Biomaterial Database

Multiple acyl-CoA dehydrogenation deficiency as decreased acyl-carnitine profile in serum. 2015

Bing Wen, and Duoling Li, and Wei Li, and Yuying Zhao, and Chuanzhu Yan

Laboratory of Neuromuscular Disorders, Department of Neurology, Qilu Hospital, Shandong University, Jinan, 250012, China.

We report a case with late onset riboflavin-responsive multiple acyl-CoA dehydrogenation deficiency (MADD) characterized by decreased acyl-carnitine profile in serum which is consistent with primary systemic carnitine deficiency (CDSP) while just the contrary to a typical MADD. This patient complained with muscle weakness, muscle pain and intermittent vomiting, and was diagnosed as polymyositis, received prednisone therapy before consulted with us. Muscle biopsy revealed mild lipid storage. The findings of serum acyl-carnitines were consistent with CDSP manifesting as decreased free and total carnitines in serum. But oral L-carnitine supplementation was not very effective to this patient and mutation analysis of the SLC22A5 gene for CDSP was normal. Later, another acyl-carnitine analysis revealed a typical MADD profile in serum, which was characterized by increased multiple acyl-carnitines. Compound heterozygous mutations were identified in electron transferring-flavoprotein dehydrogenase (ETFDH) gene which confirmed the diagnosis of MADD. After administration of riboflavin, he improved dramatically, both clinically and biochemically. Thus, late onset riboflavin-responsive MADD should be included in the differential diagnosis for adult carnitine deficiency.

UI	MeSH Term	Description	Entries
D007506	Iron-Sulfur Proteins	A group of proteins possessing only the iron-sulfur complex as the prosthetic group. These proteins participate in all major pathways of electron transport: photosynthesis, respiration, hydroxylation and bacterial hydrogen and nitrogen fixation.	Iron-Sulfur Protein,Iron Sulfur Proteins,Iron Sulfur Protein,Protein, Iron-Sulfur,Proteins, Iron Sulfur,Proteins, Iron-Sulfur,Sulfur Proteins, Iron
D008297	Male		Males
D009154	Mutation	Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.	Mutations
D002331	Carnitine	A constituent of STRIATED MUSCLE and LIVER. It is an amino acid derivative and an essential cofactor for fatty acid metabolism.	Bicarnesine,L-Carnitine,Levocarnitine,Vitamin BT,L Carnitine
D004252	DNA Mutational Analysis	Biochemical identification of mutational changes in a nucleotide sequence.	Mutational Analysis, DNA,Analysis, DNA Mutational,Analyses, DNA Mutational,DNA Mutational Analyses,Mutational Analyses, DNA
D006801	Humans	Members of the species Homo sapiens.	Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000214	Acyl Coenzyme A	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.	Acyl CoA,Fatty Acyl CoA,Long-Chain Acyl CoA,Acyl CoA, Fatty,Acyl CoA, Long-Chain,CoA, Acyl,CoA, Fatty Acyl,CoA, Long-Chain Acyl,Coenzyme A, Acyl,Long Chain Acyl CoA
D000587	Oxidoreductases Acting on CH-NH Group Donors	Enzymes catalyzing the dehydrogenation of secondary amines, introducing a C	Secondary Amine Oxidoreductases,Amine Oxidoreductases, Secondary Amine,Amine Oxidoreductases, Secondary,Oxidoreductases Acting on CH NH Group Donors,Oxidoreductases, Secondary Amine
D044927	Electron-Transferring Flavoproteins	Flavoproteins that serve as specific electron acceptors for a variety of DEHYDROGENASES. They participate in the transfer of electrons to a variety of redox acceptors that occur in the respiratory chain.	ET Flavoprotein,Electron Transfer Flavoprotein,Electron-Transferring Flavoprotein,Electron Transferring Flavoprotein,Electron Transferring Flavoproteins,Flavoprotein, ET,Flavoprotein, Electron Transfer,Flavoprotein, Electron-Transferring,Flavoproteins, Electron-Transferring,Transfer Flavoprotein, Electron
D054069	Multiple Acyl Coenzyme A Dehydrogenase Deficiency	An autosomal recessive disorder of fatty acid oxidation, and branched chain amino acids (AMINO ACIDS, BRANCHED-CHAIN); LYSINE; and CHOLINE catabolism, that is due to defects in either subunit of ELECTRON TRANSFER FLAVOPROTEIN or its dehydrogenase, electron transfer flavoprotein-ubiquinone oxidoreductase (EC 1.5.5.1).	ETFA Deficiency,ETFB Deficiency,ETFDH Deficiency,Electron Transfer Flavoprotein Alpha Subunit Deficiency,Electron Transfer Flavoprotein Beta Subunit Deficiency,Electron Transfer Flavoprotein Deficiency,Electron Transfer Flavoprotein Dehydrogenase Deficiency,Ethylmalonic-Adipic Aciduria,Ethylmalonic-Adipicaciduria,Glutaric Acidemia Type II,Glutaric Acidemia, Type 2,Glutaric Aciduria II,Glutaric Aciduria IIA,Glutaric Aciduria IIB,Glutaric Aciduria IIC,Glutaric Aciduria Type 2,Glutaric Aciduria Type II,Glutaric Aciduria, Type 2,MADD (Multiple Acyl-CoA Dehydrogenase Deficiency),Multiple Acyl-CoA Dehydrogenase Deficiency,Multiple FAD Dehydrogenase Deficiency,Aciduria, Ethylmalonic-Adipic,Acidurias, Ethylmalonic-Adipic,ETFA Deficiencies,ETFB Deficiencies,ETFDH Deficiencies,Ethylmalonic Adipic Aciduria,Ethylmalonic Adipicaciduria,Ethylmalonic-Adipic Acidurias,MADD (Multiple Acyl CoA Dehydrogenase Deficiency),MADDs (Multiple Acyl-CoA Dehydrogenase Deficiency),Multiple Acyl CoA Dehydrogenase Deficiency