Log in

Relevant bibliographies by topics / Carnitine. Biosynthese / Journal articles

To see the other types of publications on this topic, follow the link: Carnitine. Biosynthese.

Journal articles on the topic 'Carnitine. Biosynthese'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the top 50 journal articles for your research on the topic 'Carnitine. Biosynthese.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Browse journal articles on a wide variety of disciplines and organise your bibliography correctly.

1

French, Timothy J., Anthony W. Goode, Paul S. Schofield, and Mary C. Sugden. "Control of tissue carnitine contents: Effects of partial hepatectomy and liver regeneration on carnitine concentrations in liver and extrahepatic tissues of the rat." Bioscience Reports 5, no. 1 (1985): 47–55. http://dx.doi.org/10.1007/bf01117440.

Full text

Abstract:

The liver is the sole site of carnitine biosynthesis in the rat. However, the first 24 h after the surgical removal of two-thirds of the liver mass are not associated with depletion of carnitine either in the liver remnant or in a number of extrahepatic tissues with relatively short turnover times of carnitine (<24 h; heart, spleen, kidney). Dietary carnitine was not supplied. The results suggest that the capacity of the remnant liver for carnitine biosynthesis is sufficient to maintain tissue carnitine contents. Liver regeneration influenced the relative proportions of hepatic free and acy

APA, Harvard, Vancouver, ISO, and other styles

2

Carillo, Maria Rosaria, Carla Bertapelle, Filippo Scialò, et al. "L-Carnitine in Drosophila: A Review." Antioxidants 9, no. 12 (2020): 1310. http://dx.doi.org/10.3390/antiox9121310.

Full text

Abstract:

L-Carnitine is an amino acid derivative that plays a key role in the metabolism of fatty acids, including the shuttling of long-chain fatty acyl CoA to fuel mitochondrial β-oxidation. In addition, L-carnitine reduces oxidative damage and plays an essential role in the maintenance of cellular energy homeostasis. L-carnitine also plays an essential role in the control of cerebral functions, and the aberrant regulation of genes involved in carnitine biosynthesis and mitochondrial carnitine transport in Drosophila models has been linked to neurodegeneration. Drosophila models of neurodegenerative

APA, Harvard, Vancouver, ISO, and other styles

3

VAZ, Frédéric M., and Ronald J. A. WANDERS. "Carnitine biosynthesis in mammals." Biochemical Journal 361, no. 3 (2002): 417–29. http://dx.doi.org/10.1042/bj3610417.

Full text

Abstract:

Carnitine is indispensable for energy metabolism, since it enables activated fatty acids to enter the mitochondria, where they are broken down via β-oxidation. Carnitine is probably present in all animal species, and in numerous micro-organisms and plants. In mammals, carnitine homoeostasis is maintained by endogenous synthesis, absorption from dietary sources and efficient tubular reabsorption by the kidney. This review aims to cover the current knowledge of the enzymological, molecular, metabolic and regulatory aspects of mammalian carnitine biosynthesis, with an emphasis on the human and ra

APA, Harvard, Vancouver, ISO, and other styles

4

Lee Carter, A., Tom O. Abney, and David F. Lapp. "Biosynthesis and Metabolism of Carnitine." Journal of Child Neurology 10, no. 2_suppl (1995): 2S3–2S7. http://dx.doi.org/10.1177/0883073895010002s02.

Full text

Abstract:

This review article presents the biosynthesis, metabolism, sources, levels, and general functions of carnitine. Emphasis is placed on the expression of carnitine deficiency and insufficiency as well as the causes of these conditions. The various functions of carnitine are discussed as they may relate to disease treatment. (J Child Neurol 1995;10(Suppl):2S3-2S7).

APA, Harvard, Vancouver, ISO, and other styles

5

Broderick, Tom L., Frank A. Cusimano, Chelsea Carlson, and Jeganathan Ramesh Babu. "Biosynthesis of the Essential Fatty Acid Oxidation Cofactor Carnitine Is Stimulated in Heart and Liver after a Single Bout of Exercise in Mice." Journal of Nutrition and Metabolism 2018 (May 29, 2018): 1–7. http://dx.doi.org/10.1155/2018/2785090.

Full text

Abstract:

We determined whether one single bout of exercise stimulates carnitine biosynthesis and carnitine uptake in liver and heart. Free carnitine (FC) in plasma was assayed using acetyltransferase and [14C]acetyl-CoA in Swiss Webster mice after 1 hour of moderate-intensity treadmill running or 4 hours and 8 hours into recovery. Liver and heart were removed under the same conditions for measurement of carnitine biosynthesis enzymes (liver butyrobetaine hydroxylase, γ-BBH; heart trimethyllysine dioxygenase, TMLD), organic cation transporter-2 (OCTN2, carnitine transporter), and liver peroxisome prolif

APA, Harvard, Vancouver, ISO, and other styles

6

Longo, Nicola. "Primary Carnitine Deficiency and Newborn Screening for Disorders of the Carnitine Cycle." Annals of Nutrition and Metabolism 68, Suppl. 3 (2016): 5–9. http://dx.doi.org/10.1159/000448321.

Full text

Abstract:

Carnitine is needed for transfer of long-chain fatty acids across the inner mitochondrial membrane for subsequent β-oxidation. Carnitine can be synthesized by the body and is also obtained in the diet through consumption of meat and dairy products. Defects in carnitine transport such as those caused by defective activity of the OCTN2 transporter encoded by the SLC22A5 gene result in primary carnitine deficiency, and newborn screening programmes can identify patients at risk for this condition before irreversible damage. Initial biochemical diagnosis can be confirmed through molecular testing,

APA, Harvard, Vancouver, ISO, and other styles

7

Almannai, Mohammed, Majid Alfadhel, and Ayman W. El-Hattab. "Carnitine Inborn Errors of Metabolism." Molecules 24, no. 18 (2019): 3251. http://dx.doi.org/10.3390/molecules24183251.

Full text

Abstract:

Carnitine plays essential roles in intermediary metabolism. In non-vegetarians, most of carnitine sources (~75%) are obtained from diet whereas endogenous synthesis accounts for around 25%. Renal carnitine reabsorption along with dietary intake and endogenous production maintain carnitine homeostasis. The precursors for carnitine biosynthesis are lysine and methionine. The biosynthetic pathway involves four enzymes: 6-N-trimethyllysine dioxygenase (TMLD), 3-hydroxy-6-N-trimethyllysine aldolase (HTMLA), 4-N-trimethylaminobutyraldehyde dehydrogenase (TMABADH), and γ-butyrobetaine dioxygenase (BB

APA, Harvard, Vancouver, ISO, and other styles

8

VAZ, Frédéric M., and Ronald J. A. WANDERS. "Carnitine biosynthesis in mammals." Biochemical Journal 361, no. 3 (2002): 417. http://dx.doi.org/10.1042/0264-6021:3610417.

Full text

APA, Harvard, Vancouver, ISO, and other styles

9

Upadhyay, Aman, Layla Al-Nakkash, and Tom L. Broderick. "Effects of Exercise Training on Renal Carnitine Biosynthesis and Uptake in the High-Fat and High-Sugar-Fed Mouse." Molecules 25, no. 9 (2020): 2100. http://dx.doi.org/10.3390/molecules25092100.

Full text

Abstract:

(1) Background: Diet-induced obesity inhibits hepatic carnitine biosynthesis. Herein, the effects of high-fat (HF) and high-sugar (HFHS) feeding and exercise training (ET) on renal carnitine biosynthesis and uptake were determined. (2) Methods: Male C57BL/6J mice were assigned to the following groups: lean control (standard chow), HFHS diet, and HFHS diet with ET. ET consisted of 150 min of treadmill running per week for 12 weeks. Protein levels of γ-butyrobetaine hydroxylase (γ-BBH) and organic cation transporter-2 (OCTN2) were measured as markers of biosynthesis and uptake, respectively. (3)

APA, Harvard, Vancouver, ISO, and other styles

10

Hanai, Tatsunori, Makoto Shiraki, Kenji Imai, Atsushi Suetugu, Koji Takai, and Masahito Shimizu. "Usefulness of Carnitine Supplementation for the Complications of Liver Cirrhosis." Nutrients 12, no. 7 (2020): 1915. http://dx.doi.org/10.3390/nu12071915.

Full text

Abstract:

Carnitine is a vitamin-like substance that regulates lipid metabolism and energy production. Carnitine homeostasis is mainly regulated by dietary intake and biosynthesis in the organs, including the skeletal muscle and the liver. Therefore, liver cirrhotic patients with reduced food intake, malnutrition, biosynthetic disorder, and poor storage capacity of carnitine in the skeletal muscle and liver are more likely to experience carnitine deficiency. In particular, liver cirrhotic patients with sarcopenia are at a high risk for developing carnitine deficiency. Carnitine deficiency impairs the im

APA, Harvard, Vancouver, ISO, and other styles

11

Broderick, Tom L., Adil El Midaoui, Jean-Louis Chiasson, Donghao Wang, Marek Jankowski та Jolanta Gutkowska. "The effects of exercise training on γ-butyrobetaine hydroxylase and novel organic cation transporter-2 gene expression in the rat". Applied Physiology, Nutrition, and Metabolism 36, № 6 (2011): 781–89. http://dx.doi.org/10.1139/h11-094.

Full text

Abstract:

The concentration of carnitine in plasma is generally increased with exercise training, suggesting that either carnitine biosynthesis is stimulated or renal reabsorption of carnitine is enhanced, or both. Carnitine, an essential cofactor in the oxidation of fatty acids, is released into the plasma following hydroxylation by γ-butyrobetaine hydroxylase (BBH), the final enzyme in the biosynthetic pathway found primarily in the liver. The organic cation transporter (OCTN2), the carnitine transporter found in kidney, is important in the distribution of carnitine by facilitating its renal reabsorpt

APA, Harvard, Vancouver, ISO, and other styles

12

Rebouche, C. J. "Ascorbic acid and carnitine biosynthesis." American Journal of Clinical Nutrition 54, no. 6 (1991): 1147S—1152S. http://dx.doi.org/10.1093/ajcn/54.6.1147s.

Full text

APA, Harvard, Vancouver, ISO, and other styles

13

Borum, Peggy R. "Role of carnitine during development." Canadian Journal of Physiology and Pharmacology 63, no. 5 (1985): 571–76. http://dx.doi.org/10.1139/y85-097.

Full text

Abstract:

Fatty acids are an important fuel source for neonates. The utilization of long chain fatty acids as a fuel source is dependent upon adequate concentrations of carnitine. Carnitine also has functions in other physiological processes critical to the survival of the neonate such as lipolysis, thermogenesis, ketogenesis, and possibly regulation of certain aspects of nitrogen metabolism. Plasma and tissue carnitine concentrations in neonates are depressed compared with those of older individuals. The capability for carnitine biosynthesis is much less in the neonate than in the adult. Human milk con

APA, Harvard, Vancouver, ISO, and other styles

14

Vaz, Frédéric M., Bela Melegh, Judit Bene, et al. "Analysis of Carnitine Biosynthesis Metabolites in Urine by HPLC–Electrospray Tandem Mass Spectrometry." Clinical Chemistry 48, no. 6 (2002): 826–34. http://dx.doi.org/10.1093/clinchem/48.6.826.

Full text

Abstract:

Abstract Background: We developed a method to determine the urinary concentrations of metabolites in the synthetic pathway for carnitine from N6-trimethyllysine and applied this method to determine their excretion in control individuals. In addition, we investigated whether newborns are capable of carnitine synthesis from deuterium-labeled N6-trimethyllysine. Methods: Urine samples were first derivatized with methyl chloroformate. Subsequently, the analytes were separated by ion-pair, reversed-phase HPLC and detected online by electrospray tandem mass spectrometry. Stable-isotope-labeled refer

APA, Harvard, Vancouver, ISO, and other styles

15

Kozulić, B., K. Mosbach, and F. Meussdoerffer. "Biosynthesis of soluble carnitine acetyltransferases from the yeast Candida tropicalis." Biochemical Journal 253, no. 3 (1988): 845–49. http://dx.doi.org/10.1042/bj2530845.

Full text

Abstract:

Soluble carnitine acetyltransferase from Candida tropicalis is synthesized as a 76 kDa precursor, which is monomeric and possesses no or very little carnitine acetyltransferase activity. Maturation of the enzyme begins with proteolytic processing of the 76 kDa precursor to 64 and 57 kDa subunits. The processed subunits subsequently associate into two kinds of active oligomers; the 57 kDa subunits are assembled into a tetramer and the 64 kDa subunits into an octamer. Formation of these oligomers depends apparently on growth conditions, since both oligomers were present in cells grown in continu

APA, Harvard, Vancouver, ISO, and other styles

16

Ringseis, Robert, Gaiping Wen та Klaus Eder. "Regulation of Genes Involved in Carnitine Homeostasis by PPARαacross Different Species (Rat, Mouse, Pig, Cattle, Chicken, and Human)". PPAR Research 2012 (2012): 1–11. http://dx.doi.org/10.1155/2012/868317.

Full text

Abstract:

Recent studies in rodents convincingly demonstrated that PPARαis a key regulator of genes involved in carnitine homeostasis, which serves as a reasonable explanation for the phenomenon that energy deprivation and fibrate treatment, both of which cause activation of hepatic PPARα, causes a strong increase of hepatic carnitine concentration in rats. The present paper aimed to comprehensively analyse available data from genetic and animal studies with mice, rats, pigs, cows, and laying hens and from human studies in order to compare the regulation of genes involved in carnitine homeostasis by PPA

APA, Harvard, Vancouver, ISO, and other styles

17

Maas, Marijn N., Jordi C. J. Hintzen, Miriam R. B. Porzberg, and Jasmin Mecinović. "Trimethyllysine: From Carnitine Biosynthesis to Epigenetics." International Journal of Molecular Sciences 21, no. 24 (2020): 9451. http://dx.doi.org/10.3390/ijms21249451.

Full text

Abstract:

Trimethyllysine is an important post-translationally modified amino acid with functions in the carnitine biosynthesis and regulation of key epigenetic processes. Protein lysine methyltransferases and demethylases dynamically control protein lysine methylation, with each state of methylation changing the biophysical properties of lysine and the subsequent effect on protein function, in particular histone proteins and their central role in epigenetics. Epigenetic reader domain proteins can distinguish between different lysine methylation states and initiate downstream cellular processes upon rec

APA, Harvard, Vancouver, ISO, and other styles

18

El-Hattab, Ayman W., and Fernando Scaglia. "Disorders of carnitine biosynthesis and transport." Molecular Genetics and Metabolism 116, no. 3 (2015): 107–12. http://dx.doi.org/10.1016/j.ymgme.2015.09.004.

Full text

APA, Harvard, Vancouver, ISO, and other styles

19

Elimrani, Ihsan, Karim Lahjouji, Ernest Seidman, Marie-Josée Roy, Grant A. Mitchell, and Ijaz Qureshi. "Expression and localization of organic cation/carnitine transporter OCTN2 in Caco-2 cells." American Journal of Physiology-Gastrointestinal and Liver Physiology 284, no. 5 (2003): G863—G871. http://dx.doi.org/10.1152/ajpgi.00220.2002.

Full text

Abstract:

l-Carnitine is derived both from dietary sources and biosynthesis. Dietary carnitine is absorbed in the small intestine and then distributed to other organs. Previous studies using Caco-2 cells demonstrated that the transport ofl-carnitine in the intestine involves a carrier-mediated system. The purpose of this study was to determine whether the uptake of l-carnitine in Caco-2 cells is mediated by the recently identified organic cation/carnitine transporter (OCTN2). Kinetics ofl-[3H]carnitine uptake were investigated with or without specific inhibitors. l-Carnitine uptake in mature cells was s

APA, Harvard, Vancouver, ISO, and other styles

20

Mok, Amy Y. P., and William C. McMurray. "Biosynthesis of phosphatidic acid by glycerophosphate acyltransferases in rat liver mitochondria and microsomes." Biochemistry and Cell Biology 68, no. 12 (1990): 1380–92. http://dx.doi.org/10.1139/o90-201.

Full text

Abstract:

The acyltransferases that catalyze the synthesis of phosphatidic acid from labelled sn-[14C]glycero-3-phosphate and fatty acyl carnitine or coenzyme A derivatives have been shown to be present in both isolated mitochondria and microsomes from rat liver. The major reaction product was phosphatidic acid in both subcellular fractions. A small quantity of lysophosphatidic acid and neutral lipids were produced as by-products. Divalent cations had significant effects on both mitochondrial and microsomal fractions in stimulating acylation using palmitoyl CoA, but not when palmitoyl carnitine was used

APA, Harvard, Vancouver, ISO, and other styles

21

Gnoni, Antonio, Serena Longo, Gabriele V. Gnoni, and Anna M. Giudetti. "Carnitine in Human Muscle Bioenergetics: Can Carnitine Supplementation Improve Physical Exercise?" Molecules 25, no. 1 (2020): 182. http://dx.doi.org/10.3390/molecules25010182.

Full text

Abstract:

l-Carnitine is an amino acid derivative widely known for its involvement in the transport of long-chain fatty acids into the mitochondrial matrix, where fatty acid oxidation occurs. Moreover, l-Carnitine protects the cell from acyl-CoA accretion through the generation of acylcarnitines. Circulating carnitine is mainly supplied by animal-based food products and to a lesser extent by endogenous biosynthesis in the liver and kidney. Human muscle contains high amounts of carnitine but it depends on the uptake of this compound from the bloodstream, due to muscle inability to synthesize carnitine. M

APA, Harvard, Vancouver, ISO, and other styles

22

Kepka, Alina, Agnieszka Ochocinska, Małgorzata Borzym-Kluczyk, et al. "Preventive Role of L-Carnitine and Balanced Diet in Alzheimer’s Disease." Nutrients 12, no. 7 (2020): 1987. http://dx.doi.org/10.3390/nu12071987.

Full text

Abstract:

The prevention or alleviation of neurodegenerative diseases, including Alzheimer’s disease (AD), is a challenge for contemporary health services. The aim of this study was to review the literature on the prevention or alleviation of AD by introducing an appropriate carnitine-rich diet, dietary carnitine supplements and the MIND (Mediterranean-DASH Intervention for Neurodegenerative Delay) diet, which contains elements of the Mediterranean diet and the Dietary Approaches to Stop Hypertension (DASH) diet. L-carnitine (LC) plays a crucial role in the energetic metabolism of the cell. A properly b

APA, Harvard, Vancouver, ISO, and other styles

23

Di Cristo, Francesca, Anna Calarco, Filomena Anna Digilio, et al. "The Discovery of Highly Potent THP Derivatives as OCTN2 Inhibitors: From Structure-Based Virtual Screening to In Vivo Biological Activity." International Journal of Molecular Sciences 21, no. 19 (2020): 7431. http://dx.doi.org/10.3390/ijms21197431.

Full text

Abstract:

A mismatch between β-oxidation and the tricarboxylic acid cycle (TCA) cycle flux in mitochondria produces an accumulation of lipid metabolic intermediates, resulting in both blunted metabolic flexibility and decreased glucose utilization in the affected cells. The ability of the cell to switch to glucose as an energy substrate can be restored by reducing the reliance of the cell on fatty acid oxidation. The inhibition of the carnitine system, limiting the carnitine shuttle to the oxidation of lipids in the mitochondria, allows cells to develop a high plasticity to metabolic rewiring with a dec

APA, Harvard, Vancouver, ISO, and other styles

24

van Vlies, Naomi, Sacha Ferdinandusse, Marjolein Turkenburg, Ronald J. A. Wanders та Frédéric M. Vaz. "PPARα-activation results in enhanced carnitine biosynthesis and OCTN2-mediated hepatic carnitine accumulation". Biochimica et Biophysica Acta (BBA) - Bioenergetics 1767, № 9 (2007): 1134–42. http://dx.doi.org/10.1016/j.bbabio.2007.07.001.

Full text

APA, Harvard, Vancouver, ISO, and other styles

25

Fujita, Masaharu, Takeo Nakanishi, Yuta Shibue та ін. "Hepatic uptake of γ-butyrobetaine, a precursor of carnitine biosynthesis, in rats". American Journal of Physiology-Gastrointestinal and Liver Physiology 297, № 4 (2009): G681—G686. http://dx.doi.org/10.1152/ajpgi.00238.2009.

Full text

Abstract:

γ-Butyrobetaine (GBB) is a precursor in the biosynthesis of carnitine, which plays an important role in the β-oxidation of fatty acids, and is converted to carnitine by γ-butyrobetaine dioxygenase (BBD) predominantly in liver. We investigated the molecular mechanism of hepatic uptake of GBB in rat hepatocytes. Cellular localization of rat Octn2 (rOctn2:Slc22A5) was studied by Western blot analysis. Uptake of deuterated GBB (d3-GBB) was examined in HEK293 cells expressing rOctn2 (HEK293/rOctn2) and freshly isolated rat hepatocytes. d3-GBB was quantified by use of liquid chromatography-tandem ma

APA, Harvard, Vancouver, ISO, and other styles

26

Heo, K. N., J. Odle, and In K. Han. "Effects of Dietary L-Carnitine and Protein Level on Plasma Carnitine, Energy and Carnitine Balance, and Carnitine Biosynthesis of 20 kg Pigs." Asian-Australasian Journal of Animal Sciences 13, no. 11 (2000): 1568–75. http://dx.doi.org/10.5713/ajas.2000.1568.

Full text

APA, Harvard, Vancouver, ISO, and other styles

27

Joshi, Molishree, Jihye Kim, Angelo D’Alessandro, et al. "CPT1A Over-Expression Increases Reactive Oxygen Species in the Mitochondria and Promotes Antioxidant Defenses in Prostate Cancer." Cancers 12, no. 11 (2020): 3431. http://dx.doi.org/10.3390/cancers12113431.

Full text

Abstract:

Cancers reprogram their metabolism to adapt to environmental changes. In this study, we examined the consequences of altered expression of the mitochondrial enzyme carnitine palmitoyl transferase I (CPT1A) in prostate cancer (PCa) cell models. Using transcriptomic and metabolomic analyses, we compared LNCaP-C4-2 cell lines with depleted (knockdown (KD)) or increased (overexpression (OE)) CPT1A expression. Mitochondrial reactive oxygen species (ROS) were also measured. Transcriptomic analysis identified ER stress, serine biosynthesis and lipid catabolism as significantly upregulated pathways in

APA, Harvard, Vancouver, ISO, and other styles

28

Roberts, Paul A., Jamal Bouitbir, Annalisa Bonifacio, et al. "Contractile function and energy metabolism of skeletal muscle in rats with secondary carnitine deficiency." American Journal of Physiology-Endocrinology and Metabolism 309, no. 3 (2015): E265—E274. http://dx.doi.org/10.1152/ajpendo.00001.2015.

Full text

Abstract:

The consequences of carnitine depletion upon metabolic and contractile characteristics of skeletal muscle remain largely unexplored. Therefore, we investigated the effect of N-trimethyl-hydrazine-3-propionate (THP) administration, a carnitine analog inhibiting carnitine biosynthesis and renal reabsorption of carnitine, on skeletal muscle function and energy metabolism. Male Sprague-Dawley rats were fed a standard rat chow in the absence (CON; n = 8) or presence of THP ( n = 8) for 3 wk. Following treatment, rats were fasted for 24 h prior to excision of their soleus and EDL muscles for biochem

APA, Harvard, Vancouver, ISO, and other styles

29

Bagherzadeh Rahmani, Behnam. "The effect of aerobic training and consumption of L-carnitine supplements on Gen expression of HMG-CoA reductase and LDL receptor in the liver of male Wistar rats Injected by Boldenone." International Journal of Applied Exercise Physiology 7, no. 2 (2018): 64–75. http://dx.doi.org/10.22631/ijaep.v7i2.291.

Full text

Abstract:

The aim of this study was to investigate the effect of aerobic training and consumption of L-carnitine supplements on HMG-CoA reductase and LDL receptor in the liver of male Wistar rats toxicated by Boldenone. 30 male Wistar rats aged 12 weeks (weight 195±7.94g) were randomly divided into five groups: control, sham, boldenone (5mg/kg), L-carnitine, aerobic training- L-carnitine.The endurance moderate intensity training program (55-50% of maximal oxygen consumption) performed for 6 weeks and 5 times a week. Injection once a week, on an appointed day, and in the quadriceps and hamstring was cond

APA, Harvard, Vancouver, ISO, and other styles

30

Wang, Yali, Y. Vijayendar Reddy, Abbas H. K. Al Temimi, et al. "Investigating the active site of human trimethyllysine hydroxylase." Biochemical Journal 476, no. 7 (2019): 1109–19. http://dx.doi.org/10.1042/bcj20180857.

Full text

Abstract:

Abstract The biologically important carnitine biosynthesis pathway in humans proceeds via four enzymatic steps. The first step in carnitine biosynthesis is catalyzed by trimethyllysine hydroxylase (TMLH), a non-heme Fe(II) and 2-oxoglutarate (2OG)-dependent oxygenase, which catalyzes the stereospecific hydroxylation of (2S)-Nε-trimethyllysine to (2S,3S)-3-hydroxy-Nε-trimethyllysine. Here, we report biocatalytic studies on human TMLH and its 19 variants introduced through site-directed mutagenesis. Amino acid substitutions at the sites involved in binding of the Fe(II) cofactor, 2OG cosubstrate

APA, Harvard, Vancouver, ISO, and other styles

31

Krähenbühl, Stephan, Eric P. Brass, and Charles L. Hoppel. "Decreased carnitine biosynthesis in rats with secondary biliary cirrhosis." Hepatology 31, no. 6 (2000): 1217–23. http://dx.doi.org/10.1053/jhep.2000.8105.

Full text

APA, Harvard, Vancouver, ISO, and other styles

32

Rydzik, Anna M., Ivanhoe K. H. Leung, Armin Thalhammer, Grazyna T. Kochan, Timothy D. W. Claridge, and Christopher J. Schofield. "Fluoromethylated derivatives of carnitine biosynthesis intermediates – synthesis and applications." Chem. Commun. 50, no. 10 (2014): 1175–77. http://dx.doi.org/10.1039/c3cc47581f.

Full text

APA, Harvard, Vancouver, ISO, and other styles

33

Horiuchi, Masahisa, Keiko Kobayashi, Naomasa Asaka, and Takeyori Saheki. "Secondary abnormality of carnitine biosynthesis results from carnitine reabsorptional system defect in juvenile visceral steatosis mice." Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease 1362, no. 2-3 (1997): 263–68. http://dx.doi.org/10.1016/s0925-4439(97)00089-6.

Full text

APA, Harvard, Vancouver, ISO, and other styles

34

Dhar, Pradip K., Ingrid L. Grupp, Arnold Schwartz, Gunter Grupp, and Mohammed A. Matlib. "Reduction of Carnitine Content by Inhibition of Its Biosynthesis Results in Protection of Isolated Guinea Pig Hearts against Hypoxic Damage." Journal of Cardiovascular Pharmacology and Therapeutics 1, no. 3 (1996): 235–42. http://dx.doi.org/10.1177/107424849600100307.

Full text

Abstract:

Background 3-(2,2,2-trimethylhydrazinium) propionate (THP or mildronate) is an inhibitor of carnitine biosynthesis. This study was carried out to determine whether feeding of guinea pigs with THP results in decreased myocardial-free carnitine content and, as a result, attenuates hypoxic damage in isolated and paced work-performing hearts. Methods and Results Guinea pigs were administered either distilled water or 100 mg THP/kg/day orally for 10 days. The treatment resulted in about a 50% decline in myocardial-free carnitine content, from 11.1 ± 0.2 (n = 5) to 5.6 ± 0.2 (n = 5) μM/g dry weight

APA, Harvard, Vancouver, ISO, and other styles

35

Dambrova, Maija, Helena Cirule, Baiba Svalbe, et al. "Effect of inhibiting carnitine biosynthesis on male rat sexual performance." Physiology & Behavior 95, no. 3 (2008): 341–47. http://dx.doi.org/10.1016/j.physbeh.2008.06.012.

Full text

APA, Harvard, Vancouver, ISO, and other styles

36

Sevilla, A., M. Canovas, D. Keller, S. Reimers, and J. L. Iborra. "Impairing and Monitoring Glucose Catabolite Repression in L-Carnitine Biosynthesis." Biotechnology Progress 23, no. 6 (2007): 1286–96. http://dx.doi.org/10.1021/bp070213t.

Full text

APA, Harvard, Vancouver, ISO, and other styles

37

Tanphaichitr, Vichai, та Harry P. Broquist. "Role of Lysine and ε-N-Trimethyllysine in Carnitine Biosynthesis". Nutrition Reviews 46, № 4 (2009): 164–66. http://dx.doi.org/10.1111/j.1753-4887.1988.tb05413.x.

Full text

APA, Harvard, Vancouver, ISO, and other styles

38

Deng, Xinqi, Nan Jiang, Li Guo, et al. "Protective Effects and Metabolic Regulatory Mechanisms of Shenyan Fangshuai Recipe on Chronic Kidney Disease in Rats." Evidence-Based Complementary and Alternative Medicine 2020 (August 25, 2020): 1–13. http://dx.doi.org/10.1155/2020/5603243.

Full text

Abstract:

Background. Chronic kidney disease (CKD) is one of the major causes of renal damage. Shenyan Fangshuai Recipe (SFR), a modified prescription of traditional medicine in China, showed potent effects in alleviating edema, proteinuria, and hematuria of CKD in clinical practices. In this study, we aimed to investigate scientific evidence-based efficacy as well as metabolic regulations of SFR in CKD treatment. Materials and Methods. The effect of SFR on CKD was observed in a rat model which is established with oral administration of adenine-ethambutol mixture for 21 days. Further, metabolites in ser

APA, Harvard, Vancouver, ISO, and other styles

39

Jacques, Florian, Yingjuan Zhao, Martina Kopečná та ін. "Roles for ALDH10 enzymes in γ-butyrobetaine synthesis, seed development, germination, and salt tolerance in Arabidopsis". Journal of Experimental Botany 71, № 22 (2020): 7088–102. http://dx.doi.org/10.1093/jxb/eraa394.

Full text

Abstract:

Abstract Plant genomes generally contain two aldehyde dehydrogenase 10 (ALDH10) genes, which encode NAD+-dependent enzymes. These oxidize various aminoaldehydes that are produced by the catabolism of amino acids and polyamines. ALDH10s are closely related to the animal and fungal trimethylaminobutyraldehyde dehydrogenases (TMABADHs) that are involved in the synthesis of γ-butyrobetaine, the precursor of carnitine. Here, we explore the ability of the Arabidopsis thaliana proteins AtALDH10A8 and AtALDH10A9 to oxidize aminoaldehydes. We demonstrate that these enzymes display high TMABADH activiti

APA, Harvard, Vancouver, ISO, and other styles

40

van VLIES, Naomi, Liqun TIAN, Henk OVERMARS, et al. "Characterization of carnitine and fatty acid metabolism in the long-chain acyl-CoA dehydrogenase-deficient mouse." Biochemical Journal 387, no. 1 (2005): 185–93. http://dx.doi.org/10.1042/bj20041489.

Full text

Abstract:

In the present paper, we describe a novel method which enables the analysis of tissue acylcarnitines and carnitine biosynthesis intermediates in the same sample. This method was used to investigate the carnitine and fatty acid metabolism in wild-type and LCAD−/− (long-chain acyl-CoA dehydrogenase-deficient) mice. In agreement with previous results in plasma and bile, we found accumulation of the characteristic C14:1-acylcarnitine in all investigated tissues from LCAD−/− mice. Surprisingly, quantitatively relevant levels of 3-hydroxyacylcarnitines were found to be present in heart, muscle and b

APA, Harvard, Vancouver, ISO, and other styles

41

Lin, Xi, Pasha A. Lyvers Peffer, Jason Woodworth та Jack Odle. "Ontogeny of carnitine biosynthesis in Sus scrofa domesticus, inferred from γ-butyrobetaine hydroxylase (dioxygenase) activity and substrate inhibition". American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 319, № 1 (2020): R43—R49. http://dx.doi.org/10.1152/ajpregu.00051.2020.

Full text

Abstract:

γ-Butyrobetaine hydroxylase (γ-BBH) is the last limiting enzyme of the l-carnitine biosynthesis pathway and plays an important role in catalyzing the hydroxylation of γ-butyrobetaine (γ-BB) to l-carnitine. To study the developmental effect of substrate concentration on the enzyme’s specific activity, kinetics of γ-BBH were measured in liver and kidney from newborn and 1-, 7-, 21-, 35-, 56-, and 210-day-old domestic pigs. Fresh tissue homogenates were assayed under nine concentrations of γ-BB from 0 to 1.5 mM. Substrate inhibition associated with age was observed at ≥0.6 mM of γ-BB. Hepatic act

APA, Harvard, Vancouver, ISO, and other styles

42

Leśniak, Robert K., Suzana Markolovic, Kaspars Tars та Christopher J. Schofield. "Human carnitine biosynthesis proceeds via (2S,3S)-3-hydroxy-Nε-trimethyllysine". Chemical Communications 53, № 2 (2017): 440–42. http://dx.doi.org/10.1039/c6cc08381a.

Full text

Abstract:

The stereochemistry of human trimethyllysine hydroxylase was determined to be (2S,3S)-3-hydroxy-N<sup>ε</sup>-trimethyllysine by comparison to asymmetrically synthesised (2S,3R)-3-hydroxy-N<sup>ε</sup>-trimethyllysine.

APA, Harvard, Vancouver, ISO, and other styles

43

van Vlies, Naomi, Rob Ofman, Ronald J. A. Wanders, and Frédéric M. Vaz. "Submitochondrial localization of 6-N-trimethyllysine dioxygenase − implications for carnitine biosynthesis." FEBS Journal 274, no. 22 (2007): 5845–51. http://dx.doi.org/10.1111/j.1742-4658.2007.06108.x.

Full text

APA, Harvard, Vancouver, ISO, and other styles

44

Tars, Kaspars, Janis Leitans, Andris Kazaks та ін. "Targeting Carnitine Biosynthesis: Discovery of New Inhibitors against γ-Butyrobetaine Hydroxylase". Journal of Medicinal Chemistry 57, № 6 (2014): 2213–36. http://dx.doi.org/10.1021/jm401603e.

Full text

APA, Harvard, Vancouver, ISO, and other styles

45

Vaz, Frédéric M., Sandy van Gool, Rob Ofman, Lodewijk Ijlst та Ronald J. A. Wanders. "Carnitine Biosynthesis: Identification of the cDNA Encoding Human γ-Butyrobetaine Hydroxylase". Biochemical and Biophysical Research Communications 250, № 2 (1998): 506–10. http://dx.doi.org/10.1006/bbrc.1998.9343.

Full text

APA, Harvard, Vancouver, ISO, and other styles

46

Rydzik, Anna M., Ivanhoe K. H. Leung, Armin Thalhammer, Grazyna T. Kochan, Timothy D. W. Claridge, and Christopher J. Schofield. "ChemInform Abstract: Fluoromethylated Derivatives of Carnitine biosynthesis Intermediates - Synthesis and Applications." ChemInform 45, no. 19 (2014): no. http://dx.doi.org/10.1002/chin.201419047.

Full text

APA, Harvard, Vancouver, ISO, and other styles

47

PAUL, Harbhajan S., Gail SEKAS, and Siamak A. ADIBI. "Carnitine biosynthesis in hepatic peroxisomes. Demonstration of gamma-butyrobetaine hydroxylase activity." European Journal of Biochemistry 203, no. 3 (1992): 599–605. http://dx.doi.org/10.1111/j.1432-1033.1992.tb16589.x.

Full text

APA, Harvard, Vancouver, ISO, and other styles

48

Broderick, Tom L., Frank A. Cusimano, Chelsea Carlson, and Leslie K. Tamura. "Acute Exercise Stimulates Carnitine Biosynthesis and OCTN2 Expression in Mouse Kidney." Kidney and Blood Pressure Research 42, no. 3 (2017): 398–405. http://dx.doi.org/10.1159/000478737.

Full text

APA, Harvard, Vancouver, ISO, and other styles

49

Pierce, Jessica V., Daniel Dignard, Malcolm Whiteway, and Carol A. Kumamoto. "Normal Adaptation of Candida albicans to the Murine Gastrointestinal Tract Requires Efg1p-Dependent Regulation of Metabolic and Host Defense Genes." Eukaryotic Cell 12, no. 1 (2012): 37–49. http://dx.doi.org/10.1128/ec.00236-12.

Full text

Abstract:

ABSTRACTAlthough gastrointestinal colonization by the opportunistic fungal pathogenCandida albicansis generally benign, severe systemic infections are thought to arise due to escape of commensalC. albicansfrom the gastrointestinal (GI) tract. TheC. albicanstranscription factor Efg1p is a major regulator of GI colonization, hyphal morphogenesis, and virulence. The goals of this study were to identify the Efg1p regulon during GI tract colonization and to compareC. albicansgene expression during colonization of different organs of the GI tract. Our results identified significant differences in ge

APA, Harvard, Vancouver, ISO, and other styles

50

Melegh, B., R. Hermann, and I. Bock. "Generation of hydroxytrimethyllysine from trimethyllysine limits the carnitine biosynthesis in premature infants." Acta Paediatrica 85, no. 3 (1996): 345–50. http://dx.doi.org/10.1111/j.1651-2227.1996.tb14030.x.

Full text

APA, Harvard, Vancouver, ISO, and other styles

We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!