Spatiotemporal pattern of nicotinamide adenine dinucleotide phosphate-diaphorase reactivity in the developing central nervous system of premetamorphicXenopus laevis tadpoles

2001 ◽  
Vol 437 (3) ◽  
pp. 350-362 ◽  
Author(s):  
David L. McLean ◽  
Keith T. Sillar
Keyword(s):  
Central Nervous System ◽  
Nervous System ◽  
Nicotinamide Adenine Dinucleotide ◽  
Nicotinamide Adenine Dinucleotide Phosphate ◽  
Nicotinamide Adenine ◽  
Spatiotemporal Pattern

scholarly journals Niacin in the Central Nervous System: An Update of Biological Aspects and Clinical Applications

2019 ◽  
Vol 20 (4) ◽  
pp. 974 ◽  
Author(s):  
Valeria Gasperi ◽  
Matteo Sibilano ◽  
Isabella Savini ◽  
Maria Catani
Keyword(s):  
Central Nervous System ◽  
Nervous System ◽  
Nicotinamide Adenine Dinucleotide ◽  
Cell Cycle Progression ◽  
Neuronal Development ◽  
Nicotinamide Adenine Dinucleotide Phosphate ◽  
Nicotinamide Adenine ◽  
Vitamin B3 ◽  
Traumatic Injuries ◽  
The Central Nervous System

Niacin (also known as “vitamin B3” or “vitamin PP”) includes two vitamers (nicotinic acid and nicotinamide) giving rise to the coenzymatic forms nicotinamide adenine dinucleotide (NAD) and nicotinamide adenine dinucleotide phosphate (NADP). The two coenzymes are required for oxidative reactions crucial for energy production, but they are also substrates for enzymes involved in non-redox signaling pathways, thus regulating biological functions, including gene expression, cell cycle progression, DNA repair and cell death. In the central nervous system, vitamin B3 has long been recognized as a key mediator of neuronal development and survival. Here, we will overview available literature data on the neuroprotective role of niacin and its derivatives, especially focusing especially on its involvement in neurodegenerative diseases (Alzheimer’s, Parkinson’s, and Huntington’s diseases), as well as in other neuropathological conditions (ischemic and traumatic injuries, headache and psychiatric disorders).

Cellular distribution of nicotinamide adenine dinucleotide glycohydrolase in the central nervous system

1974 ◽  
Vol 23 (14) ◽  
pp. 2060-2062 ◽  
Author(s):  
Spyridon G.A. Alivisatos ◽  
Frieda Ungar ◽  
Mariette Gerber ◽  
Ramesh C. Arora ◽  
Leroy P. Levitt ◽  
...  
Keyword(s):  
Central Nervous System ◽  
Nervous System ◽  
Nicotinamide Adenine Dinucleotide ◽  
Nicotinamide Adenine ◽  
Cellular Distribution ◽  
The Central Nervous System

scholarly journals Sirtuin 2 (SIRT2): Confusing Roles in the Pathophysiology of Neurological Disorders

2021 ◽  
Vol 15 ◽  
Author(s):  
Xiuqi Chen ◽  
Wenmei Lu ◽  
Danhong Wu
Keyword(s):  
Central Nervous System ◽  
Nervous System ◽  
Rapid Growth ◽  
Nicotinamide Adenine Dinucleotide ◽  
Neurological Disorders ◽  
Potential Role ◽  
Therapeutic Strategies ◽  
Nicotinamide Adenine ◽  
The Central Nervous System ◽  
The Brain

As a type of nicotinamide adenine dinucleotide (NAD+)-dependent deacetylases, sirtuin 2 (SIRT2) is predominantly found in the cytoplasm of cells in the central nervous system (CNS), suggesting its potential role in neurological disorders. Though SIRT2 is generally acknowledged to accelerate the development of neurological pathologies, it protects the brain from deterioration in certain circumstances. This review summarized the complex roles SIRT2 plays in the pathophysiology of diverse neurological disorders, compared and analyzed the discrete roles of SIRT2 in different conditions, and provided possible explanations for its paradoxical functions. In the future, the rapid growth in SIRT2 research may clarify its impacts on neurological disorders and develop therapeutic strategies targeting this protein.

scholarly journals CYTOCHEMICAL LOCALIZATION OF BRAIN NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE (OXIDIZED)-DEPENDENT DEHYDROGENASES QUALITATIVE AND QUANTITATIVE DISTRIBUTIONS

1974 ◽  
Vol 22 (1) ◽  
pp. 7-19 ◽  
Author(s):  
K. L. SIMS ◽  
F. C. KAUFFMAN ◽  
E. C. JOHNSON ◽  
V. M. PICKEL
Keyword(s):  
Nervous System ◽  
Nicotinamide Adenine Dinucleotide ◽  
Molecular Layer ◽  
Nicotinamide Adenine Dinucleotide Phosphate ◽  
Neuronal Cell ◽  
Nicotinamide Adenine ◽  
Experimental Conditions ◽  
Cytochemical Localization ◽  
Neuronal Cell Bodies ◽  
Neuronal Processes

This study compares the histochemical and microchemical localizations of nicotinamide adenine dinucleotide phosphate (reduced) and nicotinamide adenine dinucleotide (reduced) diaphorases and four nicotinamide adenine dinucleotide phosphate (oxidized)-dependent enzymes (glucose 6-phosphate, 6-phosphogluconate, malate and isocitrate dehydrogenases) in areas of rat metencephalon and spinal cord. For the four nicotinamide adenine dinucleotide phosphate (NADP) enzymes, the pattern of localization following use of a modified tetrazolium procedure was compared with quantitative data obtained by microdissection from the same areas in adjacent sections. Optimal experimental conditions for reaction pH, temperature, substrate, cofactor and divalent cation concentrations were used for both the quantitative analysis following microdissection and the histochemical tetrazolium procedure. Consecutive sections were also examined for isocitrate dehydrogenase (nicotinamide adenine dinucleotide (oxidized)) and nicotinamide adenine dinucleotide (reduced) diaphorase activities in addition to seriatim thionine reference sections. Our results indicate that, within the central nervous system, certain characteristic qualitative differences exist in the distribution of the nicotinamide adenine dinucleotide phosphate (oxidized)- and nicotinamide adenine dinucleotide (oxidized)-dependent dehydrogenase enzymes. Nicotinamide adenine, dinucleotide enzymes are visualized predominantly in neuronal cell bodies or neuropil consisting primarily of neuronal processes; in adjacent sections, NADP enzyme activities are visualized almost exclusively in glial elements with two important exceptions. The first is the cerebellar molecular layer where the results from both micro- and histochemical techniques indicate high levels of the NADP enzymes relative to other dehydrogenases and high activity relative to the levels of these NADP enzymes in other nervous system areas. The second exception occurs in those neuronal groups known to contain high levels of catecholamines; these data are the subject of a companion report.

Administration of Ginseng radix Decreases Nitric Oxide Synthase Expression in the Hippocampus of Streptozotocin-Induced Diabetic Rats

2004 ◽  
Vol 32 (04) ◽  
pp. 497-507 ◽  
Author(s):  
Hyun-Kyung Chang ◽  
Mi-Hyeon Jang ◽  
Baek-Vin Lim ◽  
Taeck-Hyun Lee ◽  
Min-Chul Shin ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Central Nervous System ◽  
Nervous System ◽  
Nitric Oxide Synthase ◽  
Aqueous Extract ◽  
Nicotinamide Adenine Dinucleotide ◽  
Nicotinamide Adenine Dinucleotide Phosphate ◽  
Diabetic Rats ◽  
Secondary Complications ◽  
Oxide Synthase

Nitric oxide (NO) is synthesized from L-arginine by nitric oxide synthase (NOS). Alternation of NOS expression is implicated in the pathogenesis of numerous secondary complications of diabetes. Aqueous extract of Ginseng radix has traditionally been used for the various disorders including diabetes. In this study, the effect of Ginseng radix on the NOS expression in the hippocampus of streptozotocin (STZ)-induced diabetic rats was investigated via nicotinamide adenine dinucleotide phosphate-diaphorase (NADPH-d) histochemistry. Enhanced NOS expression was detected in the hippocampus of diabetic rats and administration of Ginseng radix suppressed NOS expression. Ginseng radix may aid the treatment of central nervous system complications in diabetes.

scholarly journals Meningitis-Associated Central Nervous System Complications are Mediated by the Activation of Poly(ADP-ribose) Polymerase

2002 ◽  
Vol 22 (1) ◽  
pp. 39-49 ◽  
Author(s):  
Uwe Koedel ◽  
Frank Winkler ◽  
Barbara Angele ◽  
Adriano Fontana ◽  
Hans-Walter Pfister
Keyword(s):  
Central Nervous System ◽  
Nervous System ◽  
Endothelial Cell ◽  
Nicotinamide Adenine Dinucleotide ◽  
Clinical Status ◽  
Nicotinamide Adenine ◽  
Parp Inhibition ◽  
Acute Bacterial Meningitis ◽  
Parp Activation ◽  
Meningeal Inflammation

The present study assessed the role of PARP [poly(adenosine diphosphate-ribose) polymerase] activation in experimental pneumococcal meningitis. Mice with a targeted disruption of the PARP1 gene were protected against meningitis-associated central nervous system complications including blood-brain barrier breaching and increase in intracranial pressure. This beneficial effect was paralleled by a significant reduction in meningeal inflammation, as evidenced by significantly lower cerebrospinal fluid leukocyte counts and interleukin-1β, −6, and tumor necrosis factor-α concentrations in the brain (compared with infected wild-type mice). The reduction in inflammation and central nervous system complications was associated with an improved clinical status of infected, PARP1-deficient mice. A similar protective effect was achieved by PARP inhibition using 3-aminobenzamide, the pharmacologic efficacy of which was confirmed by a marked attenuation of meningitis-induced poly(ADP)ribose formation. When the rat brain-derived endothelial cell line GP8.3 was cocultured with macrophages, exposure to pneumococci induced endothelial cell death and was paralleled by PARP activation and a reduction in the oxidized form of cellular nicotinamide adenine dinucleotide content. Treatment with 3-aminobenzamide significantly attenuated cellular nicotinamide adenine dinucleotide depletion and pneumococci-induced cytotoxicity. Thus, PARP activation seems to play a crucial role in the development of meningitis-associated central nervous system complications and pneumococci-induced endothelial injury. Inhibitors of PARP activation could provide a potential therapy of acute bacterial meningitis.

Effect of Niacin on Mitochondria of Allium Cepa Root Cells

1967 ◽  
Vol 25 ◽  
pp. 78-79
Author(s):  
M. Arif Hayat
Keyword(s):  
Nicotinamide Adenine Dinucleotide ◽  
Hydrogen Transfer ◽  
Nicotinamide Adenine Dinucleotide Phosphate ◽  
Nicotinamide Adenine ◽  
Root Tips ◽  
Root Cells ◽  
Transfer Processes ◽  
Standard Procedures ◽  
A Cell ◽  
Critical Interest

Although it is recognized that niacin (pyridine-3-carboxylic acid), incorporated as the amide in nicotinamide adenine dinucleotide (NAD) or in nicotinamide adenine dinucleotide phosphate (NADP), is a cofactor in hydrogen transfer in numerous enzyme reactions in all organisms studied, virtually no information is available on the effect of this vitamin on a cell at the submicroscopic level. Since mitochondria act as sites for many hydrogen transfer processes, the possible response of mitochondria to niacin treatment is, therefore, of critical interest.Onion bulbs were placed on vials filled with double distilled water in the dark at 25°C. After two days the bulbs and newly developed root system were transferred to vials containing 0.1% niacin. Root tips were collected at ¼, ½, 1, 2, 4, and 8 hr. intervals after treatment. The tissues were fixed in glutaraldehyde-OsO4 as well as in 2% KMnO4 according to standard procedures. In both cases, the tissues were dehydrated in an acetone series and embedded in Reynolds' lead citrate for 3-10 minutes.

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