Formation of the Enzyme Complex in Mitochondria Is Required for Function of Trifunctional β-Oxidation Protein

The first Japanese patient with mitochondrial trifunctional protein deficiency has been identified. The patient's α- and β-subunits were synthesized, transported into the mitochondria, and converted to the mature size, but rapidly disappeared. The newly synthesized mature α- and β-subunits in t...

Full description

Saved in:
Bibliographic Details
Published inBiochemical and biophysical research communications Vol. 219; no. 3; pp. 773 - 777
Main Authors Orii, Kenji E., Aoyama, Toshifumi, Souri, Masayoshi, Jiang, Ling Ling, Orii, Koji O., Hayashi, Shuhei, Yamaguchi, Seiji, Kondo, Naomi, Orii, Tadao, Hashimoto, Takashi
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 27.02.1996
Subjects
Autoradiography
Carbon Radioisotopes
Cells, Cultured
Child, Preschool
Female
Fibroblasts - enzymology
Humans
Immunoblotting
Japan
Kinetics
Macromolecular Substances
Male
Mitochondria - enzymology
Mitochondrial Trifunctional Protein
Multienzyme Complexes - biosynthesis
Multienzyme Complexes - deficiency
Multienzyme Complexes - metabolism
Palmitic Acid
Palmitic Acids - metabolism
Skin - enzymology
Japan
Online AccessGet full text

Cover

More Information
Summary:The first Japanese patient with mitochondrial trifunctional protein deficiency has been identified. The patient's α- and β-subunits were synthesized, transported into the mitochondria, and converted to the mature size, but rapidly disappeared. The newly synthesized mature α- and β-subunits in the control cells were incorporated into the enzyme complex, α4β4, whereas those in the patient's cells were present as monomers. We propose that formation of the enzyme complex is required for stabilization of trifunctional protein.
Bibliography:ObjectType-Case Study-2
SourceType-Scholarly Journals-1
ObjectType-Feature-4
content type line 23
ObjectType-Report-1
ObjectType-Article-3
ISSN:0006-291X
1090-2104
DOI:10.1006/bbrc.1996.0309