The physical association between rat liver mitochondria and rough endoplasmic reticulum

Pickett, Cecil B.; Montisano, D F; Eisner, David; Cascarano, Joseph

doi:10.1016/0014-4827(80)90070-1

Cited by 74 publications

(32 citation statements)

References 23 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This conclusion is strongly supported by ultrastructural observations (18,20,22). These show intimate contact between ER-like vesicles and mitochondria.…”

Section: Discussionsupporting

confidence: 60%

“…2, M). However, because mitochondria isolated by differential centrifugation have associated membranes (MAM), we removed these using a Percoll gradient as described previously (18,20) to generate ultrapure mitochondria. Percoll somehow dissociates these membranes from the mitochondria.…”

Section: Resultsmentioning

confidence: 99%

“…Moreover, mitochondria are closely associated with smooth membranous sacs that resemble the ER membranes. These ER-like membranes are referred to as mitochondria-associated membranes (MAMs) (18)(19)(20)(21)(22). Thus, perhaps ceramide is made in these membranes and transferred to mitochondria.…”

mentioning

confidence: 99%

See 2 more Smart Citations

Ceramide synthesis in the endoplasmic reticulum can permeabilize mitochondria to proapoptotic proteins

Stiban

Caputo

Colombini

2008

Journal of Lipid Research

137

114

View full text Add to dashboard Cite

Increased mitochondrial ceramide levels are associated with the initiation of apoptosis. There is evidence that ceramide is causal. Thus, the conversion of the precursor, dihydroceramide, to ceramide by the enzyme dihydroceramide desaturase may be important in preparing the cell for apoptosis. Ceramide can initiate apoptosis by permeabilizing the mitochondrial outer membrane to apoptosisinducing proteins. However, the mitochondrion's ability to produce ceramide may be limited by its proteome. Here, we show that ceramide synthesized in isolated mammalian endoplasmic reticulum (ER) vesicles from either C 8 -dihydroceramide or sphingosine to produce long-chain ceramide can transfer to isolated mitochondria. The rate of transfer is consistent with a simple collision model. The transfer of the long-chain ceramide is faster than expected for an uncatalyzed process. Sufficient ceramide is transferred to permeabilize the outer membrane to cytochrome c and adenylate kinase. The mitochondria-associated membranes, ER-like membranes that are tightly associated with isolated mitochondria, can produce enough ceramide to permeabilize the outer membrane transiently. Thus, this ceramide exchange obviates the need for a complete ceramide de novo pathway in mitochondria to increase ceramide levels to the critical value required for functional changes, such as ceramide channel self-assembly followed by protein release.-Stiban, J., L. Caputo, and M. Colombini. Ceramide synthesis in the endoplasmic reticulum can permeabilize mitochondria to proapoptotic proteins. J. Lipid Res. 2008. 49: 625-634.

show abstract

“…This conclusion is strongly supported by ultrastructural observations (18,20,22). These show intimate contact between ER-like vesicles and mitochondria.…”

Section: Discussionsupporting

confidence: 60%

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

Ceramide synthesis in the endoplasmic reticulum can permeabilize mitochondria to proapoptotic proteins

Stiban

Caputo

Colombini

2008

Journal of Lipid Research

137

114

View full text Add to dashboard Cite

show abstract

“…The nascent polypeptide chains associate with the membranes of the endoplasmic reticulum [43], which by itself is associated with mitochondria. In rat liver a close association of endoplasmic reticulum and mitochondria has been observed by electron microscopic studies [44] and by biochemical methods [42,44]. Although a processing proteinase has been localized in the mitochondrial matrix [37,38], proteinases of other localization may also be involved in the processing of the cytochrome c oxidase precursor.…”

Section: Discussionmentioning

confidence: 99%

Cell-Free Synthesis of a Larger-Molecular-Weight Precursor of Cytochrome c Oxidase Subunit V from Rat Liver and the Distribution of Its mRNA between Free and Membrane-Bound Polysomes

Schmelzer¹,

Northemann²,

Kadenbach³

et al. 1982

Eur J Biochem

View full text Add to dashboard Cite

Poly(A)-rich RNA from phenol-extracted rat liver polysomes was translated in a heterologous cell-free system derived from wheat germs. The labeled translation products were incubated with an antiserum against cytochrome c oxidase subunit V. After immunoprecipitation and affinity chromatography with protein-ASepharose, the isolated antigen-immunoglobulin complexes were analyzed by sodium dodecyl sulfate/polyacrylamide gel electrophoresis and fluorography. Only one protein with an apparent molecular weight of 15 500 was visualized. In immunocompetition experiments with unlabeled individual cytochrome c oxidase subunits IV, V, VI or VII only subunit V could compete with the 15 500-M, protein synthesited in vitro. Two-dimensional fingerprints of cytochrome c oxidase subunit V and the polypeptide synthesized in vitro showed a high degree of similarity. It is concluded that the cytochrome c oxidase subunit V is synthesized as a precursor with an aminoterminal extension of about 25 amino acids. It was possible to convert the precursor of cytochrome c oxidase subunit V synthesized in vitro to its mature form by intact mitochondria as well as by submitochondrial particles. A chain length of 830 f 70 nucleotides was estimated for the poly(A)-rich mRNA of the higher-molecular-weight precursor of rat liver cytochrome c oxidase subunit V. Assuming a molecular weight of 15 500 for the precursor a non-coding region of about 300 nucleotides must exist. In experiments on the site of synthesis it is shown that the poly(A)-rich RNA for the higher-molecular-weight precursor of cytochrome c oxidase subunit V is found in free, loosely and tightly membrane-bound polyribosomes.

show abstract

“…Furthermore, it became clear from very recent work of Ades and Butow [43] that the transport of mitochondria1 proteins into yeast mitochondria cannot be regarded as an exclusive posttranslational event. A close association between rough endoplasmic reticulum and mitochondria has been observed in vivo by electron microscopic studies of rat liver [44]. Complexes of rough endoplasmic reticulum and mitochondria have also been isolated from rat liver homogenates by differential centrifugation [20].…”

Section: Discussionmentioning

confidence: 99%

The Size and Distribution of Cytochrome c Oxidase Subunit IV mRNA between Free and Membrane‐Bound Polyribosomes

Northemann

Schmelzer

Heinrich

1981

European Journal of Biochemistry

View full text Add to dashboard Cite

A length of 990 ± 80 nucleotides was estimated for the poly(A)‐rich mRNA of the higher‐molecular‐weight precursor of rat liver cytochrome c oxidase subunit IV. Assuming a molecular weight of 19500 for the cytochrome c oxidase subunit IV precursor, a non‐coding region of about 350 necleotides must exist. In experiments in the site of synthesis it is shown that the poly(A)‐rich RNA for the higher‐molecular‐weight precursor of cytochrome c oxidase subunit IV is found in free, loosely and tightly membrane‐bound polyribosomes. This finding does not agree with the present picture of free polysomes as the exclusive site of synthesis for mitochondrial proteins.

show abstract

The physical association between rat liver mitochondria and rough endoplasmic reticulum

Cited by 74 publications

References 23 publications

Ceramide synthesis in the endoplasmic reticulum can permeabilize mitochondria to proapoptotic proteins

Ceramide synthesis in the endoplasmic reticulum can permeabilize mitochondria to proapoptotic proteins

Cell-Free Synthesis of a Larger-Molecular-Weight Precursor of Cytochrome c Oxidase Subunit V from Rat Liver and the Distribution of Its mRNA between Free and Membrane-Bound Polysomes

The Size and Distribution of Cytochrome c Oxidase Subunit IV mRNA between Free and Membrane‐Bound Polyribosomes

Contact Info

Product

Resources

About