased three- to fourfold, consistent with the reticulocytosis. Adenylate kinase and adenine phosphoribosyltransferase activities were normal. The activities of all enzymes of the Embden-Meyerhof and hexose monophosphate shunt pathways and enzymes related to glutathione metabolism were normal or increased, consistent with the reticulocytosis. The concentrations of glycolytic intermediates, other than adenine nucleotides, were normal. The conversion of glucose, adenosine, and inosine to lactate was normal or increased. Autohemolysis was of the Dacie Type II. The concentrations of erythrocyte-reduced glutathione were high normal or elevated. The stained blood film showed a striking degree of basophilic stippling of the erythrocytes. Studies of the erythrocytes of the patient’s only known relative, a son, have failed to reveal any hematologic or enzymatic abnormalities. A direct causal relationship between RPK deficiency, high ATP concentrations, and nonspherocytic hemolytic anemia could not be derived from data now available. The final decision as to whether the deficiency is primary and causative or is an epiphenomenon requires investigation of additional cases.

scholarly journals Acquired granular pool defect in stored platelets

Blood ◽  
1981 ◽  
Vol 57 (2) ◽  
pp. 203-208
Author(s):  
AK Rao ◽  
S Niewiarowski ◽  
S Murphy
Keyword(s):  
Adenine Nucleotide ◽  
Adenine Nucleotides ◽  
Energy Charge ◽  
Adenylate Energy Charge ◽  
Platelet Factor ◽  
Final Volume ◽  
Before And After ◽  
Functional Defect ◽  
Metabolic Pool ◽  
The Mean

Platelets stored as concentrates (PC) for 72 h at 22 degrees C develop a functional defect. Alterations in adenine nucleotides of platelets have been shown to affect platelet function. Adenine nucleotide content of platelets was measured before and after storage and a decrease of 27.1 /+- 1.7% (mean /+- SE) in ATP and 39.1 /+- 2.6% in ADP were found in 34 PC stored with final volume of 50 ml. In 11 PC with 30 ml volume. ATP and ADP decreased by 39.4 /+- 3.2% and 49.4 /+- 2.1%, respectively. The mean ATP to ADP ratio of stored platelets was significantly higher than of fresh platelets in both groups, suggesting a relatively greater decrease in granular than metabolic pool nucleotides. Levels of low affinity platelet factor 4 measured by radioimmunoassay in plasma from 0.86 /+- 0.08 microgram/ml in the fresh PC to 8.59 /+- 0.39 microgram/ml in stored PC, indicating a concomitant alpha-granular secretion. Labeling of metabolic pool with 14C-adenine revealed a mean decrease in the adenylate energy charge of 2.0 /+- 0.4% in 12 of 16 stored PC, with a lower ATP and higher hypoxanthine labeling in stored as compared to fresh platelets. These observations suggest that stored platelets develop an acquired defect in both dense and alpha granules and in their ability to maintain ATP homeostasis.

Adenine Nucleotides in Platelets from Normal and Uraemic Subjects

1968 ◽  
Vol 19 (01/02) ◽  
pp. 036-040 ◽  
Author(s):  
W. R Pitney ◽  
H Hinterberger ◽  
M Potter
Keyword(s):  
Glass Bead ◽  
Adenine Nucleotide ◽  
Adenine Nucleotides ◽  
Blood Samples ◽  
Nucleotide Content ◽  
Before And After

SummaryAdenine nucleotides in platelets from normal and uraemic subjects were measured before and after passage of blood through glass bead filters. Platelets from uraemic subjects contained normal amounts of ATP, ADP, AMP and total nucleotides. Normal platelets which had passed through filters contained higher concentrations of ATP, ADP and total nucleotides than platelets in control blood samples, indicating either heterogeneity of adenine nucleotide content in normal platelets or possibly adsorption of nucleotides onto platelets during their passage through the filters. This phenomenon was not observed with platelets from uraemic patients.

scholarly journals Amelioration of Energy Metabolism by Melatonin in Skeletal Muscle of Rats With LPS Induced Endotoxemia

2016 ◽  
pp. 833-842 ◽  
Author(s):  
E. OZKOK ◽  
H. YORULMAZ ◽  
G. ATES ◽  
A. AKSU ◽  
N. BALKIS ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Energy Metabolism ◽  
Muscle Tissue ◽  
High Performance ◽  
Succinic Dehydrogenase ◽  
Adenosine Monophosphate ◽  
Adenosine Diphosphate ◽  
Creatine Phosphate ◽  
Before And After ◽  
Hematoxylin And Eosin

In the literature, few studies have investigated the effects of melatonin on energy metabolism in skeletal muscle in endotoxemia. We investigated the effects of melatonin on tissue structure, energy metabolism in skeletal muscle, and antioxidant level of rats with endotoxemia. We divided rats into 4 groups, control, lipopolysaccharide (LPS) (20 mg/kg, i.p., single dose), melatonin (10 mg/kg, i.p., three times), and melatonin + LPS. Melatonin was injected i.p. 30 min before and after the 2nd and 4th hours of LPS injection. Antioxidant status was determined by glutathione (GSH) measurement in the blood. Muscle tissue was stained using modified Gomori trichrome (MGT), succinic dehydrogenase (SDH), and cytochrome oxidase (COX) and histological scored. Also the sections were then stained with hematoxylin and eosin. The stained sections were visualized and photographed. Creatine, creatine phosphate, adenosine triphosphate (ATP), adenosine diphosphate (ADP), and adenosine monophosphate (AMP) levels were investigated using high performance liquid chromatography (HPLC) in muscle tissue. In the Melatonin + LPS group, blood GSH levels were increased compared with the LPS group (P<0.01). Melatonin reduced myopathic changes in the LPS group according to the histopathologic findings. In addition, ATP values were increased compared with the LPS group (P<0.05). Our findings showed melatonin treatment prevented muscle damage by increasing ATP and GSH levels in rats with LPS induced endotoxemia.

Studies on the Mechanism whereby Platelets are Clumped by Adenosine Diphosphate

1966 ◽  
Vol 15 (01/02) ◽  
pp. 036-051 ◽  
Author(s):  
Th. H Spaet ◽  
Ilze Lejnieks
Keyword(s):  
Energy Source ◽  
Divalent Cation ◽  
Platelet Rich Plasma ◽  
Adenine Nucleotides ◽  
Adenosine Monophosphate ◽  
Adenosine Diphosphate ◽  
Red Cells ◽  
Binding Reaction ◽  
Platelet Poor Plasma ◽  
Suitable Medium

SummaryThe effect of platelets on C14-labeled adenosine diphosphate (ADP) was studied. It was found that :1. A small amount of radioactive ADP in platelet-rich plasma became irreversibly bound to platelets, but on extraction radioactivity was found as a conversion mixture of adenine nucleotides resembling that in the platelet pool. Red cells showed similar binding and conversion, but only platelets were clumped by ADP. Nucleotides with little or no clumping activity (ATP, AMP and adenosine) bound to platelets and red cells in a manner similar to that of ADP, and they also yielded similar intracellular conversion products.2. Platelet-poor plasma converted ADP into adenosine monophosphate (AMP), but this activity was destroyed at 56° C in 10 minutes. Heated, platelet- poor plasma was a suitable medium for washing and suspending platelets in these studies.3. Platelets washed and suspended in heated plasma were clumped by ADP and produced ADP-dephosphorylation only in the presence of divalent cation. Red cells showed no ability to dephosphorylate ADP in this system.4. Platelets washed in saline or studied in the presence of excess AMP were not clumped by ADP nor did they yield ADP-dephosphorylation. Benadryl inhibited platelet clumping, but was without effect on ADP-dephosphorylation.It is suggested that ADP clumps platelets by serving as an energy source to activate a binding reaction as yet unidentified.

In the absence of phosphate shuttling, exercise reveals the in vivo importance of creatine-independent mitochondrial ADP transport

2016 ◽  
Vol 473 (18) ◽  
pp. 2831-2843 ◽  
Author(s):  
Paula M. Miotto ◽  
Graham P. Holloway
Keyword(s):  
Energy Homeostasis ◽  
Adenine Nucleotide ◽  
Control Point ◽  
Anion Channel ◽  
Adenosine Monophosphate ◽  
Adenosine Diphosphate ◽  
Glycolytic Flux ◽  
Voltage Dependent Anion Channel ◽  
Voltage Dependent

The transport of cytosolic adenosine diphosphate (ADP) into the mitochondria is a major control point in metabolic homeostasis, as ADP concentrations directly affect glycolytic flux and oxidative phosphorylation rates within mitochondria. A large contributor to the efficiency of this process is thought to involve phosphocreatine (PCr)/Creatine (Cr) shuttling through mitochondrial creatine kinase (Mi-CK), whereas the biological importance of alterations in Cr-independent ADP transport during exercise remains unknown. Therefore, we utilized an Mi-CK knockout (KO) model to determine whether in vivo Cr-independent mechanisms are biologically important for sustaining energy homeostasis during exercise. Ablating Mi-CK did not alter exercise tolerance, as the time to volitional fatigue was similar between wild-type (WT) and KO mice at various exercise intensities. In addition, skeletal muscle metabolic profiles after exercise, including glycogen, PCr/Cr ratios, free ADP/adenosine monophosphate (AMP), and lactate, were similar between genotypes. While these data suggest that the absence of PCr/Cr shuttling is not detrimental to maintaining energy homeostasis during exercise, KO mice displayed a dramatic increase in Cr-independent mitochondrial ADP sensitivity after exercise. Specifically, whereas mitochondrial ADP sensitivity decreased with exercise in WT mice, in stark contrast, exercise increased mitochondrial Cr-independent ADP sensitivity in KO mice. As a result, the apparent ADP Km was 50% lower in KO mice after exercise, suggesting that in vivo activation of voltage-dependent anion channel (VDAC)/adenine nucleotide translocase (ANT) can support mitochondrial ADP transport. Altogether, we provide insight that Cr-independent ADP transport mechanisms are biologically important for regulating ADP sensitivity during exercise, while highlighting complex regulation and the plasticity of the VDAC/ANT axis to support adenosine triphosphate demand.

scholarly journals Structure and Physiological Regulation of AMPK

2018 ◽  
Vol 19 (11) ◽  
pp. 3534 ◽  
Author(s):  
Yan Yan ◽  
X. Zhou ◽  
H. Xu ◽  
Karsten Melcher
Keyword(s):  
Energy Homeostasis ◽  
Adenine Nucleotide ◽  
Energy State ◽  
Adenine Nucleotides ◽  
Adenosine Monophosphate ◽  
Nucleotide Binding ◽  
Kinase Domain ◽  
Catabolic Pathways ◽  
Α Subunit ◽  
Ampk Activity

Adenosine monophosphate (AMP)-activated protein kinase (AMPK) is a heterotrimeric αβγ complex that functions as a central regulator of energy homeostasis. Energy stress manifests as a drop in the ratio of adenosine triphosphate (ATP) to AMP/ADP, which activates AMPK’s kinase activity, allowing it to upregulate ATP-generating catabolic pathways and to reduce energy-consuming catabolic pathways and cellular programs. AMPK senses the cellular energy state by competitive binding of the three adenine nucleotides AMP, ADP, and ATP to three sites in its γ subunit, each, which in turn modulates the activity of AMPK’s kinase domain in its α subunit. Our current understanding of adenine nucleotide binding and the mechanisms by which differential adenine nucleotide occupancies activate or inhibit AMPK activity has been largely informed by crystal structures of AMPK in different activity states. Here we provide an overview of AMPK structures, and how these structures, in combination with biochemical, biophysical, and mutational analyses provide insights into the mechanisms of adenine nucleotide binding and AMPK activity modulation.

scholarly journals Acquired granular pool defect in stored platelets

Blood ◽  
1981 ◽  
Vol 57 (2) ◽  
pp. 203-208 ◽  
Author(s):  
AK Rao ◽  
S Niewiarowski ◽  
S Murphy
Keyword(s):  
Adenine Nucleotide ◽  
Adenine Nucleotides ◽  
Energy Charge ◽  
Adenylate Energy Charge ◽  
Platelet Factor ◽  
Final Volume ◽  
Before And After ◽  
Functional Defect ◽  
Metabolic Pool ◽  
The Mean

Abstract Platelets stored as concentrates (PC) for 72 h at 22 degrees C develop a functional defect. Alterations in adenine nucleotides of platelets have been shown to affect platelet function. Adenine nucleotide content of platelets was measured before and after storage and a decrease of 27.1 /+- 1.7% (mean /+- SE) in ATP and 39.1 /+- 2.6% in ADP were found in 34 PC stored with final volume of 50 ml. In 11 PC with 30 ml volume. ATP and ADP decreased by 39.4 /+- 3.2% and 49.4 /+- 2.1%, respectively. The mean ATP to ADP ratio of stored platelets was significantly higher than of fresh platelets in both groups, suggesting a relatively greater decrease in granular than metabolic pool nucleotides. Levels of low affinity platelet factor 4 measured by radioimmunoassay in plasma from 0.86 /+- 0.08 microgram/ml in the fresh PC to 8.59 /+- 0.39 microgram/ml in stored PC, indicating a concomitant alpha-granular secretion. Labeling of metabolic pool with 14C-adenine revealed a mean decrease in the adenylate energy charge of 2.0 /+- 0.4% in 12 of 16 stored PC, with a lower ATP and higher hypoxanthine labeling in stored as compared to fresh platelets. These observations suggest that stored platelets develop an acquired defect in both dense and alpha granules and in their ability to maintain ATP homeostasis.

scholarly journals CFAP45 deficiency causes situs abnormalities and asthenospermia by disrupting an axonemal adenine nucleotide homeostasis module

2020 ◽  
Vol 11 (1) ◽  
Author(s):  
Gerard W. Dougherty ◽  
Katsutoshi Mizuno ◽  
Tabea Nöthe-Menchen ◽  
Yayoi Ikawa ◽  
Karsten Boldt ◽  
...  
Keyword(s):  
Atp Hydrolysis ◽  
Adenine Nucleotide ◽  
Adenosine Monophosphate ◽  
Adenosine Diphosphate ◽  
Situs Inversus Totalis ◽  
Proteomic Profiling ◽  
Binding Interface ◽  
Axonemal Dynein ◽  
Cilia And Flagella

Abstract Axonemal dynein ATPases direct ciliary and flagellar beating via adenosine triphosphate (ATP) hydrolysis. The modulatory effect of adenosine monophosphate (AMP) and adenosine diphosphate (ADP) on flagellar beating is not fully understood. Here, we describe a deficiency of cilia and flagella associated protein 45 (CFAP45) in humans and mice that presents a motile ciliopathy featuring situs inversus totalis and asthenospermia. CFAP45-deficient cilia and flagella show normal morphology and axonemal ultrastructure. Proteomic profiling links CFAP45 to an axonemal module including dynein ATPases and adenylate kinase as well as CFAP52, whose mutations cause a similar ciliopathy. CFAP45 binds AMP in vitro, consistent with structural modelling that identifies an AMP-binding interface between CFAP45 and AK8. Microtubule sliding of dyskinetic sperm from Cfap45−/− mice is rescued with the addition of either AMP or ADP with ATP, compared to ATP alone. We propose that CFAP45 supports mammalian ciliary and flagellar beating via an adenine nucleotide homeostasis module.

Principal Acid-Soluble Nucleotides in Adductor Muscle of the Scallop Placopecten magellanicus and Their Degradation during Postmortem Storage in Ice

1970 ◽  
Vol 27 (1) ◽  
pp. 83-92 ◽  
Author(s):  
Doris Fraser Hiltz ◽  
W. J. Dyer
Keyword(s):  
Degradation Products ◽  
Adenine Nucleotides ◽  
Storage Period ◽  
Adenosine Monophosphate ◽  
Adenosine Diphosphate ◽  
Fish Muscle ◽  
Adductor Muscle ◽  
Principal Minor ◽  
Uridine Diphosphate ◽  
Total Acid

In scallop adductor muscle stored at 0 C, postmortem degradation of adenosine triphosphate (ATP), the predominant nucleotide at death, primarily follows the route ATP → adenosine diphosphate (ADP) → adenosine monophosphate (AMP) → adenosine → inosine → hypoxanthine (Hx). In one lot of scallops, however, inosine monophosphate (IMP) was present as an intermediate along with AMP. Hence, an alternate pathway, similar to that in fish muscle, whereby AMP is degraded to inosine and Hx via IMP rather than adenosine, may exist under certain (undefined) conditions. ATP dephosphorylation was much slower than in fish muscle; however, a rapid turnover of the intermediates in the degradative sequence, indicating relatively high activities of the enzymes catalyzing these reactions, resulted in the formation of appreciable amounts of Hx (3–4 μmole/g) within the edible storage period. In preliminary tests, taste scores correlated well with Hx contents, suggesting that measurement of Hx content may be a useful index of quality in scallop meats.Column chromatographic analyses showed that adenine nucleotides and their degradation products accounted for about 90% of the total acid-soluble purines and pyrimidines in scallop adductor muscle, with nicotinamide adenine dinucleotide and uridine diphosphate glucose as the principal minor nucleotide constituents. The muscle also contained considerable amounts of homarine (2–3 μmole/g). Glycolysis showed no relation to nucleotide degradation, both processes demonstrating a relatively slow postmortem catabolic rate in scallop muscle.

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