title: The expression of subunit c correlates with and thus may limit the biosynthesis of the mitochondrial F0F1-ATPase in brown adipose tissue.
abstract: A low content of mitochondrial ATPase in brown adipose tissue (BAT) has previously been found to contrast with high levels of the transcripts of the beta-subunit of the F1 part of the ATPase and of the transcripts of the mitochondrial encoded subunits (Houstĕk, J., Tvrdík, P., Pavelka, S., and Baudysová, M. (1991) FEBS Lett. 294, 191-194). To delineate which subunit limits the synthesis of the ATPase complex, we have studied the expression of the nuclear genes encoding subunits alpha, beta, and gamma of the catalytic F1 part and the b, c, d, and OSCP subunits of the F0 part of the ATPase. In comparison with other tissues of mice, high levels of transcripts of alpha-F1, beta-F1, gamma-F1, b-F0, d-Fo, and OSCP were found in BAT. The only genes expressed at a low level in BAT were those of the c-F0 subunit. The levels of c-F0 transcripts were 4-70-fold lower in BAT than in other tissues. An analogous expression pattern of the ATPase genes was found in BAT of adult rat and hamster. In BAT of newborn lamb, which, in contrast to other mammals, has a high content of mitochondrial ATPase, correspondingly high levels of c-F0 mRNA were found Expression of the c-F0 genes also correlated well with the ontogenic development of BAT in the hamster, being high during the first postnatal week when mitochondria are nonthermogenic and contain a relatively high amount of ATPase, but low on subsequent days when ATPase content decreases, as the thermogenic function develops. It is suggested that expression of the c-F0 genes and subsequent synthesis of the hydrophobic subunit c of the membrane-intrinsic F0 part of the enzyme may control the biosynthesis of the ATPase complex in BAT. An analogous regulatory role of the c-F0 subunit could be postulated in other tissues.
authors.affiliation: Institute of Physiology, Academy of Sciences of the Czech Republic, Prague.
authors.forename: J
authors.initials: J
authors.lastname: Houstĕk
authors.forename: U
authors.initials: U
authors.lastname: Andersson
authors.forename: P
authors.initials: P
authors.lastname: Tvrdík
authors.forename: J
authors.initials: J
authors.lastname: Nedergaard
authors.forename: B
authors.initials: B
authors.lastname: Cannon
mesh_terms: D000273:Adipose Tissue / Q000201:enzymology; D002001:Adipose Tissue, Brown / Q000201:enzymology* / Q000254:growth & development; D000375:Aging / Q000378:metabolism*; D000818:Animals; D000831:Animals, Newborn; D015152:Blotting, Northern; D001921:Brain / Q000201:enzymology; D006224:Cricetinae; D015342:DNA Probes; D015971:Gene Expression Regulation, Enzymologic; D046911:Macromolecular Substances; D008647:Mesocricetus; D051379:Mice; D008815:Mice, Inbred Strains; D008928:Mitochondria / Q000201:enzymology*; D008929:Mitochondria, Heart / Q000201:enzymology; D008930:Mitochondria, Liver / Q000201:enzymology; D018482:Muscle, Skeletal / Q000201:enzymology; D009928:Organ Specificity; D006180:Proton-Translocating ATPases / Q000096:biosynthesis*; D012333:RNA, Messenger / Q000032:analysis / Q000096:biosynthesis; D012756:Sheep
chemical_list: D015342:DNA Probes; D046911:Macromolecular Substances; D012333:RNA, Messenger; D006180:Proton-Translocating ATPases