Molecular analysis of a patient with carnitine palmitoyltransferase II deficiency

Jun Akanuma, Kaoru Wataya, Yoichi Matubara, Teiji Yamamoto, Junichi Kira, Kuniaki Narisawa

Research output: Contribution to journalArticlepeer-review


Carnitine palmitoyltransferase (CPT), one of the key enzymes of β- oxidation, translocates long-chain fatty acids from the cytosolic compartment into the mitochondrial matrix to undergo β-oxidation. Recently, the CPT system has been characterized to consist of two distinct mitochondrial membrane-bound enzymes, CPT I, located on the inner side of the outer mitochondrial membrane, and CPT II, located on the inner mitochondrial membrane. We have investigated a Japanese patient with muscular manifestations who was previously reported as CPT deficiency. Enzymatic analysis of her cultured lymphoblasts revealed that CPT II activity was reduced to 5.8%, indicating that the patient suffered from CPT II deficiency. Molecular analysis identified a missense mutation, a glutamate (174)-to- lysine substitution (E174K), in the CPT II cDNA. The patient was homozygous for the mutation. The presence of the mutation was confirmed by PCR-RFLP with a mismatched primer to generate Mbo II recognition sequence at the mutation site. It has been reported that CPT II deficiency manifests as two different clinical phenotypes: a muscular form and a hepatocardiomuscular form. To our knowledge, this is the first case of CPT II deficiency with muscular symptoms to be characterized by molecular analysis in Japan.

Original languageEnglish
Pages (from-to)532-535
Number of pages4
JournalClinical Neurology
Issue number6
Publication statusPublished - Jun 1997

All Science Journal Classification (ASJC) codes

  • Clinical Neurology


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