Rapid postnatal changes in F1-ATPase proteins and in the uncoupling protein in brown adipose tissue mitochondria of the newborn rat

Luis, A M; Cuezva, J M

doi:10.1016/0006-291x(89)92425-x

Cited by 14 publications

(5 citation statements)

References 12 publications

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“…organelles [11,15,16] or in the liver in situ [11], as well as in the regenerating liver [17], in other mammalian tissues [18,19] and in other organisms [20][21][22][23].…”

Section: Introductionmentioning

confidence: 99%

Subcellular structure containing mRNA for β subunit of mitochondrial H+-ATP synthase in rat hepatocytes is translationally active

Ricart

Egea

Izquierdo

et al. 1997

Biochemical Journal

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We have recently reported that the nuclear-encoded mRNA for the beta subunit of mitochondrial H+-ATP synthase (beta-mRNA) is localized in rounded, electron-dense clusters in the cytoplasm of rat hepatocytes. Clusters of beta-mRNA are often found in close proximity to mitochondria. These findings suggested a role for these structures in controlling the cytoplasmic expression and sorting of the encoded mitochondrial precursor. Here we have addressed the question of whether the structures containing beta-mRNA are translationally active. For this purpose a combination of high-resolution in situ hybridization and immunocytochemical procedures was used. Three different co-localization criteria showed that beta-mRNA-containing structures always revealed positive immunoreactive signals for mitochondrial H+-ATP synthase (F1-ATPase), ribosomal and hsc70 proteins. Furthermore, clusters show evidence in situ of developmental changes in the translational efficiency of the beta-mRNA. These findings suggest that structures containing beta-mRNA are translationally active irrespective of their cytoplasmic location. The immunocytochemical quantification of the cytoplasmic presentation of hsc70 in the hepatocyte reveals that approx. 86% of the protein has a dispersed distribution pattern. However, the remaining hsc70 is presented in clusters of which only half reveal positive hybridization for beta-mRNA. The interaction of hsc70 with the beta-F1-ATPase precursor protein is documented by the co-localization of F1-ATPase immunoreactive material within cytoplasmic clusters of hsc70 and by the co-immunoprecipitation of hsc70 with the beta-subunit precursor from liver post-mitochondrial supernatants. Taken together, these results suggest a role for hsc70 in the translation/sorting pathway of the mammalian precursor of the beta-F1-ATPase protein.

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“…organelles [11,15,16] or in the liver in situ [11], as well as in the regenerating liver [17], in other mammalian tissues [18,19] and in other organisms [20][21][22][23].…”

Section: Introductionmentioning

confidence: 99%

Subcellular structure containing mRNA for β subunit of mitochondrial H+-ATP synthase in rat hepatocytes is translationally active

Ricart

Egea

Izquierdo

et al. 1997

Biochemical Journal

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“…The postnatal development of mitochondrial function has been studied previously in liver [15][16][17] and in brown adipose tissue [ 18]. In both tissues, postnatal development of the mitochondrial respiratory complexes takes place during the first hour of extrauterine life [1 ].…”

Section: Introductionmentioning

confidence: 99%

Postnatal Development of the Complexes of the Electron Transport Chain in Isolated Rat Brain Mitochondria

et al. 1994

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The postnatal development of the complexes of the electron transport chain in isolated rat brain mitochondria were investigated. Nonsynaptosomal brain mitochondria were isolated from rats aged 1–60 days, and the activities of mitochondrial complexes I, II–III, IV, V and citrate synthase were measured. There was a significant increase in the activity of complex I from postnatal day 1 to day 21, and in the activities of complex II–III, complex IV and citrate synthase from postnatal day 1 to day 60. In contrast, the activity of complex V increased significantly between postnatal day 1 and day 10 where it attained adult levels. These data are consistent with the increasing demand for mitochondrial ATP production as the brain develops and as aerobic glycolysis becomes the major pathway for energy production.

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“…SDS-polyacrylamide gel electrophoresis fractionation of mitochondrial and peroxisomal proteins (fractions 5 and 15 of the gradient, respectively) and Western-blotting with rabbit anti-[rat liver mitochondrial Fi-ATPase] serum (Fig. 2B), revealed the expected existence of the (Y and ,8 subunits of the Fi-ATPase complex in the mitochondrial fraction [10,21] and the existence of a single immunoreactive protein in the peroxisomal fraction with an apparent molecular weight similar to the a-subunit of the mitochondrial F1 complex.…”

Section: Resultsmentioning

confidence: 99%

Immunological detection of the mitochondrial F₁‐ATPase α subunit in the matrix of rat liver peroxisomes

et al. 1990

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Rat liver peroxisomes contain in their matrix the a-subunit of the mitochondrial F,-ATPase complex. The identification of this protein in liver peroxisomes has been achieved by immunoelectron microscopy and subcellular fractionation. No /?-subunit of the mitochondrial F,-ATPase complex was detected in the peroxisomal fractions obtained in sucrose gradients or in Nycodenz pelletkd peroxisomes. The consensus peroxisomal targeting sequence (Ala-Lys-Leu) is found at the carboxy terminus of the mature cc-subunit from bovine heart and rat liver mitochondria. Due to the dual subcellular localization of the a-subunit and to the structural homologies that exist between this protein and molecular chaperones [(1990) Biol. Chem. 265,7713-77161 it is suggested that the protein should perform another functional role(s) in both organelles, plus to its characteristic involvement in the regulation of mitochondrial ATPase activity.

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Rapid postnatal changes in F1-ATPase proteins and in the uncoupling protein in brown adipose tissue mitochondria of the newborn rat

Cited by 14 publications

References 12 publications

Subcellular structure containing mRNA for β subunit of mitochondrial H+-ATP synthase in rat hepatocytes is translationally active

Subcellular structure containing mRNA for β subunit of mitochondrial H+-ATP synthase in rat hepatocytes is translationally active

Postnatal Development of the Complexes of the Electron Transport Chain in Isolated Rat Brain Mitochondria

Immunological detection of the mitochondrial F₁‐ATPase α subunit in the matrix of rat liver peroxisomes

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Rapid postnatal changes in F1-ATPase proteins and in the uncoupling protein in brown adipose tissue mitochondria of the newborn rat

Cited by 14 publications

References 12 publications

Subcellular structure containing mRNA for β subunit of mitochondrial H+-ATP synthase in rat hepatocytes is translationally active

Subcellular structure containing mRNA for β subunit of mitochondrial H+-ATP synthase in rat hepatocytes is translationally active

Postnatal Development of the Complexes of the Electron Transport Chain in Isolated Rat Brain Mitochondria

Immunological detection of the mitochondrial F1‐ATPase α subunit in the matrix of rat liver peroxisomes

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Immunological detection of the mitochondrial F₁‐ATPase α subunit in the matrix of rat liver peroxisomes