Novel mutations in the gene encoding very long-chain acyl-CoA dehydrogenase identified in patients with partial carnitine palmitoyltransferase ii deficiency

2012 ◽  
Vol 47 (2) ◽  
pp. 224-229 ◽  
Author(s):  
Paul J. Isackson ◽  
Kristin A. Sutton ◽  
Karl Y. Hostetler ◽  
Georgirene D. Vladutiu
Keyword(s):  
Carnitine Palmitoyltransferase ◽  
Novel Mutations ◽  
Gene Encoding ◽  
Chain Acyl ◽  
Carnitine Palmitoyltransferase Ii ◽  
Long Chain

scholarly journals Importance of albumin binding in the assay for carnitine palmitoyltransferase

1983 ◽  
Vol 216 (2) ◽  
pp. 495-498 ◽  
Author(s):  
K McCormick ◽  
V J Notar-Francesco
Keyword(s):  
Enzyme Activity ◽  
Carnitine Palmitoyltransferase ◽  
Albumin Binding ◽  
Biochemical Modification ◽  
Physiological Relevance ◽  
Chain Acyl ◽  
Absolute Quantity ◽  
Substrate Concentrations ◽  
Long Chain ◽  
Do So

Alterations in the long-chain acyl-CoA binding to albumin in the carnitine palmitoyltransferase (CPT) assay appreciably affect the reaction at commonly used substrate concentrations. Since in the CPT assay the latter are typically well below saturation or Vmax. values, the measured enzyme activity depends on both the absolute quantity of albumin in the CPT assay and any biochemical modification of its binding. The present study verifies the striking dependence of the K0.5 for palmitoyl-CoA on albumin and the misleading ‘activation’ of the enzyme by compounds that also avidly bind to albumin. In assessing the intracellular physiological relevance of any modifier of CPT, the effects of protein binding in the assay assume particular importance. Indeed, any compound that alters CPT activity may do so, not directly, but as an assay artifact changing the free or unbound substrate concentrations.

Identification of Four Novel Mutations in Patients with Carnitine Palmitoyltransferase II (CPT II) Deficiency

1998 ◽  
Vol 64 (4) ◽  
pp. 229-236 ◽  
Author(s):  
Bing-Zhi Yang ◽  
Jia-Huan Ding ◽  
Tracy Dewese ◽  
Diane Roe ◽  
Guocheng He ◽  
...  
Keyword(s):  
Carnitine Palmitoyltransferase ◽  
Novel Mutations ◽  
Carnitine Palmitoyltransferase Ii ◽  
Cpt Ii Deficiency

Carnitine palmitoyltransferases in pea leaf chloroplasts: partial purification, location, and properties

2000 ◽  
Vol 78 (3) ◽  
pp. 328-335 ◽  
Author(s):  
Christine Masterson ◽  
Clifford Wood
Keyword(s):  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Carnitine Palmitoyltransferase ◽  
Chloroplast Envelope ◽  
Partial Purification ◽  
Western Blots ◽  
Chain Acyl ◽  
Long Chain ◽  
Inner Envelope

Carnitine palmitoyltransferase (EC 2.3.1.21), an enzyme that catalyses the reversible transfer of activated long-chain acyl groups between CoASH and L-carnitine, has been confirmed in pea leaf chloroplasts. This enzyme is bound to the chloroplast inner envelope membrane and has two isoforms, one bound to the outside (cytosol side) of the inner envelope and one bound to the inside (stromal side) of the inner envelope. Malonyl CoA inhibited the activity of the outer carnitine palmitoyltransferase, while stimulating the activity of the inner isoform and may be a regulator of these enzymes in vivo. Carnitine palmitoyltransferase was solubilized from the chloroplast envelope by detergent treatment and the two isoforms separated by Q-Sepharose anion exchange chromatography. Both proteins were immunochemically observed by probing Western blots of sodium dodecyl sulfate - polyacrylamide gel electrophoresis gels using an anti-beef heart mitochondrial carnitine palmitoyltransferase polyclonal antibody. The monomeric molecular mass of the protein recognized by this antibody was approximately 20 kDa. This 20-kDa protein also bound3H-carnitine. Both isoforms had broad acyl CoA substrate specificities, but showed increased activity with desaturated long-chain acyl CoAs, exhibiting a preference for linolenoyl CoA. A role for carnitine palmitoyltransferase in the shuttling of fatty acids across the chloroplast envelope is suggested.Key words: Pisum sativum, chloroplasts, carnitine palmitoyltransferase, fatty acid metabolism, eukaryotic pathway, membrane transport.

Novel mutations in myopathic form of carnitine palmitoyltransferase II deficiency in a Chinese patient

2013 ◽  
Vol 425 ◽  
pp. 125-127 ◽  
Author(s):  
Sun Young Cho ◽  
Tak-Shing Siu ◽  
Oliver Ma ◽  
Sidney Tam ◽  
Ching-wan Lam
Keyword(s):  
Chinese Patient ◽  
Carnitine Palmitoyltransferase ◽  
Novel Mutations ◽  
Carnitine Palmitoyltransferase Ii

An ignored cause of red urine in children: rhabdomyolysis due to carnitine palmitoyltransferase II (CPT-II) deficiency

2017 ◽  
Vol 30 (2) ◽  
Author(s):  
Engin Melek ◽  
Fatma Derya Bulut ◽  
Bahriye Atmış ◽  
Berna Şeker Yılmaz ◽  
Aysun Karabay Bayazıt ◽  
...  
Keyword(s):  
Clinical Phenotype ◽  
Carnitine Palmitoyltransferase ◽  
Long Chain Fatty Acids ◽  
Infantile Form ◽  
Dark Urine ◽  
Recurrent Rhabdomyolysis ◽  
History Of ◽  
Carnitine Palmitoyltransferase Ii ◽  
Cpt Ii Deficiency ◽  
Long Chain

AbstractCarnitine palmitoyltransferase II (CPT-II) deficiency is an autosomal recessively inherited disorder involving the β-oxidation of long-chain fatty acids, which leads to rhabdomyolysis and subsequent acute renal failure. The clinical phenotype varies from a severe infantile form to a milder muscle form. Here, we report a 9-year-old boy referred to our hospital for the investigation of hematuria with a 2-day history of dark urine and malaise. As no erythrocytes in the microscopic examination of the urine and hemoglobinuria were present, myoglobinuria due to rhabdomyolysis was the most probable cause of dark urine. After excluding the other causes of rhabdomyolysis, with the help of metabolic investigations, the patient was suspected to have CPT-II deficiency, the most common cause of metabolic rhabdomyolysis. Our aim in presenting this case is to emphasize considering rhabdomyolysis in the differential diagnosis of dark urine in order to prevent recurrent rhabdomyolysis and renal injury.

FACL4, a New Gene Encoding Long-Chain Acyl-CoA Synthetase 4, Is Deleted in a Family with Alport Syndrome, Elliptocytosis, and Mental Retardation

Genomics ◽  
1998 ◽  
Vol 47 (3) ◽  
pp. 350-358 ◽  
Author(s):  
Monica Piccini ◽  
Francesca Vitelli ◽  
Mirella Bruttini ◽  
Barbara R. Pober ◽  
Jon J. Jonsson ◽  
...  
Keyword(s):  
Mental Retardation ◽  
Alport Syndrome ◽  
Gene Encoding ◽  
Chain Acyl ◽  
New Gene ◽  
Long Chain

scholarly journals Identification of novel mutations in Spanish patients with muscle carnitine palmitoyltransferase II deficiency

2000 ◽  
Vol 15 (6) ◽  
pp. 579-580 ◽  
Author(s):  
Miguel A. Mart�n ◽  
Juan C. Rubio ◽  
Pilar del Hoyo ◽  
Alberto Garc�a ◽  
Fernando Bustos ◽  
...  
Keyword(s):  
Carnitine Palmitoyltransferase ◽  
Novel Mutations ◽  
Carnitine Palmitoyltransferase Ii

scholarly journals Different Lipid Signature in Fibroblasts of Long-Chain Fatty Acid Oxidation Disorders

Cells ◽  
2021 ◽  
Vol 10 (5) ◽  
pp. 1239
Author(s):  
Khaled I. Alatibi ◽  
Judith Hagenbuchner ◽  
Zeinab Wehbe ◽  
Daniela Karall ◽  
Michael J. Ausserlechner ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Oxidation ◽  
Chain Fatty Acid ◽  
Acid Oxidation ◽  
Long Chain Fatty Acid ◽  
Fatty Acid Oxidation Disorders ◽  
Chain Acyl ◽  
Inflammatory Phenotype ◽  
Carnitine Palmitoyltransferase Ii ◽  
Long Chain

Long-chain fatty acid oxidation disorders (lc-FAOD) are a group of diseases affecting the degradation of long-chain fatty acids. In order to investigate the disease specific alterations of the cellular lipidome, we performed undirected lipidomics in fibroblasts from patients with carnitine palmitoyltransferase II, very long-chain acyl-CoA dehydrogenase, and long-chain 3-hydroxyacyl-CoA dehydrogenase. We demonstrate a deep remodeling of mitochondrial cardiolipins. The aberrant phosphatidylcholine/phosphatidylethanolamine ratio and the increased content of plasmalogens and of lysophospholipids support the theory of an inflammatory phenotype in lc-FAOD. Moreover, we describe increased ratios of sphingomyelin/ceramide and sphingomyelin/hexosylceramide in LCHAD deficiency which may contribute to the neuropathic phenotype of LCHADD/mitochondrial trifunctional protein deficiency.

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