期刊
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS
卷 1757, 期 9-10, 页码 1357-1365出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbabio.2006.07.007
关键词
respiratory chain complex; ATP synthase; HSP60; prohibitin; transglutaminase 2 knock out mice; protein disulphide isomerase
资金
- Medical Research Council [MC_U132670600] Funding Source: Medline
- Telethon [GGP06254] Funding Source: Medline
- MRC [MC_U132670600] Funding Source: UKRI
- Medical Research Council [MC_U132670600] Funding Source: researchfish
In this study we provide the first in vivo evidences showing that, under physiological conditions, tissue transglutaminase (TG2) might acts as a protein disulphide isomerase (PDI) and through this activity contributes to the correct assembly of the respiratory chain complexes. Mice lacking TG2 exhibit mitochondrial energy production impairment, evidenced by decreased ATP levels after physical challenge. This defect is phenotypically reflected in a dramatic decrease of motor behaviour of the animals. We propose that the molecular mechanism, underlying such a phenotype.. resides in a defective disulphide bonds formation in ATP synthase (complex V), NADH-ubiquinone oxidoreductase (complex I), succinate-ubiquinone oxidoreductase (complex II) and cytochrome c oxidase (complex IV). In addition, TG2-PDI might control the respiratory chain by modulating the formation of the prohibitin complexes. These data elucidate a new pathway that directly links the TG2-PDI enzymatic activity with the regulation of mitochondrial respiratory chain function. (c) 2006 Elsevier B.V. All rights reserved.
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