Turnover and Degradation of Mitochondria and Their Proteins

Grisolı́a, Santiago; Knecht, Erwin; Hernández-Yago, José; Wallace, R.

doi:10.1002/9780470720585.ch11

Cited by 6 publications

(3 citation statements)

References 13 publications

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“…Consistent with evidence indicating that turnover of mitochondrial inner membrane and matrix proteins depends upon mitophagy [133, 134], inhibition of autophagy enhanced the accumulation of red (older) MitoTimer [129], demonstrating the utility of the construct for the assessment of mitophagy.…”

Section: Introductionsupporting

confidence: 71%

Mitochondrial quality control: Easy come, easy go

Stotland¹,

Gottlieb²

2015

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

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“Friends come and go but enemies accumulate.”Arthur Bloch Mitochondrial networks in eukaryotic cells are maintained via regular cycles of degradation and biogenesis. These complex processes function in concert with one another to eliminate dysfunctional mitochondria in a specific and targeted manner and coordinate the biogenesis of new organelles. This review covers the two aspects of mitochondrial turnover, focusing on the main pathways and mechanisms involved. The review also summarizes the current methods and techniques for analyzing mitochondrial turnover in vivo and in vitro, from the whole animal proteome level to the level of single organelle.

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Section: Introductionsupporting

confidence: 71%

Mitochondrial quality control: Easy come, easy go

Stotland¹,

Gottlieb²

2015

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

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“…Autophagy has been found to be a self‐nutrient‐providing system for cell survival under starvation conditions , and an important system for degradation of miss‐folded or long‐lived proteins, and superfluous or damaged organelle such as mitochondria . Starvation‐caused poverty of nutrients induces autophagy for cell survival via autophagy‐mediated recycling of nutrients contained in cells themselves .…”

Section: Introductionmentioning

confidence: 99%

“…Autophagy has been found to be a self-nutrient-providing system for cell survival under starvation conditions [1][2][3], and an important system for degradation of miss-folded or long-lived proteins, and superfluous or damaged organelle such as mitochondria [4][5][6].…”

Section: Introductionmentioning

confidence: 99%

Cytosolic chloride ion is a key factor in lysosomal acidification and function of autophagy in human gastric cancer cell

Hosogi

Kusuzaki

Inui

et al. 2014

J Cellular Molecular Medi

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The purpose of the present study was to clarify roles of cytosolic chloride ion (Cl−) in regulation of lysosomal acidification [intra-lysosomal pH (pHlys)] and autophagy function in human gastric cancer cell line (MKN28). The MKN28 cells cultured under a low Cl− condition elevated pHlys and reduced the intra-lysosomal Cl− concentration ([Cl−]lys) via reduction of cytosolic Cl− concentration ([Cl−]c), showing abnormal accumulation of LC3II and p62 participating in autophagy function (dysfunction of autophagy) accompanied by inhibition of cell proliferation via G0/G1 arrest without induction of apoptosis. We also studied effects of direct modification of H+ transport on lysosomal acidification and autophagy. Application of bafilomycin A1 (an inhibitor of V-type H+-ATPase) or ethyl isopropyl amiloride [EIPA; an inhibitor of Na+/H+ exchanger (NHE)] elevated pHlys and decreased [Cl−]lys associated with inhibition of cell proliferation via induction of G0/G1 arrest similar to the culture under a low Cl− condition. However, unlike low Cl− condition, application of the compound, bafilomycin A1 or EIPA, induced apoptosis associated with increases in caspase 3 and 9 without large reduction in [Cl−]c compared with low Cl− condition. These observations suggest that the lowered [Cl−]c primarily causes dysfunction of autophagy without apoptosis via dysfunction of lysosome induced by disturbance of intra-lysosomal acidification. This is the first study showing that cytosolic Cl− is a key factor of lysosome acidification and autophagy.

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Protein degradation in human T-lymphocytes

et al. 1981

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Protein from resting or phytohemagglutinin-stimulated human peripheral blood T-lymphocytes, pulse-labeled 'in vitro' for 1 h with 3H-leucine, had a half-life of 30 h.Small, nondividing lymphocytes have been used to study the activation process induced by mitogens because metabolic, functional and morphological parameters undergo large-scale changes 1. Therefore, these cells also provide a convenient model to clarify the regulation of protein metabolism, because protein synthesis can be regulated in a precise way during activation. Although there has been considerable work on protein synthesis in lymphocytes 1, little has been done in the area of protein degradation, a process which is of equal importance with synthesis in maintaining and regulating the protein content of the cells 2. The present paper describes the general characteristics of protein degradation in human T-lymphocytes. Material and methods.Human peripheral blood T-lymphocytes were obtained as previously described 3. Cell viability, checked by trypan blue exclusion, was over 95% and differential counts showed 96.0% T-cells. Cells were incubated at 37 ~ in an atmosphere of 5% CO 2 in RPMI 1640 medium (Flow Lag, Irvine, Scotland) (106 viable cells/ml) with 10% foetal bovine serum 100 U/ml penicillin and 100 gg/ml streptomycin. For phytohemagglutinin (PHA) stimulation, T-cells were incubated at 37 ~ for 30 h in the same medium containing 25 gg/ml PHA-P (Difco Lag, Detroit, Michigan, USA). To study the time course of the stimulation, T-lymphocytes cultures were incubated as described above for 6, 24, 48, 72 and 96 h. 1 h before ending the incubation period, cultures were pulse-labeled with [methyl-3H]-thymidine (2 ~tCi/ml, 2 Ci/mmole). Autoradiographs were made, as previously described 4, by the 'stripping film' technique. Labeled and unlabeled lymphocytes were evaluated in 3 smears per case (300 cells/case). Lymphocytes from untreated chronic lymphocytic leukaemia (CLL) diagnosed as T-cell leukaemia were isolated and incubated under the same conditions as the normal lymphocytes. For radioactive labeling, cells were incubated in medium 3 containing L-[4, 5-HI leucine (0.05 mM, 52 Ci/mmole) for 1 h in siliconized Erlenmeyer flasks at 37~ with shaking. Then, the cells were washed 4 times with fresh medium containing 2 mM unlabeled leucine with 5 min incubations at 37 ~ between resuspension of the cells in medium and centrifugations at 300 x g. After washing, the cells were chased at 37~ in fresh medium containing 2 mM L-leucine for 24 h. Aliquots of medium were removed at different intervals, cooled in ice and centrifuged (300x g, 5 min) at 4 ~ The cell pellet was resuspended in phosphate buffered saline. Supernatants and cells were precipitated with 5% trichloroacetic acid (TCA). Precipitates were dissolved in 0.2 N NaOH. Radioactivity was determined by liquid scintillation counting. All counts were corrected for quenching using an internal standard. The TCA-soluble radioactivity of supernatant and cells at each time-point was calculated as the differen...

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Turnover and Degradation of Mitochondria and Their Proteins

Cited by 6 publications

References 13 publications

Mitochondrial quality control: Easy come, easy go

Mitochondrial quality control: Easy come, easy go

Cytosolic chloride ion is a key factor in lysosomal acidification and function of autophagy in human gastric cancer cell

Protein degradation in human T-lymphocytes

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