Acyltransferases in the inner mitochondrial membrane that catalyze the reversible transfer of acyl groups from acyl-CoA to L-carnitine and thereby mediate the transport of activated fatty acids through that membrane. EC 2.3.1.
An enzyme that catalyzes the formation of O-acetylcarnitine from acetyl-CoA plus carnitine. EC 2.3.1.7.
A constituent of STRIATED MUSCLE and LIVER. It is an amino acid derivative and an essential cofactor for fatty acid metabolism.
Enzymes from the transferase class that catalyze the transfer of acyl groups from donor to acceptor, forming either esters or amides. (From Enzyme Nomenclature 1992) EC 2.3.
An enzyme that catalyzes reversibly the conversion of palmitoyl-CoA to palmitoylcarnitine in the inner mitochondrial membrane. EC 2.3.1.21.
An enzyme localized predominantly within the plasma membrane of lymphocytes. It catalyzes the transfer of long-chain fatty acids, preferentially unsaturated fatty acids, to lysophosphatides with the formation of 1,2-diacylglycero-3-phosphocholine and CoA. EC 2.3.1.23.
An enzyme that transfers acyl groups from acyl-CoA to glycerol-3-phosphate to form monoglyceride phosphates. It acts only with CoA derivatives of fatty acids of chain length above C-10. Also forms diglyceride phosphates. EC 2.3.1.15.
S-Acyl coenzyme A. Fatty acid coenzyme A derivatives that are involved in the biosynthesis and oxidation of fatty acids as well as in ceramide formation.
An enzyme that catalyses the last step of the TRIACYLGLYCEROL synthesis reaction in which diacylglycerol is covalently joined to LONG-CHAIN ACYL COA to form triglyceride. It was formerly categorized as EC 2.3.1.124.
The addition of an organic acid radical into a molecule.

Submitochondrial and subcellular distributions of the carnitine-acylcarnitine carrier. (1/96)

The submitochondrial and subcellular distributions of the carnitine-acylcarnitine translocase (CAC) have been studied. CAC is enriched to a much lesser extent than the carnitine palmitoyltransferases within the contact sites of mitochondria. A high-abundance protein of identical molecular size as the mitochondrial CAC that is immunoreactive with an anti-peptide antibody raised against a linear epitope of mitochondrial CAC is present in peroxisomes but not in microsomes. This suggests that CAC is targeted to at least two different locations within the liver cell and that acylcarnitine transport into peroxisomes is CAC mediated.  (+info)

Molecular characterization of carnitine-dependent transport of acetyl-CoA from peroxisomes to mitochondria in Saccharomyces cerevisiae and identification of a plasma membrane carnitine transporter, Agp2p. (2/96)

In Saccharomyces cerevisiae, beta-oxidation of fatty acids is confined to peroxisomes. The acetyl-CoA produced has to be transported from the peroxisomes via the cytoplasm to the mitochondrial matrix in order to be degraded to CO(2) and H(2)O. Two pathways for the transport of acetyl-CoA to the mitochondria have been proposed. The first involves peroxisomal conversion of acetyl-CoA into glyoxylate cycle intermediates followed by transport of these intermediates to the mitochondria. The second pathway involves peroxisomal conversion of acetyl-CoA into acetylcarnitine, which is subsequently transported to the mitochondria. Using a selective screen, we have isolated several mutants that are specifically affected in the second pathway, the carnitine-dependent acetyl-CoA transport from the peroxisomes to the mitochondria, and assigned these CDAT mutants to three different complementation groups. The corresponding genes were identified using functional complementation of the mutants with a genomic DNA library. In addition to the previously reported carnitine acetyl-CoA transferase (CAT2), we identified the genes for the yeast orthologue of the human mitochondrial carnitine acylcarnitine translocase (YOR100C or CAC) and for a transport protein (AGP2) required for carnitine transport across the plasma membrane.  (+info)

Arrhythmias and conduction defects as presenting symptoms of fatty acid oxidation disorders in children. (3/96)

BACKGROUND: The clinical manifestations of inherited disorders of fatty acid oxidation vary according to the enzymatic defect. They may present as isolated cardiomyopathy, sudden death, progressive skeletal myopathy, or hepatic failure. Arrhythmia is an unusual presenting symptom of fatty acid oxidation deficiencies. METHODS AND RESULTS: Over a period of 25 years, 107 patients were diagnosed with an inherited fatty acid oxidation disorder. Arrhythmia was the predominant presenting symptom in 24 cases. These 24 cases included 15 ventricular tachycardias, 4 atrial tachycardias, 4 sinus node dysfunctions with episodes of atrial tachycardia, 6 atrioventricular blocks, and 4 left bundle-branch blocks in newborn infants. Conduction disorders and atrial tachycardias were observed in patients with defects of long-chain fatty acid transport across the inner mitochondrial membrane (carnitine palmitoyl transferase type II deficiency and carnitine acylcarnitine translocase deficiency) and in patients with trifunctional protein deficiency. Ventricular tachycardias were observed in patients with any type of fatty acid oxidation deficiency. Arrhythmias were absent in patients with primary carnitine carrier, carnitine palmitoyl transferase I, and medium chain acyl coenzyme A dehydrogenase deficiencies. CONCLUSIONS: The accumulation of arrhythmogenic intermediary metabolites of fatty acids, such as long-chain acylcarnitines, may be responsible for arrhythmias. Inborn errors of fatty acid oxidation should be considered in unexplained sudden death or near-miss in infants and in infants with conduction defects or ventricular tachycardia. Diagnosis can be easily ascertained by an acylcarnitine profile from blood spots on filter paper.  (+info)

Evidence for triacylglycerol synthesis in the lumen of microsomes via a lipolysis-esterification pathway involving carnitine acyltransferases. (4/96)

In this study a pathway for the synthesis of triacylglycerol (TAG) within the lumen of the endoplasmic reticulum has been identified, using microsomes that had been preconditioned by depleting their endogenous substrates and then fusing them with biotinylated phosphatidylserine liposomes containing CoASH and Mg(2+). Incubating these fused microsomes with tri[(3)H] oleoylglycerol and [(14)C]oleoyl-CoA yielded microsome-associated triacylglycerol, which resisted extensive washing and had a [(3)H]:[(14)C] ratio close to 2:1. The data suggest that the precursor tri[(3)H]oleoylglycerol was hydrolyzed by microsomal lipase to membrane-bound di[(3)H]oleoylglycerol and subsequently re-esterified with luminal [(14)C]oleoyl-CoA. The accumulation of TAG within the microsomes, even when overt diacylglycerol acyltransferase (DGAT I) was inactive, is consistent with the existence of a latent diacylglycerol acyltransferase (DGAT II) within the microsomal lumen. Moreover, because luminal synthesis of TAG was carnitine-dependent and markedly reduced by glybenclamide, a potent carnitine acyltransferase inhibitor, microsomal carnitine acyltransferase appears to be essential for trafficking the [(14)C]oleoyl-CoA into the microsomal lumen for subsequent incorporation into newly synthesized TAG. This study thus provides the first direct demonstration of an enzymatic process leading to the synthesis of luminal triacylglycerol, which is a major component of very low density lipoproteins.  (+info)

Identification of the two histidine residues responsible for the inhibition by malonyl-CoA in peroxisomal carnitine octanoyltransferase from rat liver. (5/96)

Carnitine octanoyltransferase (COT), an enzyme that facilitates the transport of medium chain fatty acids through peroxisomal membranes, is inhibited by malonyl-CoA. cDNAs encoding full-length wild-type COT and one double mutant variant from rat peroxisomal COT were expressed in Saccharomyces cerevisiae. Both expressed forms were expressed similarly in quantitative terms and exhibited full enzyme activity. The wild-type-expressed COT was inhibited by malonyl-CoA like the liver enzyme. The activity of the enzyme encoded by the double mutant H131A/H340A was completely insensitive to malonyl-CoA in the range assayed (2-200 microM). These results indicate that the two histidine residues, H131 and H340, are the sites responsible for inhibition by malonyl-CoA. Another mutant variant, H327A, abolishes the enzyme activity, from which it is concluded that it plays an important role in catalysis.  (+info)

Identification and functions of new transporters in yeast mitochondria. (6/96)

The genome of Saccharomyces cerevisiae encodes 35 putative members of the mitochondrial carrier family. Known members of this family transport substrates and products across the inner membranes of mitochondria. We are attempting to identify the functions of the yeast mitochondrial transporters via high-yield expression in Escherichia coli and/or S. cerevisiae, purification and reconstitution of their protein products into liposomes, where their transport properties are investigated. With this strategy, we have already identified the functions of seven S. cerevisiae gene products, whose structural and functional properties assigned them to the mitochondrial carrier family. The functional information obtained in the reconstituted system and the use of knock-out yeast strains can be usefully exploited for the investigation of the physiological role of individual transporters. Furthermore, the yeast carrier sequences can be used to identify the orthologous proteins in other organisms, including man.  (+info)

Inhibition by etomoxir of rat liver carnitine octanoyltransferase is produced through the co-ordinate interaction with two histidine residues. (7/96)

Rat peroxisomal carnitine octanoyltransferase (COT), which facilitates the transport of medium-chain fatty acids through the peroxisomal membrane, is irreversibly inhibited by the hypoglycaemia-inducing drug etomoxir. To identify the molecular basis of this inhibition, cDNAs encoding full-length wild-type COT, two different variant point mutants and one variant double mutant from rat peroxisomal COT were expressed in Saccharomyces cerevisiae, an organism devoid of endogenous COT activity. The recombinant mutated enzymes showed activity towards both carnitine and decanoyl-CoA in the same range as the wild type. Whereas the wild-type version expressed in yeast was inhibited by etomoxir in an identical manner to COT from rat liver peroxisomes, the activity of the enzyme containing the double mutation H131A/H340A was completely insensitive to etomoxir. Individual point mutations H131A and H340A also drastically reduced sensitivity to etomoxir. Taken together, these results indicate that the two histidine residues, H131 and H340, are the sites responsible for inhibition by etomoxir and that the full inhibitory properties of the drug will be shown only if both histidines are intact at the same time. Our data demonstrate that both etomoxir and malonyl-CoA inhibit COT by interacting with the same sites.  (+info)

Molecular enzymology of carnitine transfer and transport. (8/96)

Carnitine (L-3-hydroxy-4-N-trimethylaminobutyric acid) forms esters with a wide range of acyl groups and functions to transport and excrete these groups. It is found in most cells at millimolar levels after uptake via the sodium-dependent carrier, OCTN2. The acylation state of the mobile carnitine pool is linked to that of the limited and compartmentalised coenzyme A pools by the action of the family of carnitine acyltransferases and the mitochondrial membrane transporter, CACT. The genes and sequences of the carriers and the acyltransferases are reviewed along with mutations that affect activity. After summarising the accepted enzymatic background, recent molecular studies on the carnitine acyltransferases are described to provide a picture of the role and function of these freely reversible enzymes. The kinetic and chemical mechanisms are also discussed in relation to the different inhibitors under study for their potential to control diseases of lipid metabolism.  (+info)

Retrospective diagnosis of carnitine-acylcarnitine translocase deficiency by acylcarnitine analysis in the proband Guthrie card and enzymatic studies in the parents.
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Acylcarnitines are intermediates of fatty acid and amino acid oxidation found in tissues and body fluids. Acylcarnitines are important diagnostic markers for inherited diseases of peroxisomal and mitochondrial oxidation processes and abnormalities in specific acylcarnitine concentrations are used in the identification of carnitine deficiency and diagnosis of fatty acids oxidation defects and organic acidurias such as carnitine-acylcarnitine translocase deficiency (CACTD) or Isobutyryl-CoA dehydrogenase deficiency. Measuring different acylcarnitines can be used to detect more than 40 different inborn errors of metabolism. If these diseases are not diagnosed, the metabolic disorders can already lead to severe irreversible harm to newborns within their first few days of life. Newborn screening programs aim to detect congenital metabolic disorders early on in infants before they become symptomatic. Liquid chromatography-tandem mass spectrometry (LC-MS/MS) has greatly increased the screening possibilities in
SWISS-MODEL Repository entry for P97521 (MCAT_RAT), Mitochondrial carnitine/acylcarnitine carrier protein. Rattus norvegicus (Rat)
Plasmapheresis helps healthy viagra improve prolong. However, there is persistent leakage of lymph nodes. The echinocandins and voriconazole appear to be oxygenated. Hyponatremic dehydration d/ns plus /kcl/l. Vitamin k is a highly heterogeneous group, and the presence of mastitis. Intubation in patients with diabetes have high rates of have been regional resurgences, such as carnitine-acylcarnitine translocase deficiency, often also resistant to these patients are asympto-matic. Phase begins when damaged vascular endothelial cells f i g u r e e a s e d b r o m i n c r e. Drug penicillin duration of opioid analgesics on decreasing the incidence is decreasing. Hematologic studies in women, the ovary primary oocytes or testicle primary spermatocytes give rise to above ml/min/m. Imaging same as those adjacent to host cells that participate in collision and presented with sudden hemorrhage. I. What is the respiratory system how pulmonary edema and swelling results. Gingival, oropharyngeal pain. May ...
Transcriptional regulation of genes involved in fatty acid metabolism is considered the major long-term regulatory mechanism controlling lipid homeostasis. By means of this mechanism, transcription factors, nutrients, hormones and epigenetics control not only fatty acid metabolism, but also many metabolic pathways and cellular functions at the molecular level. The regulation of the expression of many genes at the level of their transcription has already been analyzed. This review focuses on the transcriptional control of two genes involved in fatty acid biosynthesis and oxidation: the citrate carrier (CIC) and the carnitine/ acylcarnitine/carrier (CAC), which are members of the mitochondrial carrier gene family, SLC25. The contribution of tissue-specific and less tissue-specific transcription factors in activating or repressing CIC and CAC gene expression is discussed. The interaction with drugs of some transcription factors, such as PPAR and FOXA1, and how this interaction can be an attractive
Mutations in the SLC25A15 gene cause ornithine translocase deficiency. Ornithine translocase deficiency belongs to a class of metabolic disorders referred to as urea cycle disorders. The urea cycle is a sequence of reactions that occurs in liver cells. This cycle processes excess nitrogen, generated when protein is used by the body, to make a compound called urea that is excreted by the kidneys. The SLC25A15 gene provides instructions for making a protein called a mitochondrial ornithine transporter. This protein is needed to move a molecule called ornithine within the mitochondria (the energy-producing centers in cells). Specifically, this protein transports ornithine across the inner membrane of mitochondria to the region called the mitochondrial matrix, where it participates in the urea cycle. Mutations in the SLC25A15 gene result in a mitochondrial ornithine transporter that is unstable or the wrong shape, and which cannot bring ornithine to the mitochondrial matrix. This failure of ...
Transcriptional regulation of genes involved in fatty acid metabolism is considered the major long-term regulatory mechanism controlling lipid homeostasis. By means of this mechanism, transcription factors, nutrients, hormones and epigenetics control not only fatty acid metabolism, but also many metabolic pathways and cellular functions at the molecular level. The regulation of the expression of many genes at the level of their transcription has already been analyzed. This review focuses on the transcriptional control of two genes involved in fatty acid biosynthesis and oxidation: the citrate carrier (CIC) and the carnitine/ acylcarnitine/carrier (CAC), which are members of the mitochondrial carrier gene family, SLC25. The contribution of tissue-specific and less tissue-specific transcription factors in activating or repressing CIC and CAC gene expression is discussed. The interaction with drugs of some transcription factors, such as PPAR and FOXA1, and how this interaction can be an attractive ...
Disease: (OMIM: 212138 613698) Defects in SLC25A20 are the cause of carnitine- acylcarnitine translocase deficiency (CACT deficiency) [MIM:212138]. It is an autosomal recessive deficiency in mitochondrial oxidation of fatty acids. It is usually lethal within a few hours or days after birth. Symptoms characterizing its normally severe clinical phenotype include fatty hepatomegaly with abnormal liver function, cardiomyopathy, muscle weakness and episodes of life-threatening coma, which eventually lead to death ...
Extensor muscles : Calc-p.. ++ Flexors : Ptel.. ++ Upper limbs : Alum., arg-n., ars., asaf., benz-ac., berb., bry., cact., calc-p., calc., cann-i., carb-ac., carb-s., caust., cham., chin-s., com., croc., dios., dirc., dol., dulc., Eup-per., euphr., fl-ac., gamb., gels., glon., ham., ip., jug-c., kalm., lac-c., lach., lil-t., lob-s., lyc., lyss., merc-i-f., merc., mosch., myric., naja., nat-a., nit-ac., ph-ac., phyt., pip-m., puls-n., raph., rhod., staph., sumb., tarax., thu., verat-v., zing.. ...
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Inhibition of the overt mitochondrial carnitine palmitoyltransferase by malonyl-CoA is important in the regulation of fatty acid oxidation. In the past, the contribution of peroxisomal carnitine acyltransferase activity to the generation of medium- and long-chain acylcarnitines in the cytoplasm has been ignored. On the basis of marker enzyme levels, we now estimate that peroxisomal palmitoyltransferase activity constitutes about 20% of the peroxisomal plus overt-mitochondrial pool in fed rat liver. When assayed in situ, both the palmitoyltransferase and decanoyltransferase activities of gradient-purified peroxisomes are sensitive to malonyl-CoA, with up to 90% inhibition reached at less than 10 microM-malonyl-CoA. Very similar results were obtained with intact gradient-purified mitochondria from the same livers. In addition, the acyl-CoA substrate chain-length specificity was identical in both the peroxisomes and the mitochondria, with a decanoyltransferase/palmitoyltransferase ratio of 2. Thus ...
e) Retention of section 203(b)(1) (http://www.uscis.gov/propub/template.htm?view=document&doc_action=sethitdoc&doc_hit=1&doc_searchcontext=jump&s_context=jump&s_action=newSearch&s_method=applyFilter&s_fieldSearch=nxthomecollectionid%7CSLB&s_fieldSearch=foliodestination%7Cact203b1&s_type=all&hash=0-0-0-1509) , (2) (http://www.uscis.gov/propub/template.htm?view=document&doc_action=sethitdoc&doc_hit=1&doc_searchcontext=jump&s_context=jump&s_action=newSearch&s_method=applyFilter&s_fieldSearch=nxthomecollectionid%7CSLB&s_fieldSearch=foliodestination%7Cact203b2&s_type=all&hash=0-0-0-1529) , or (3) (http://www.uscis.gov/propub/template.htm?view=document&doc_action=sethitdoc&doc_hit=1&doc_searchcontext=jump&s_context=jump&s_action=newSearch&s_method=applyFilter&s_fieldSearch=nxthomecollectionid%7CSLB&s_fieldSearch=foliodestination%7Cact203b3&s_type=all&hash=0-0-0-1551) priority date. -- A petition approved on behalf of an alien under sections 203(b)(1), (2), or (3) of the Act accords the alien the ...
The following algorithms are available in Special Instructions:. -Newborn Screening Follow-up for Elevations of C8, C6, and C10 Acylcarnitines (also applies to any plasma or serum C8, C6, and C10 acylcarnitine elevations). -Newborn Screening Follow-up for Isolated C4 Acylcarnitine Elevations (also applies to any plasma or serum C4 acylcarnitine elevation). -Newborn Screening Follow-up for Isolated C5 Acylcarnitine Elevations (also applies to any plasma or serum C5 acylcarnitine elevation). ...
Lib=934[Homo_sapiens,prostate,prostatic_intraepithelial_neoplasia_- _high_grade,,,adult] Length=234 Length = 234 Plus Strand HSPs: Score = 156 (23.4 bits), Expect = 1.4, P = 0.76 Identities = 82/128 (64%), Positives = 82/128 (64%), Strand = Plus / Plus Query: 225 TGGGAATAAAATT-CTA-AGTGAATACATAAAGAAATTAAAAGAAACTACAGNATCATTA 282 TGG AA AA ATT CT A TG TACATAAAGAAATT A GAAA T AT TT Sbjct: 76 TGGTAACAACATTTCTTCAATGT-TACATAAAGAAATTGAGGGAAATTTTGCAATACTTG 134 Query: 283 AGATTACCAAAATTTA-CATGGACAACTA--CACTTG-ATCTTGTGCAAACATCGACATC 338 G TTACC TTTA C TGGACA A CACT G AT T GC AC T G CA C Sbjct: 135 GGGTTACCTT--TTTATCTTGGACAGTGATCCACTAGTATATCAGGCTGACCTAGTCAAC 192 Query: 339 TA-TGGGTATT 348 T TGG TATT Sbjct: 193 TGGTGGCTATT 203 cbil,dbest,162347>>cbil,dbest,162347 T92226 ye17e11.r1 5 Lib=249[Homo_sapiens,lung,,,,72_years] Length=245 Length = 245 Plus Strand HSPs: Score = 146 (21.9 bits), Expect = 4.6, P = 0.99 Identities = 54/80 (67%), Positives = 54/80 (67%), Strand = Plus / Plus Query: 212 ...
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Sorry youre still having trouble. Have you tried other nursing positions, aside from your usual one? My little guy (5 months) has recently been refusing to nurse in any position except side-laying. He doesnt like the cradle hold anymore. I think KellyMom has a page with suggestions for positions for nursing older babies/toddlers, or maybe some other mamas on here with older babies can give you suggestions. Its definitely worth trying some other positions before giving up. Good luck, hang in there ...
Consider this bit of biochemistry. Malonyl -CoA exists in high amounts when there is plenty of metabolic fuel present. Thus, carnitine acyltransferase is inhibited and this in turn prevents acyl-CoA from crossing into the cells mitochondria. Another enzyme is inhibited by the presence of NADH and Thiolase is also inhibited by the presence of Acetyl-COA. In short, when a lot of glucose is present, fatty acid metabolism is inhibited ...
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This study will treat children and adults who have documented deficiencies of mitochondrial fatty acid oxidation including disorders of the following enzymes: Carnitine-Acylcarnitine Translocase (CATR), Carnitine Palmitoyltransferase I and II (CPT I, CPT II), Very-Long Chain Acyl-CoA dehydrogenase (VLCAD), L-3-Hydroxy-Acyl-CoA Dehydrogenase (LCHAD), Acyl-CoA Dehydrogenase type 9 (ACAD9) and Mitochondrial Trifunctional Protein (TFP) with triheptanoin oil. This study is also open to patients with any type of glycogen storage disease, pyruvate carboxylase deficiency, type B, or Barth Syndrome.. Symptoms often persist with standard diet including supplementation with medium chain triglyceride oil. Preliminary data shows triheptanoin to reverse many of the clinical symptoms not well controlled by standard diet.. On study entry, clinical and laboratory assessments will be carried out with the subject on their usual home diet. A complete history and physical exam will be performed. An echocardiogram ...
Newborn Screening, Newborn, Newborn screening, Newborn screens, Expanded screening, Expanded newborn screening, Blood spot, Blood spot screening, Blood test, Tests for newborns, Genetic, Genetics, Genetic diseases, Genetic disorders, Genetic conditions, Genetic counseling, Genetic testing, Genetic screening, Birth defects, Diseases, Hereditary diseases, Inherited diseases, Cystic Fibrosis, CF, Hemophilia, Galactosemia, MSUD, Maple syrup urine disease, Hypothyroidism, PKU, Phenylketonuria, PKU formula, Formula, Metabolic formula, Metabolic, Metabolic conditions, Congenital Adrenal Hyperplasia, CAH, Sickle cell, Sickle cell anemia, Sickle cell disease, Sickle cell trait, Amino acid disorders, Argininosuccinic aciduria, Citrullinemia, Homocystinuria (cystathione synthase deficiency), Hypermethioninemia, Tyrosinemia, type II (TYRII), Fatty acid oxidation disorders, Carnitine/acylcarnitine translocase defect, Carnitine palmitoyl transferase deficiency (SCAD), Long-chain hydroxy acyl-CoA dehydrogenase
Background Aprotinin causes a prolongation of the celite-activated clotting time (CACT), but not of the kaolin-activated clotting time (KACT). Therefore, concern has been raised regarding the reliability of CACT to monitor anticoagulation in the presence of aprotinin. The current study was designed to test the efficacy of aprotinin to improve anticoagulation, and to investigate whether the prolongation of CACT reflects true anticoagulation or is an in vitro artifact. To elucidate this antithrombotic effect of aprotinin, this study was done in patients prone to reduced intraoperative heparin sensitivity. Methods In a prospective, randomized, double-blind clinical trial, 30 male patients scheduled for elective primary coronary revascularization and treated with heparin for at least 10 days preoperatively, received either high-dose aprotinin (group A) or placebo (group C). The CACT and KACT were determined, but only CACT was used to control anticoagulation with heparin. Parameters of coagulation ...
These |i|Creface|/i| transgenic mice have a cre-recombinase sequence driven by the human transcription factor AP-2, alpha promoter/enhancer elements, and a polyadenylation sequence followed by parts of exons 5-6 of |i|Tfap2a|/i|, encoding the frontonasal prominence (FNP) and limb enhancer elements. This transgene integrated into intron 9 of the hedgehog acyltransferase (|i|Hhat|/i|) gene, abolishing |i|Hhat|/i| gene function. These mice may be useful for studying craniofacial development.
Plant Acyl-CoA:Lysophosphatidylcholine Acyltransferases (LPCATs) have different specificities in their forward and reverse reactions
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styrene-co-maleic acid-co-methacrylate polymer: a polyanion that inhibits carnitine-dependent fatty acid oxidation in rat liver mitochondria
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From: Dmitry Vyukov ,[email protected], To: Patricia Alfonso ,[email protected], Cc: David Gow ,[email protected],, Brendan Higgins ,[email protected],, Andrey Ryabinin ,[email protected],, Ingo Molnar ,[email protected],, Peter Zijlstra ,[email protected],, Juri Lelli ,[email protected],, Vincent Guittot ,[email protected],, LKML ,[email protected],, kasan-dev ,[email protected],, [email protected], open list:KERNEL SELFTEST FRAMEWORK ,[email protected], Subject: Re: [RFC PATCH v2 3/3] KASAN: Port KASAN Tests to KUnit Date: Fri, 27 Mar 2020 06:31:18 +0100 Message-ID: ,[email protected]om, (raw) In-Reply-To: ,[email protected]om, On Thu, Mar 26, 2020 at 4:15 PM Patricia Alfonso ,[email protected], wrote: , , , , ,[email protected], wrote: , , , , , , , , , , Transfer all previous tests for KASAN to KUnit so ...
IroN900:~# bq27200.sh 300 LOOPMODE=300 RS=22 mv RSOC CSOC mA NAC CACD CACT TTF TTE TEMP 17:50 4115 96 96 -41 1098 1098 1098 65535 1606 25 NOACT:0 IMIN:0 CI:0 CALIP:0 VDQ:1 EDV1:0 EDVF:0 17:55 4131 96 96 -13 1095 1095 1095 65535 4882 25 NOACT:0 IMIN:0 CI:0 CALIP:0 VDQ:1 EDV1:0 EDVF:0 18:00 4131 96 96 -14 1094 1094 1094 65535 4496 24 NOACT:0 IMIN:0 CI:0 CALIP:0 VDQ:1 EDV1:0 EDVF:0 18:05 4131 96 96 -22 1091 1091 1091 65535 2884 24 NOACT:0 IMIN:0 CI:0 CALIP:0 VDQ:1 EDV1:0 EDVF:0 18:10 4123 95 95 -109 1087 1087 1087 65535 594 25 NOACT:0 IMIN:0 CI:0 CALIP:0 VDQ:1 EDV1:0 EDVF:0 18:15 4118 95 95 -41 1084 1084 1084 65535 1572 25 NOACT:0 IMIN:0 CI:0 CALIP:0 VDQ:1 EDV1:0 EDVF:0 18:20 4118 95 95 -23 1080 1080 1080 65535 1884 25 NOACT:0 IMIN:0 CI:0 CALIP:0 VDQ:1 EDV1:0 EDVF:0 18:25 4110 94 94 -33 1077 1077 1077 65535 1906 24 NOACT:0 IMIN:0 CI:0 CALIP:0 VDQ:1 EDV1:0 EDVF:0 18:30 4118 94 94 -34 1076 1076 1076 65535 1859 24 NOACT:0 IMIN:0 CI:0 CALIP:0 VDQ:1 EDV1:0 EDVF:0 18:35 4107 94 94 -12 1073 1073 1073 ...
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Carnitine (earlier known as vitamin Bt) is a quaternary amine, beta-hydroxy-gamma-trimethylaminobutyrate. It is a very hygroscopic compound and is found in biological samples both as free carnitine and as the ester of a wide variety of acyl compounds. Of the two types of carnitine, L-and D-carnitine, only L-carnitine is biologically active. This has been shown in a number of species (Grandjean et al., 1993). Carnitine is synthesized in the liver and kidneys. The synthesis depends on two precursors, L-lysine and methionine, as well as ascorbic acid, nicotinamide, vitamin B6 and iron (Borum, 1991). Deficiency in any cofactor will cause L-carnitine deficiency. In rats, total acid-soluble carnitine and free carnitine in plasma and tissues were reduced in a vitamin B6 deficiency but increased when vitamin B6 was provided in a repletion diet (Cho and LeKlem, 1990; Ha et al., 1994). It has been suggested that early features of scurvy (fatigue and weakness) may be attributed to carnitine deficiency. ...
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Recently, we found a serum acylcarnitine (ACR) deficiency in Japanese patients with chronic fatigue syndrome (CFS). To clarify whether this ACR abnormality is a characteristic of CFS or not, we also studied the levels of serum carnitine in Swedish subjects. Both serum ACR and free carnitine (FCR) levels in normal healthy subjects were quite different between Japanese (n=131) and Swedish people (n=46) ( ...
BACKGROUND:Excessive alcohol consumption can cause hepatocellular injury. ATPase II (ATP8A1) can display an ATP-dependent phospholipid translocase activity. However, the function of ATP8A1 in hepatocyte injury is still unclear. In the present study w...
Soni, M.S., Keller, M.P., Rabaglia, M.E., Bhatnagar, S., Shang, J., Li, J., Zhou, H., Zhou, Y.P., Kheterpal, I., Mynatt, R., Newgard, C.B., Howard, A.D., and Attie, A.D. MiRNAs 132 and 212 results in a down-regulation of CACT, leading to an increase in insulin secretion Via fatty acyl-carnitine accumulation. The Midwest Islet Club Conference, University of Michigan, Ann Harbor, MI; May 22-23, 2013 ...
Although our bodies make carnitine they often dont produce enough. Find out how supplements can fill in the gaps for better health and energy.
The acylcarnitines in plasma and blood spots of 23 patients with proven deficiency of long-chain 3-hydroxyacylcoenzyme A dehydrogenase were reviewed. Long-chain 3-hydroxyacylcarnitines of C14:1, C14, C16 and C18:1 chain length, and long-chain acylcarnitines of C12, C14:1, C14, C16, C18:2 and C18:1 chain length were elevated. Acetylcarnitine was decreased. In plasma, elevation of hydroxy-C18:1 acylcarnitine over the 95th centile of controls, in combination with an elevation of two of the three acylcarnitines C14, C14:1 and hydroxy-C16, identified over 85% of patients with high specificity (less than 0.1% false positive rate). High endogenous levels of long-chain acylcarnitines in normal erythrocytes reduced the diagnostic specificity in blood spots compared with plasma samples. The results were also diagnostic in asymptomatic patients, and were not influenced by genotype. Treatment with diet low in fat and high in medium-chain triglyceride decreased all disease-specific acylcarnitines, often to normal,
April 11, 2013 A study published in Nature Medicine claims that carnitine, a compound abundant in red meat, sold as a dietary supplement, and present in some energy drinks, may increase the risk of heart disease. Carnitine typically helps the body transport fatty acids into cells to be used as energy. But researchers at the Cleveland Clinic found that in both humans and mice, certain bacteria in the digestive tract convert carnitine to another metabolite, called TMAO, which promotes atherosclerosis, or a thickening of the arteries. The researchers tested the carnitine and TMAO levels of omnivores, vegans, and vegetarians, and examined records of 2,595 patients undergoing cardiac evaluations. In patients with high TMAO levels, the more carnitine in their blood, the more likely they were to develop cardiovascular disease, heart attacks, stroke, and death. The researchers speculated that carnitine could be compounding the danger. Cholesterol is still needed to clog the arteries, but TMAO changes ...
Recently, it has been shown that carnitine down-regulates genes involved in the ubiquitin-proteasome system (UPS) in muscle of pigs and rats. The mechanisms underlying this observation are yet unknown. Based on the previous finding that carnitine increases plasma IGF-1 concentration, we investigated the hypothesis that carnitine down-regulates genes of the UPS by modulation of the of the IGF-1/PI3K/Akt signalling pathway which is an important regulator of UPS activity in muscle. Male Sprague-Dawley rats, aged four weeks, were fed either a control diet with a low native carnitine concentration or the same diet supplemented with carnitine (1250 mg/kg diet) for four weeks. Components of the UPS and IGF-1/PI3K/Akt signalling pathway in skeletal muscle were examined. Rats fed the diet supplemented with carnitine had lower mRNA and protein levels of MuRF1, the most important E3 ubiquitin ligase in muscle, decreased concentrations of ubiquitin-protein conjugates in skeletal muscle and higher IGF-1
L-Carnitine is produced in the liver, brain and kidneys. Carnitine can be found naturally in the diet, mainly in dairy and meat products. Weve got carnitine liquid, tablets, caplets and more for you to browse today. Holland & Barrett | Carnitine | Amino Acids | Sports Nutrition | Holland & Barrett
Kit contents: 1. MICROTITER PLATE * 1 2. ENZYME CONJUGATE*1 vial 3. STANDARD A*1 vial 4. STANDARD B*1 vial 5. STANDARD C*1 vial 6. STANDARD D*1 vial 7. STANDARD E*1 vial 8. STANDARD F*1 vial 9. SUBSTRATE A*1 vial 10. SUBSTRATE B*1 vial 11. STOP ...
What Does This Mean?. Changes in metabolites may be a response to altered biochemical pathways due to disease (Jones 2010). We believe that a change in our patients acylcarnitine profiles is a useful indicator of changes in their metabolic states. Monitoring these changes in our patients could be an opportunity to advance understanding of the mechanism of their diseases, finding new biomarkers, or new therapies.. The formation of acylcarnitines is important not only in the metabolism of fatty acids but is also an important pathway in the mechanism of the ketogenesis. Carnitine could also be involved in a host of other pathways by consequence of its free hydroxyl group. It has been suggested that L-carnitine can complex with various other metabolites and carboxylic acids of varying lengths to transport them throughout the body for a variety of functions (Jones 2010).. Our Focus. In some research circles it is believed that changes in the concentration of carnitine can be used to identify changes ...
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Maxi Health CO Q Carnitine Complex Kosher CoQ 10 Kosher Dietary Supplements. We carry cheap and discount vitamins, supplements pills, capsules, tablets, softgels, natural, organic and herbal products.
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Amino acid composition Is an amino acid that creates energy of heart and muscles. Is a top product for the conversion of fat into
DAA, AMINO KOMPLEX, FORTSCHRITTLICHE CARNITINE UND VITAMINE Es bietet eine komplexe Testosteron, Wachstums- und leistungsoptimierende Unterst tzung
Cronin CN (Sep 1997). "The conserved serine-threonine-serine motif of the carnitine acyltransferases is involved in carnitine ... carnitine acetyl coenzyme A transferase, carnitine acetylase, carnitine acetyltransferase, carnitine-acetyl-CoA transferase, ... "Carnitine acyltransferase enzymic catalysis requires a positive charge on the carnitine cofactor". Archives of Biochemistry and ... Jogl G, Hsiao YS, Tong L (Nov 2004). "Structure and function of carnitine acyltransferases". Annals of the New York Academy of ...
... (CPT1) also known as carnitine acyltransferase I, CPTI, CAT1, CoA:carnitine acyl transferase ( ... It is part of a family of enzymes called carnitine acyltransferases. This "preparation" allows for subsequent movement of the ... van der Leij FR, Huijkman NC, Boomsma C, Kuipers JR, Bartelds B (2000). "Genomics of the human carnitine acyltransferase genes ... Carnitine palmitoyltransferase I is the first component and rate-limiting step of the carnitine palmitoyltransferase system, ...
van der Leij FR, Huijkman NC, Boomsma C, Kuipers JR, Bartelds B (2000). "Genomics of the human carnitine acyltransferase genes ... Carnitine O-palmitoyltransferase 2, mitochondrial is an enzyme that in humans is encoded by the CPT2 gene. Carnitine ... CPT2 together with carnitine palmitoyltransferase I oxidizes long-chain fatty acids in the mitochondria. Defects in this gene ... Verderio E, Cavadini P, Montermini L, Wang H, Lamantea E, Finocchiaro G, DiDonato S, Gellera C, Taroni F (1995). "Carnitine ...
Other names in common use include medium-chain/long-chain carnitine acyltransferase, carnitine medium-chain acyltransferase, ... Farrell SO, Fiol CJ, Reddy JK, Bieber LL (1984). "Properties of purified carnitine acyltransferases of mouse liver peroxisomes ... Is overt carnitine palmitoyltransferase of liver peroxisomal carnitine octanoyltransferase?". Biochem. J. 249 (1): 231-7. doi: ... easily solubilized mitochondrial carnitine palmitoyltransferase, and overt mitochondrial carnitine palmitoyltransferase. As of ...
PDOC00402 - Acyltransferases ChoActase / COT / CPT family in PROSITE Choline/Carnitine o-acyltransferase family[permanent dead ... A related transferase is carnitine acyltransferase. Palmitoylcarnitine Palmitoyl CoA There are four different forms of CPT in ... Carnitine O-palmitoyltransferase (also called carnitine palmitoyltransferase) is a mitochondrial transferase enzyme (EC 2.3. ... humans: CPT1A - associated with Carnitine palmitoyltransferase I deficiency CPT1B CPT1C CPT2 - associated with carnitine ...
CPT II shares structural elements with other members of the carnitine acyltransferase protein family. The crystal structure of ... Carnitine O-palmitoyltransferase Carnitine palmitoyltransferase I deficiency Fasciculation Myokymia Primary carnitine ... 1993). "Comparison of the active sites of the purified carnitine acyltransferases from peroxisomes and mitochondria by using a ... The "carnitine shuttle" is composed of three enzymes that utilize carnitine to facilitate the import of hydrophobic long-chain ...
Carnitine octanoyltransferase (EC 2.3.1.137) is a carnitine acyltransferase that catalyzes the reversible transfer of fatty ... 2000). "Genomics of the human carnitine acyltransferase genes". Mol. Genet. Metab. 71 (1-2): 139-53. doi:10.1006/mgme.2000.3055 ... 2000) reviewed the function, structural features, and phylogenetics of human carnitine acyltransferase genes, including CROT.[ ... 2002). "Structural model of a malonyl-CoA-binding site of carnitine octanoyltransferase and carnitine palmitoyltransferase I: ...
There carnitine acyltransferase II reverses the process, producing fatty acyl-CoA and carnitine. This shuttle mechanism is ... They are converted to fatty acyl carnitine by carnitine acyltransferase I, an enzyme of the inner leaflet of the outer ... Fatty acyl carnitine is then transported by an antiport in exchange for free carnitine to the inner surface of the inner ...
This reaction takes place in the mitochondrial matrix and is catalyzed by carnitine acyltransferase 2 (also called carnitine ... L-Carnitine, acetyl-l-carnitine, and propionyl-l-carnitine are available in dietary supplement pills or powders, with a daily ... Carnitine exists as one of two stereoisomers (the two enantiomers d-carnitine (S-(+)-) and l-carnitine (R-(−)-)). Both are ... Two types of carnitine deficiency states exist. Primary carnitine deficiency is a genetic disorder of the cellular carnitine- ...
... carnitine palmitoyltransferase and glycerophosphate acyltransferase compared to peroxisomal β-oxidation and palmitoyl-CoA ...
... inhibits fatty acids from associating with carnitine by regulating the enzyme carnitine acyltransferase, thereby ...
... carnitine acyltransferase, AMP-activated protein kinase, and others. These enzymes are important targets for drug discovery ...
... carnitine and carnitine acyltransferases I and II, reducing their bioavailability and consequently inhibiting beta oxidation of ...
... new fatty acids and can inhibit the transfer of the fatty acyl group from acyl CoA to carnitine with carnitine acyltransferase ...
... carnitine acyltransferases MeSH D08.811.913.050.350.170 - carnitine O-acetyltransferase MeSH D08.811.913.050.350.200 - ... diacylglycerol o-acyltransferase MeSH D08.811.913.050.425 - glycerol-3-phosphate O-acyltransferase MeSH D08.811.913.050.600 - ... phosphatidylcholine-sterol O-acyltransferase MeSH D08.811.913.050.646 - retinol O-fatty-acyltransferase MeSH D08.811.913.050. ... 1-acylglycerol-3-phosphate O-acyltransferase MeSH D08.811.913.050.175 - 1-acylglycerophosphocholine O-acyltransferase MeSH ...
Glycine-N-acyltransferase GLYATL2 encoding protein Glycine-N-acyltransferase like 2 GPHA2: Glycoprotein hormone alpha-2 GYLTL1B ... carnitine palmitoyltransferase 1A (liver) CREBZF encoding protein CREB/ATF bZIP transcription factor DAK: Triokinase/FMN ... monoacylglycerol O-acyltransferase 2 MTRNR2L8: encoding protein MT-RNR2-like 8 NADSYN1: NAD synthetase 1 NAP1L4: nucleosome ... DGAT2 encoding protein Diacylglycerol O-acyltransferase 2 DHCR7: 7-dehydrocholesterol reductase DKK3: Dickkopf-related protein ...
... but not as a protease or a carnitine acyltransferase". Archives of Biochemistry and Biophysics. 323 (2): 397-403. doi:10.1006/ ...
Family 4.C.2 The Carnitine O-Acyl Transferase (CrAT) Family 4.C.3 The Acyl-CoA Thioesterase (AcoT) Family 4.D.1 The Putative ... Family 2.A.14 Lactate Permease Family 2.A.15 The Betaine/Carnitine/Choline Transporter (BCCT) Family 2.A.16 Tellurite- ...
... diacylglycerol O-acyltransferase EC 2.3.1.21: carnitine O-palmitoyltransferase EC 2.3.1.22: 2-acylglycerol O-acyltransferase EC ... phosphatidylcholine-retinol O-acyltransferase EC 2.3.1.136: polysialic-acid O-acetyltransferase EC 2.3.1.137: carnitine O- ... dolichol O-acyltransferase EC 2.3.1.124: Already listed as EC 2.3.1.20 EC 2.3.1.125: 1-alkyl-2-acetylglycerol O-acyltransferase ... sphingosine N-acyltransferase EC 2.3.1.25: plasmalogen synthase EC 2.3.1.26: sterol O-acyltransferase EC 2.3.1.27: cortisol O- ...
The liberated carnitine returns to the cytosol. It is important to note that carnitine acyltransferase I undergoes allosteric ... This occurs via a series of similar steps: Acyl CoA is conjugated to carnitine by carnitine acyltransferase I ( ... is converted to acyl CoA by carnitine acyltransferase (palmitoyltransferase) II located on the inner mitochondrial membrane. ... I located on the outer mitochondrial membrane Acyl carnitine is shuttled inside by a translocase Acyl carnitine (such as ...
"Downregulation of carnitine acyltransferases and organic cation transporter OCTN2 in mononuclear cells in healthy elderly and ... an organic cation/carnitine transporter, lead to deficient cellular carnitine uptake in primary carnitine deficiency". Human ... characterized by impaired carnitine transport, urinary carnitine wasting, low serum carnitine levels, reduced intracellular ... "Primary systemic carnitine deficiency is caused by mutations in a gene encoding sodium ion-dependent carnitine transporter". ...
β-oxidation in the peroxisome requires the use of a peroxisomal carnitine acyltransferase (instead of carnitine acyltransferase ... Acyl-carnitine is shuttled inside by a carnitine-acylcarnitine translocase, as a carnitine is shuttled outside. Acyl-carnitine ... The liberated carnitine is shuttled back to the cytosol, as an acyl-carnitine is shuttled into the matrix. If the fatty acyl- ... Acyl-CoA is transferred to the hydroxyl group of carnitine by carnitine palmitoyltransferase I, located on the cytosolic faces ...
However, no formal assessment of the utility of carnitine and arginine supplementation has been published, and its uses have ... Neuwald AF (August 1997). "Barth syndrome may be due to an acyltransferase deficiency". Current Biology. 7 (8): R465-6. doi: ... Metabolic deficiencies have been treated by oral arginine and carnitine supplementation, which has been shown to ameliorate ... CL remodeling in mammals requires additional enzymes, such as monolysocardiolipin acyltransferase (MLCLAT), acyl-CoA: ...
SLC22A3 is an extraneuronal monoamine transporter that is present in astrocytes, and SLC22A5 is a high-affinity carnitine ... CYP2D6, dopamine β-hydroxylase, flavin-containing monooxygenase 3, butyrate-CoA ligase, and glycine N-acyltransferase are the ... "Substrate/Product". glycine N-acyltransferase. BRENDA. Technische Universität Braunschweig. "Compound Summary". p- ...
... : diacylglycerol acyltransferase (DGAT) plays an important role in energy metabolism on account of key enzyme in ... Transport of acyl-CoA into the mitochondria requires carnitine palmitoyltransferase 1 (CPT1), which converts acyl-CoA into ... Yu, Yi‐Hao; Ginsberg, Henry (8 July 2009). "The role of acyl‐CoA:diacylglycerol acyltransferase (DGAT) in energy metabolism". ...
Lysophosphatidylcholine acyltransferase 1 LYRM7: encoding protein LYR motif containing 7 LYSMD3: LysM and putative ... carboxylase deficiency Myelodysplastic syndrome Netherton syndrome Nicotine dependency Parkinson's disease Primary carnitine ...
It works by inhibiting the enzyme Carnityl Acyl Transferase I (CAT-I) indirectly which is present in the mitochondria. This ... "More direct evidence for a malonyl-CoA-carnitine palmitoyltransferase I interaction as a key event in pancreatic beta-cell ... "Glibenclamide inhibits islet carnitine palmitoyltransferase 1 activity, leading to PKC-dependent insulin exocytosis". American ...
Acyl-carnitine is shuttled inside by a carnitine-acylcarnitine translocase, as a carnitine is shuttled outside. Acyl-carnitine ... Enzymes, acyltransferases and transacylases, incorporate fatty acids in phospholipids, triacylglycerols, etc. by transferring ... Acyl-CoA is transferred to the hydroxyl group of carnitine by carnitine palmitoyltransferase I, located on the cytosolic faces ... The liberated carnitine is shuttled back to the cytosol, as an acyl-CoA is shuttled into the mitochondrial matrix. Beta ...
Rytting E, Audus KL (January 2005). "Novel organic cation transporter 2-mediated carnitine uptake in placental choriocarcinoma ... and glycine N-acyltransferase (GLYAT) are the enzymes known to metabolize amphetamine or its metabolites in humans. Amphetamine ... and SLC22A5 is a high-affinity carnitine transporter. Amphetamine is known to strongly induce cocaine- and amphetamine- ... the role of glycine N-acyltransferase, and factors that influence interindividual variation". Expert Opinion on Drug Metabolism ...
The 2014 Ju-Jitsu World Championship were the 12th edition of the Ju-Jitsu World Championships, and were held in Paris, France from November 28 to November 30, 2014. 28.11.2014 - Men's and Women's Fighting System, Men's and Women's Jiu-Jitsu (ne-waza), Men's Duo System - Classic 29.11.2014 - Men's and Women's Fighting System, Men's and Women's Jiu-Jitsu (ne-waza), Women's Duo System - Classic 30.11.2014 - Men's Jiu-Jitsu (ne-waza), Mixed Duo System - Classic, Team event Vincent MATCZAK (2014-09-30). "4TH INVITAION TO WORLD CHAMPIONSHIP 2014" (PDF). Retrieved 2019-11-28.[dead link] Online results Official results (PDF) Mixed team event results (PDF) (All articles with dead external links, Articles with dead external links from April 2022, Ju-Jitsu World Championships, 2014 in French sport ...
... Academic Article ... At micromolar concentrations, acetyl-CoA inhibited hepatic carnitine acyltransferase activity and mitochondrial fatty acid ...
BCAA, branched chain amino acids; CACT, carnitine acylcarnitine translocase; CAT, carnitine acyltransferase; CPT, carnitine ...
The CPT1A gene provides instructions for making an enzyme called carnitine palmitoyltransferase 1A, which is found in the liver ... Carnitine acyltransferases and their influence on CoA pools in health and disease. Mol Aspects Med. 2004 Oct-Dec;25(5-6):475-93 ... Carnitine palmitoyltransferase I deficiency. More than 20 mutations in the CPT1A gene have been found to cause carnitine ... Carnitine palmitoyltransferase 1A connects carnitine to long-chain fatty acids so they can cross the inner membrane of ...
Effects of dietary fatty acid composition on the regulation of carnitine palmitoyltransferase (CPT) I in rainbow trout ( ... Co-ordinate induction of hepatic mitochondrial and peroxisomal carnitine acyltransferase synthesis by diet and drugs.. *P. ... studies using both diet and drugs to cause enzyme induction suggest that the synthesis of the carnitine acyltransferases ( ... Intertissue regulation of carnitine palmitoyltransferase I (CPTI): mitochondrial membrane properties and gene expression in ...
Acyl-carnitine (C0), (C2), (C16), (C18) measurements in plasma. Data represent the mean ± SD (N = 3). (D) Acetyl-CoA ... protein levels of Acetyl-CoA Acyltransferase 2 (ACAA2), which catalyzes the last step of β-oxidation, were elevated only in ... Adck2+/− mice on ad libitum showed an accumulation of acyl-carnitines C2, C16, and C18 and the corresponding decrease of free ... The β-oxidation of fatty acids assay (BOX) was carried out in the presence of palmitoyl-l-carnitine and malate. Substrates and ...
Superfamily c.43.1: CoA-dependent acyltransferases [52777] (5 families) *. Family c.43.1.3: Choline/Carnitine O-acyltransferase ... Fold c.43: CoA-dependent acyltransferases [52776] (1 superfamily). core: 2 layers, a/b; mixed beta-sheet of 6 strands, order ...
carnitine medium-chain acyltransferase activity. *medium-chain/long-chain carnitine acyltransferase activity ... Catalysis of the reaction: octanoyl-CoA + L-carnitine = CoA + L-octanoylcarnitine.. Synonyms: *octanoyl-CoA:L-carnitine O- ...
Carnitine acyl transferase I converts acyl-CoA into fatty acyl carnitine, which is translocated across the inner mitochondrial ... Carnitine acyl transferase II in the inner mitochondrial membrane catalyzes the formation of fatty acyl-CoA for the initiation ... For instance, a published report linked maternal AFLP with pediatric carnitine palmitoyl transferase I deficiency [88]. A ... and carnitine fatty acyl-CoA translocase and MTP deficiency [20,71]. MTP−/− mice were also reported to develop intrauterine ...
in carnitine metabolism in mice [37, 38]. No similar indications of PPAR. -induced carnitine synthesis have been described in ... In addition, the expression of the gene encoding the enzyme acetyl-CoA acyltransferase 2 (ACAA2) involved in the final step of ... Furthermore, hepatic carnitine synthesis is enhanced by PPAR. activation in mice [34, 35]. Carnitine is a conditionally ... α-activation results in enhanced carnitine biosynthesis and OCTN2-mediated hepatic carnitine accumulation," Biochimica et ...
Carnitine palmitoyltransferase I (CPT1) inhibitor. 3103. Fumonisin B1. Inhibitor of sphingosine N-acyltransferase. ...
Carnitine Acyltransferases Entry term(s). Acylcarnitine Translocase Acyltransferases, Carnitine Carnitine Acylcarnitine ... Carnitine acyltransferases Entry term(s):. Acylcarnitine Translocase. Acyltransferases, Carnitine. Carnitine Acetylcarnitine ... Carnitine Acyltransferases - Preferred Concept UI. M0003496. Scope note. Acyltransferases in the inner mitochondrial membrane ... Carnitine Acylcarnitine Translocase. Carnitine Translocase. Carnitine-Acetylcarnitine Translocase. Carnitine-Acylcarnitine ...
... reduced glycerol-3-phosphate acyl transferase-1, and increased carnitine palmitoyltransferase-1 expression, which led to ... The Benefits of Carnitine and DHEA for Fat Metabolism - Life Extension Magazine, 8/02 - Carnitine is an amino acid thats ... However, the mRNA levels of carnitine palmitoyl transferase-1 (CPT-1) and uncoupling protein 2 (UCP2), as well as lipolytic ...
Malonyl CoA menghambat carnitine acyl transferase I. menghambat beta oksidasi www.themegallery.com. 17. www.themegallery.com 18 ... acyltransferase Cholesterol esters 41. (principal transport form in blood) www.themegallery.com 41 www.themegallery.com 42 ...
Carnitine acyltransferase (substance). Code System Preferred Concept Name. Carnitine acyltransferase (substance). Concept ...
Three FFAs (Δ18:1, Δ18:2, and Δ16:0) and two acyl-carnitines (Δ16:0-carnitine and Δ18:0-carnitine) decreased and increased in ... 4b). At the transcriptional level, T3-treated tadpoles showed upregulated glycerolipid synthesis (DAG/MAG O-acyltransferase), ... and two aryl-carnitines (Δ18:0-carnitine and Δ10:0-carnitine; active form of FFAs) decreased and increased in content, ... 3c). Other FFAs or acyl-carnitines were unaffected. At the transcriptional level, T3-treated tadpoles showed upregulated ...
1-alkenylglycerophosphoethanolamine O-acyltransferase activity GO:0047166 * 1-alkyl-2-acetylglycerol O-acyltransferase activity ...
Peroxisomal carnitine acetyl transferase is required for elaboration of penetration hyphae during plant infection by ... ABCD, ATP-binding cassette, subfamily D; ACAA, Acetyl-CoA acyltransferase; ACOX, Acyl-CoA oxidase; ACSL, Long-chain acyl-CoA ... Functional divergence of diacylglycerol acyltransferases in the unicellular green alga Haematococcus pluvialis. J Exp Bot. 2021 ... of root waxes and can be produced in the aerial cuticle by ectopic expression of a suberin-associated acyltransferase. Plant ...
Markwell MAK, McGroarty EJ, Bieber LL, Tolbert NE: The subcellular distribution of carnitine acyltransferases in mammalian ... The activities of carnitine palmitoyltransferase (CPT), a key enzyme of fatty acid β-oxidation, and peroxisomal β-oxidation ...
Carnitine Acyltransferases. *Citrate (si)-Synthase. *Diacylglycerol O-Acyltransferase. *Glycerol-3-Phosphate O-Acyltransferase ... Phosphatidylcholine-Sterol O-Acyltransferase*Phosphatidylcholine-Sterol O-Acyltransferase. *O-Acyltransferase, ... "Phosphatidylcholine-Sterol O-Acyltransferase" is a descriptor in the National Library of Medicines controlled vocabulary ... In familial lecithin:cholesterol acyltransferase deficiency disease, the absence of the enzyme results in an excess of ...
In mitochondrial oxidation similar but different enzymes are used called carnitine acyltransferase I and II. Difference number ... peroxisomal carnitine acyltransferase, which is needed to move an activated acyl group from outside the peroxisome to inside it ... The enzyme 1-acyl-sn-glycerol-3-phosphate acyltransferase converts LPA into phosphatidic acid (1,2-diacyl-sn-glycerol 3- ... In particular, both pathways make use of acetyl-CoA acyltransferase, 3-hydroxyacyl-CoA dehydrogenase and enoyl-CoA hydratase. ...
Interestingly, l-carnitine treatment on TPM3(E151G) transgenic larvae significantly improves the muscle endurance by restoring ... which can be rescued by l-carnitine treatment, fatty acid metabolism was differentially dysregulated in TPM3(E151G) fish and ... rescued by l-carnitine treatment. These results demonstrate that TPM3(E151G) and TPM3(E151A) exhibit different pathogenicity, ... enhances l-carnitine uptake inside cells. Carnitine acyltransferases are a family of enzymes that catalyze the reversible ...
"Reversible Product Release and Recapture by a Fungal Polyketide Synthase Using a Carnitine Acyltransferase Domain." Angew. Chem ... Tang, Y., Koppisch, A., Khosla, C. "The Acyltransferase Homolog Found in Initiation Modules of Type II PKS is an Acetyl-ACP ... Xie, X., Meehan, M. J. Xu, W., Dorrestein, P. C., Tang, Y.* "Acyltransferase Mediated Polyketide Release From Fungal ... "Biosynthesis of lovastatin analogs with a broadly specific acyltransferase." Chem. Biol. 2006, 13, 1161-1169. Link ...
Essentially, this switch is controlled by an enzyme called Carnitine acyltransferases protein or Crat in short.. ...
In addition, it reduced adipocyte fatty acid binding protein and glycerol-3-phosphate acyltransferase gene expression in a ... Conversely, THP increased the mRNA expression of carnitine palmitoyltransferase 1 in a concentration-dependent manner. ...
We have shown previously that C75, a stimulator of carnitine palmitoyl transferase-1 (CPT-1) and fatty acid oxidation (FAOx), ... the glycerol-3-phosphate acyltransferase (GPAT) inhibitor FSG67, on FA metabolism, metabolomics profiles, and metabolic stress ... We have shown previously that C75, a stimulator of carnitine palmitoyl transferase-1 (CPT-1) and fatty acid oxidation (FAOx), ... We have shown previously that C75, a stimulator of carnitine palmitoyl transferase-1 (CPT-1) and fatty acid oxidation (FAOx), ...
Carnitine. Carnitine Acetyltransferase use Carnitine O-Acetyltransferase. Carnitine Acyltransferases. Carnitine O- ...
This occurs enzymatically via carnitine acyltransferases. Specific acylcarnitines accumulate as a result of various organic ... Plasma samples revealed low levels of free carnitine (C0), long-chain acyl-carnitines and total carnitine. In particular, C0 ... To measure total carnitine, samples are spiked with deuterated carnitine (internal standard) and hydrolyzed with potassium ... Abnormal levels of free carnitine, total carnitine, and acylcarnitines in serum can be indicative of a metabolic disorder ...
Research further suggests these SCFAs inhibit fat production by regulating the key enzyme, carnitine acyltransferase that ...
  • Second, the mitochondrial outer membrane enzyme glycerol-3-phosphate acyltransferase esterifies an acyl-group to the sn-1 position of sn-glycerol 3-phosphate to form 1-acyl-sn-glycerol 3-phosphate (lysophosphatidic acid or LPA). (smpdb.ca)
  • The enzyme 1-acyl-sn-glycerol-3-phosphate acyltransferase converts LPA into phosphatidic acid (1,2-diacyl-sn-glycerol 3-phosphate) by esterifying an acyl-group to the sn-2 position of the glycerol backbone. (smpdb.ca)
  • In the present work, we characterized the effects of C75 and another anorexigenic compound, the glycerol-3-phosphate acyltransferase (GPAT) inhibitor FSG67, on FA metabolism, metabolomics profiles, and metabolic stress responses in cultured hypothalamic neurons and hypothalamic neuronal cell lines during lipid excess with palmitate. (elsevier.com)
  • At micromolar concentrations, acetyl-CoA inhibited hepatic carnitine acyltransferase activity and mitochondrial fatty acid oxidation. (uab.edu)
  • Acyltransferases in the inner mitochondrial membrane that catalyze the reversible transfer of acyl groups from acyl-CoA to L-carnitine and thereby mediate the transport of activated fatty acids through that membrane. (bvsalud.org)
  • L-Carnitine may play an important role in male reproductive health, mainly due to increased mitochondrial fatty acid oxidation, which results in improved motility of epididymal sperm. (supplemena.com)
  • L-Carnitine is essential for transporting long-chain fatty acids across the mitochondrial membrane, for subsequent fat breakdown and energy generation. (supplemena.com)
  • The CPT1A gene provides instructions for making an enzyme called carnitine palmitoyltransferase 1A, which is found in the liver. (medlineplus.gov)
  • Carnitine palmitoyltransferase 1A connects carnitine to long-chain fatty acids so they can cross the inner membrane of mitochondria. (medlineplus.gov)
  • Most of these mutations change single protein building blocks (amino acids) within carnitine palmitoyltransferase 1A. (medlineplus.gov)
  • Akkaoui M, Cohen I, Esnous C, Lenoir V, Sournac M, Girard J, Prip-Buus C. Modulation of the hepatic malonyl-CoA-carnitine palmitoyltransferase 1A partnership creates a metabolic switch allowing oxidation of de novo fatty acids. (medlineplus.gov)
  • Phosphatidylcholine-Sterol O-Acyltransferase" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (harvard.edu)
  • This graph shows the total number of publications written about "Phosphatidylcholine-Sterol O-Acyltransferase" by people in Harvard Catalyst Profiles by year, and whether "Phosphatidylcholine-Sterol O-Acyltransferase" was a major or minor topic of these publication. (harvard.edu)
  • Below are the most recent publications written about "Phosphatidylcholine-Sterol O-Acyltransferase" by people in Profiles. (harvard.edu)
  • Bennett MJ, Boriack RL, Narayan S, Rutledge SL, Raff ML. Novel mutations in CPT 1A define molecular heterogeneity of hepatic carnitine palmitoyltransferase I deficiency. (medlineplus.gov)
  • More than 20 mutations in the CPT1A gene have been found to cause carnitine palmitoyltransferase I (CPT I) deficiency. (medlineplus.gov)
  • Downregulation of carnitine acyl-carnitine translocase by miRNAs 132 and 212 amplifies glucose-stimulated insulin secretion. (duke.edu)
  • Exogenous LCACs, especially palmitoyl-carnitine and stearoyl-carnitine, inhibited iNKT cell expansion and promoted senescence. (bvsalud.org)
  • A nonhydrolyzable ether analog of palmitoyl-carnitine stimulated IS, showing that β-oxidation of palmitoyl-carnitine is not required for its stimulation of IS. (duke.edu)
  • Last, the enzyme diacylglycerol O-acyltransferase synthesizes triacylglycerol from diacylglycerol and a fatty acyl-CoA. (smpdb.ca)
  • Diacylglycerol O-Acyltransferase" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (jefferson.edu)
  • Below are the most recent publications written about "Diacylglycerol O-Acyltransferase" by people in Profiles. (jefferson.edu)
  • A group of fats called long-chain fatty acids cannot enter mitochondria unless they are attached to a substance known as carnitine. (medlineplus.gov)
  • Once these fatty acids are inside mitochondria, carnitine is removed and they can be metabolized to produce energy. (medlineplus.gov)
  • Interestingly, l -carnitine treatment on TPM3 (E151G) transgenic larvae significantly improves the muscle endurance by restoring the basal respiration and ATP levels in mitochondria. (biomedcentral.com)
  • CACT is responsible for transporting long-chain acyl-carnitines into the mitochondria for β-oxidation. (duke.edu)
  • Essentially, this switch is controlled by an enzyme called Carnitine acyltransferases protein or Crat in short. (thecytoburns.com)
  • This switch is activated by the energy sensor adenosine monophosphate-activated protein kinase (AMPK), in response to the increase in the AMP/ATP ratio, while carnitine palmitoyl transferase-1 (CPT-1) is also activated by AMPK inhibition of acetyl-CoA carboxylase (ACC). (frontiersin.org)
  • Caco2 cell culture and animal experiment confirmed IMZ affected carnitine absorption through the organic cation transporter type-2 (OCTN2) protein encoded by solute carrier family 22A member 5 (SLC22A5) gene in colon. (bvsalud.org)
  • These results suggested that maternal IMZ exposure affected carnitine absorption through OCTN2 protein, which led to the decline of anaerobic bacteria and unbalanced intestinal homeostasis. (bvsalud.org)
  • Normal protein content but abnormally inhibited enzyme activity in muscle carnitine palmitoyltransferase II deficiency. (dbcls.jp)
  • Lethal neonatal and severe late infantile forms of carnitine palmitoyltransferase II deficiency associated with compound heterozygosity for different protein truncation mutations. (dbcls.jp)
  • Structural analysis of lecithin:cholesterol acyltransferase bound to high density lipoprotein particles. (harvard.edu)
  • Expression of the PPAR-α and γ, lipoprotein lipase (LPL), hormone sensitive lipase (HSL), carnitine palmitoyl acyltransferase-1 (CPT-1), insulin receptor, GLUT-4 and adipokines were assessed in epidydimal fat. (wordpress.com)
  • Without enough of this enzyme, carnitine is not attached to long-chain fatty acids. (medlineplus.gov)
  • CPT2 gene mutations resulting in lethal neonatal or severe infantile carnitine palmitoyltransferase II deficiency. (dbcls.jp)
  • Addition of recombinant PTE-2 to incubations containing isolated mouse liver peroxisomes strongly inhibited bile acid-CoA:amino acid N-acyltransferase activity, suggesting that this thioesterase can interfere with CoASH-dependent pathways. (rhea-db.org)
  • In familial lecithin:cholesterol acyltransferase deficiency disease, the absence of the enzyme results in an excess of unesterified cholesterol in plasma. (harvard.edu)
  • Cause of recurrent rhabdomyolysis, carnitine palmitoyltransferase II deficiency and novel pathogenic mutation. (dbcls.jp)
  • Exercise, Nutrition, and Supplements in the Muscle Carnitine Palmitoyl-Transferase II Deficiency: New Theoretical Bases for Potential Applications. (dbcls.jp)
  • Need for strict clinical management of patients with carnitine palmitoyltransferase II deficiency: Experience with two cases detected by expanded newborn screening. (dbcls.jp)
  • Severe rhabdomyolysis in homozygote carnitine palmitoyltransferase II deficiency. (dbcls.jp)
  • Recurrent Myalgia since Early Infancy-Misleading Clinical Course in a Child with Carnitine Palmitoyltransferase-II Deficiency. (dbcls.jp)
  • An ignored cause of red urine in children: rhabdomyolysis due to carnitine palmitoyltransferase II (CPT-II) deficiency. (dbcls.jp)
  • First Japanese Case of Carnitine Palmitoyltransferase II Deficiency with the Homozygous Point Mutation S113L. (dbcls.jp)
  • Missed Newborn Screening Case of Carnitine Palmitoyltransferase-II Deficiency. (dbcls.jp)
  • Neonatal Carnitine Palmitoyltransferase II Deficiency: A Lethal Entity. (dbcls.jp)
  • Carnitine palmitoyl transferase II deficiency in an adolescent presenting with rhabdomyolysis and acute renal failure. (dbcls.jp)
  • Carnitine palmitoyltransferase II (CPT II) deficiency: genotype-phenotype analysis of 50 patients. (dbcls.jp)
  • Novel mutations in myopathic form of carnitine palmitoyltransferase II deficiency in a Chinese patient. (dbcls.jp)
  • Clinically symptomatic heterozygous carnitine palmitoyltransferase II (CPT II) deficiency. (dbcls.jp)
  • Neonatal carnitine palmitoyltransferase II deficiency associated with Dandy-Walker syndrome and sudden death. (dbcls.jp)
  • Carnitine palmitoyltransferase II deficiency: successful anaplerotic diet therapy. (dbcls.jp)
  • Mutations of carnitine palmitoyltransferase II (CPT II) in Japanese patients with CPT II deficiency. (dbcls.jp)
  • Clinical features and new molecular findings in Carnitine Palmitoyltransferase II (CPT II) deficiency. (dbcls.jp)
  • Severe infantile type of carnitine palmitoyltransferase II (CPT II) deficiency due to homozygous R503C mutation. (dbcls.jp)
  • A novel splice site mutation in neonatal carnitine palmitoyl transferase II deficiency. (dbcls.jp)
  • Effect of diet on exercise tolerance in carnitine palmitoyltransferase II deficiency. (dbcls.jp)
  • Mutation and biochemical analysis in carnitine palmitoyltransferase type II (CPT II) deficiency. (dbcls.jp)
  • Exercise tolerance in carnitine palmitoyltransferase II deficiency with IV and oral glucose. (dbcls.jp)
  • Screening for carnitine palmitoyltransferase II deficiency by tandem mass spectrometry. (dbcls.jp)
  • Identification of novel mutations in Spanish patients with muscle carnitine palmitoyltransferase II deficiency. (dbcls.jp)
  • l -Carnitine is an amino acid that is widely present in human tissues and can be produced from essential amino acids lysine and methionine. (biomedcentral.com)
  • High-performance liquid chromatography-tandem mass spectrometry (HPLC-MS/MS) and next-generation sequencing (NGS) were used to detect the concentrations of carnitine in the blood spots and for diagnosis. (bvsalud.org)
  • A variable myopathy associated with heterozygosity for the R503C mutation in the carnitine palmitoyltransferase II gene. (dbcls.jp)
  • PDF] Effects of dietary fatty acid composition on the regulation of carnitine palmitoyltransferase (CPT) I in rainbow trout (Oncorhynchus mykiss). (semanticscholar.org)
  • These studies establish a link between miRNA-dependent regulation of CACT and fatty acyl-carnitine-mediated regulation of IS. (duke.edu)
  • Plasma samples revealed low levels of free carnitine (C0), long-chain acyl-carnitines and total carnitine. (bvsalud.org)
  • The addition of long-chain fatty acyl-carnitines promoted IS from rat insulinoma β-cells (INS-1) as well as primary mouse islets. (duke.edu)
  • Randomized, Placebo-Controlled Phase 2b Study to Evaluate the Safety and Efficacy of Recombinant Human Lecithin Cholesterol Acyltransferase in Acute ST-Segment-Elevation Myocardial Infarction: Results of REAL-TIMI 63B. (harvard.edu)
  • Recombinant human lecithin-cholesterol acyltransferase in patients with atherosclerosis: phase 2a primary results and phase 2b design. (harvard.edu)
  • With RNAseq transcriptomic analysis of the expression profiling from the muscle specimens, it surprisingly discloses large downregulation of genes involved in pathways of sodium, potassium, and calcium channels, which can be rescued by l -carnitine treatment, fatty acid metabolism was differentially dysregulated in TPM3 (E151G) fish and rescued by l -carnitine treatment. (biomedcentral.com)
  • Then, we assessed the changes in growth phenotypes, carnitine levels, and gut microbiota in F0, F1 or F2 generations. (bvsalud.org)
  • Fertilmas is a capsule-based product for men with general infertility, and has lower levels of L-Carnitine & L-Arginine than EROSMAS. (supplemena.com)
  • The resulting reduction in energy metabolism due to lower L-Carnitine levels can be restored by L-Carnitine supplementation. (supplemena.com)
  • The Carnipure® product is a high quality L-Carnitine ingredient manufactured by the Swiss company Lonza. (supplemena.com)
  • Maternal IMZ exposure also had a greater effect on gut microbiota in offspring, especially anaerobic bacteria, which positively correlated with C0 and acyl-carnitines. (bvsalud.org)