Characterization of mitochondrial respiratory complexes involved in the regulation of myoblast differentiation

2021 ◽  
Author(s):  
Béatrice Chabi ◽  
Hanane Hennani ◽  
Fabienne Cortade ◽  
Chantal Wrutniak‐Cabello
Keyword(s):  
Myoblast Differentiation ◽  
Respiratory Complexes ◽  
Mitochondrial Respiratory

scholarly journals Mitochondrial DNA: Distribution, Mutations, and Elimination

Cells ◽  
2019 ◽  
Vol 8 (4) ◽  
pp. 379 ◽  
Author(s):  
Yan ◽  
Duanmu ◽  
Zeng ◽  
Liu ◽  
Song
Keyword(s):  
Mitochondrial Dna ◽  
Mitochondrial Matrix ◽  
Endonuclease G ◽  
Respiratory Complexes ◽  
Dna Distribution ◽  
Mitochondrial Functions ◽  
Mitochondrial Respiratory

Mitochondrion harbors its own DNA (mtDNA), which encodes many critical proteins for the assembly and activity of mitochondrial respiratory complexes. mtDNA is packed by many proteins to form a nucleoid that uniformly distributes within the mitochondrial matrix, which is essential for mitochondrial functions. Defects or mutations of mtDNA result in a range of diseases. Damaged mtDNA could be eliminated by mitophagy, and all paternal mtDNA are degraded by endonuclease G or mitophagy during fertilization. In this review, we describe the role and mechanism of mtDNA distribution and elimination. In particular, we focus on the regulation of paternal mtDNA elimination in the process of fertilization.

Characterization of human myoblast differentiation for tissue-engineering purposes by quantitative gene expression analysis

2011 ◽  
Vol 5 (8) ◽  
pp. e197-e206 ◽  
Author(s):  
Jens Stern-Straeter ◽  
Gabriel Alejandro Bonaterra ◽  
Stefan S. Kassner ◽  
Stefanie Zügel ◽  
Karl Hörmann ◽  
...  
Keyword(s):  
Gene Expression ◽  
Tissue Engineering ◽  
Expression Analysis ◽  
Gene Expression Analysis ◽  
Myoblast Differentiation ◽  
Quantitative Gene Expression ◽  
Human Myoblast

scholarly journals Enzymatic activities of mitochondrial respiratory complexes from children muscular biopsies. Age-related evolutions

1995 ◽  
Vol 1228 (1) ◽  
pp. 43-50 ◽  
Author(s):  
Etienne Lefai ◽  
Anne Terrier-Cayre ◽  
Annie Vincent ◽  
Odile Boespflug-Tanguy ◽  
Alain Tanguy ◽  
...  
Keyword(s):  
Enzymatic Activities ◽  
Respiratory Complexes ◽  
Age Related ◽  
Mitochondrial Respiratory

scholarly journals An Isolated Complex V Inefficiency and Dysregulated Mitochondrial Function in Immortalized Lymphocytes from ME/CFS Patients

2020 ◽  
Author(s):  
Daniel Missailidis ◽  
Sarah Annesley ◽  
Claire Allan ◽  
Oana Sanislav ◽  
Brett Lidbury ◽  
...  
Keyword(s):  
Steady State ◽  
Fatty Acid ◽  
Mitochondrial Function ◽  
Complex I ◽  
Atp Synthesis ◽  
Beta Oxidation ◽  
Respiratory Capacity ◽  
Respiratory Complexes ◽  
Stress Sensing ◽  
Mitochondrial Respiratory

Myalgic Encephalomyelitis/Chronic Fatigue Syndrome (ME/CFS) is an enigmatic condition characterized by exacerbation of symptoms after exertion (post-exertional malaise or “PEM”), and by fatigue whose severity and associated requirement for rest are excessive and disproportionate to the fatigue-inducing activity. There is no definitive molecular marker or known underlying pathological mechanism for the condition. Increasing evidence for aberrant energy metabolism suggests a role for mitochondrial dysfunction in ME/CFS. Our objective was therefore to measure mitochondrial function and cellular stress sensing in actively metabolising patient blood cells. We immortalized lymphoblasts isolated from 51 ME/CFS patients diagnosed according to the Canadian Consensus Criteria and an age- and gender-matched control group. Parameters of mitochondrial function and energy stress sensing were assessed by Seahorse extracellular flux analysis, proteomics, and an array of additional biochemical assays. As a proportion of the basal oxygen consumption rate (OCR), the rate of ATP synthesis by Complex V was significantly reduced in ME/CFS lymphoblasts, while significant elevations were observed in Complex I OCR, maximum OCR, spare respiratory capacity, nonmitochondrial OCR and “proton leak” as a proportion of the basal OCR. This was accompanied by a reduction of mitochondrial membrane potential, chronically hyperactivated TOR Complex I stress signalling and upregulated expression of mitochondrial respiratory complexes, fatty acid transporters and enzymes of the β-oxidation and TCA cycles. By contrast, mitochondrial mass and genome copy number, as well as glycolytic rates and steady state ATP levels were unchanged. Our results suggest a model in which ME/CFS lymphoblasts have a Complex V defect accompanied by compensatory upregulation of their respiratory capacity that includes the mitochondrial respiratory complexes, membrane transporters and enzymes involved in fatty acid β-oxidation. This homeostatically returns ATP synthesis and steady state levels to “normal” in the resting cells, but may leave them unable to adequately respond to acute increases in energy demand as the relevant homeostatic pathways are already activated.

Thrombopoietin (TPO) Regulates HIF-1α Level through Generation of Mitochondrial Reactive Oxygen Species (ROS).

Blood ◽  
2005 ◽  
Vol 106 (11) ◽  
pp. 3145-3145
Author(s):  
Kozue Yoshida ◽  
Keita Kirito ◽  
Kenneth Kaushansky ◽  
Norio Komatsu
Keyword(s):  
Stem Cells ◽  
Hematopoietic Stem Cells ◽  
Mitochondrial Function ◽  
Leukemic Cell ◽  
Complex Iii ◽  
Ros Generation ◽  
Ros Production ◽  
Hematopoietic Stem ◽  
Respiratory Complexes ◽  
Mitochondrial Respiratory

Abstract Hypoxia inducible factor (HIF)-1 is a master transcriptional regulator for adaptation of cells to hypoxia. In addition to hypoxic responses, HIF-1 also plays an important role in the development of hematopoietic stem cells. Genetic deletion of β subunit of HIF-1 causes impairment of hematopoiesis. Culture of hematopoietic stem cells under hypoxic condition induces elevation of HIF-1α , another subunit of HIF-1, and subsequently enhances the growth of these cells. In our previous work we found that thrombopoietin (TPO), an important and non-redundant cytokine required for normal stem cell development, induces HIF-1α elevation in the TPO-dependent human leukemic cell line UT-7/TPO and in Sca-1+/c-kit+/Gr-1- cells (Kirito, K. et.al. Blood 2005). Under normoxic conditions HIF-1α is hydroxylated on proline residues by prolyl hydroxylase (PHD), which leads to its recognition by the von Hippel-Lindau tumor suppressor protein (pVHL), leading to degradation of HIF-1α . Hypoxia inhibits PHD function, blocking ubiquitination of HIF-1α , stabilizing the protein. We found that TPO controls stability of HIF-1α even under normoxic conditions. However, the mechanism by which TPO controls the stability of the protein remains unclear. Recently, several groups have reported that mitochondrial ROS play crucial roles in stabilization of HIF-1α in response to hypoxia. Disruption of mitochondrial function, either by interfering RNA against complex III of the mitochondrial electron transport chain or genetic elimination of cytochrome c, completely abolished the hypoxia-induced HIF-1α response. Based on these findings we hypothesized that ROS might be involved in TPO-induced HIF-1α elevation. To examine our hypothesis, we first tested whether TPO induced ROS production in UT-7/TPO cells using 2′, 7′-dichlorofluorescein diacetate, a redox sensitive fluorescence dye, and found that the hormone clearly induced ROS production in these cells. Next, we analyzed whether TPO-induced ROS generation is required for accumulation of HIF-1α . Pre-treatment of UT-7/TPO cells with the ROS scavenger catalase completely blocked HIF-1α elevation after TPO treatment. Furthermore, diphenylene iodinium (DPI), an inhibitor for ROS generating flavoenzymes including mitochondrial respiratory complexes, also inhibited the effects of TPO on HIF-1α levels. These results indicate that TPO induced HIF-1α activation is mediated by ROS production. To study the molecular pathway(s) by which TPO affects ROS, we tested the effects of ROS blockade on several known TPO-responsive signaling molecules; neither DPI nor catalase affected the activation of JAK2, STAT5, p38-MAPK or p42/p44-ERK induced by TPO, although AKT activation was blocked. Moreover, LY294002, an inhibitor of PI3-kinase and its activation of AKT also blocked of the HIF-1α response to TPO. Finally, inhibition of mitochondrial function in UT-7/TPO cells with rotenone or oligomycin also inhibited TPO-dependent accumulation of HIF-1α without affecting Jak2 activation. In conclusion, we found that TPO regulates HIF-1α levels through activation of ROS generation within mitochondrial respiratory complexes. We speculate that TPO mimics hypoxia by induction of ROS generation at mitochondria and subsequent elevation of HIF-1α , and regulates important genes for metabolisms and survival of hematopoietic stem cells.

scholarly journals Defect of mitochondrial respiratory chain is a mechanism of ROS overproduction in a rat model of alcoholic liver disease: role of zinc deficiency

2016 ◽  
Vol 310 (3) ◽  
pp. G205-G214 ◽  
Author(s):  
Qian Sun ◽  
Wei Zhong ◽  
Wenliang Zhang ◽  
Zhanxiang Zhou
Keyword(s):  
Mitochondrial Dna ◽  
Liver Disease ◽  
Zinc Deficiency ◽  
Alcoholic Liver Disease ◽  
Alcohol Exposure ◽  
Ros Production ◽  
Chronic Alcohol ◽  
Respiratory Complexes ◽  
Chronic Alcohol Exposure ◽  
Mitochondrial Respiratory

Morphological and functional alterations of hepatic mitochondria have been documented in patients with alcoholic liver disease (ALD). Our recent study demonstrated that zinc level was decreased in whole liver and mitochondria by chronic alcohol feeding. The present study was undertaken to determine whether zinc deficiency mediates alcohol-induced mitochondrial electron transport chain (ETC) defect and whether defective ETC function may lead to generation of reactive oxygen species (ROS). Male Wistar rats were pair fed with the Lieber-DeCarli control or ethanol diet for 5 mo. Chronic alcohol exposure increased hepatic triglyceride, free fatty acid, and 4-hydroxynonenal (4HNE) levels; meanwhile hepatic mitochondrial 4HNE level was also increased. Moreover, hepatic mitochondrial respiratory complexes I, III, IV, and V and hepatic ATP production were decreased by chronic alcohol exposure. Chronic alcohol feeding decreased peroxisome proliferator-activated receptor gamma coactivator-1-alpha (PGC1α), nuclear respiratory factor 1 (NRF1), mitochondrial transcription factor A (TFAM), and mitochondrial DNA. HepG2 cells were treated with N, N, N′, N′-tetrakis (2-pyridylmethyl) ethylenediamine (TPEN) for 6 h. Zinc deficiency significantly decreased mitochondrial respiratory complexes I, III, and IV. In addition, PGC1α, NRF1, and TFAM levels as well as mitochondrial DNA were significantly decreased by TPEN treatment. Knockdown of mitochondrial respiratory complexes I, III, or IV by shRNA caused a decrease in mitochondrial membrane potential and an increase in ROS production. These results suggest that alcohol-induced hepatic zinc deficiency could inactivate mitochondrial biogenesis pathway and decrease mitochondrial DNA replication, which, in turn, decreases mitochondrial complex protein expression. The defect of mitochondrial respiratory complexes may worsen alcohol-induced ROS production.

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