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Article ; Online: Understanding differential aspects of microdiffusion (channeling) in the Coenzyme Q and Cytochrome c regions of the mitochondrial respiratory system.

Lenaz, Giorgio / Nesci, Salvatore / Genova, Maria Luisa

2023 Volume 74, Page(s) 101822

Abstract: Over the past decades, models of the organization of mitochondrial respiratory system have been controversial. The goal of this perspective is to assess this "conflict of models" by focusing on specific kinetic evidence in the two distinct segments of ... ...

Abstract	Over the past decades, models of the organization of mitochondrial respiratory system have been controversial. The goal of this perspective is to assess this "conflict of models" by focusing on specific kinetic evidence in the two distinct segments of Coenzyme Q- and Cytochrome c-mediated electron transfer. Respiratory supercomplexes provide kinetic advantage by allowing a restricted diffusion of Coenzyme Q and Cytochrome c, and short-range interaction with their partner enzymes. In particular, electron transfer from NADH is compartmentalized by channeling of Coenzyme Q within supercomplexes, whereas succinate oxidation proceeds separately using the free Coenzyme Q pool. Previous evidence favoring Coenzyme Q random diffusion in the NADH-dependent electron transfer is due to downstream flux interference and misinterpretation of results. Indeed, electron transfer by complexes III and IV via Cytochrome c is less strictly dependent on substrate channeling in mammalian mitochondria. We briefly describe these differences and their physiological implications.
MeSH term(s)	Ubiquinone/metabolism ; Cytochrome c Group/metabolism ; Animals ; Cattle ; Mammals/metabolism ; Electron Transport Chain Complex Proteins/metabolism ; Mitochondria/metabolism ; Heart/physiology ; Swine
Chemical Substances	Ubiquinone (1339-63-5) ; Cytochrome c Group ; Electron Transport Chain Complex Proteins
Language	English
Publishing date	2023-11-30
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2056923-3
ISSN	1872-8278 ; 1567-7249
ISSN (online)	1872-8278
ISSN	1567-7249
DOI	10.1016/j.mito.2023.11.005
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Article ; Online: The Interplay Between Respiratory Supercomplexes and ROS in Aging.

Genova, Maria Luisa / Lenaz, Giorgio

Antioxidants & redox signaling

2015 Volume 23, Issue 3, Page(s) 208–238

Abstract: Significance: The molecular mechanism of aging is still vigorously debated, although a general consensus exists that mitochondria are significantly involved in this process. However, the previously postulated role of mitochondrial-derived reactive ... ...

Abstract	Significance: The molecular mechanism of aging is still vigorously debated, although a general consensus exists that mitochondria are significantly involved in this process. However, the previously postulated role of mitochondrial-derived reactive oxygen species (ROS) as the damaging agents inducing functional loss in aging has fallen out of favor in the recent past. In this review, we critically examine the role of ROS in aging in the light of recent advances on the relationship between mitochondrial structure and function. Recent advances: The functional mitochondrial respiratory chain is now recognized as a reflection of the dynamic association of respiratory complexes in the form of supercomplexes (SCs). Besides providing kinetic advantage (channeling), SCs control ROS generation by the respiratory chain, thus providing a means to regulate ROS levels in the cell. Depending on their concentration, these ROS are either physiological signals essential for the life of the cell or toxic species that damage cell structure and functions. Critical issues: We propose that under physiological conditions the dynamic nature of SCs reversibly controls the generation of ROS as signals involved in mitochondrial-nuclear communication. During aging, there is a progressive loss of control of ROS generation so that their production is irreversibly enhanced, inducing a vicious circle in which signaling is altered and structural damage takes place. Future directions: A better understanding on the forces affecting SC association would allow the manipulation of ROS generation, directing these species to their physiological signaling role.
MeSH term(s)	Aging ; Animals ; Electron Transport ; Electron Transport Complex I/metabolism ; Electron Transport Complex II/metabolism ; Humans ; Mitochondria/metabolism ; Mitochondria/pathology ; Reactive Oxygen Species/metabolism ; Signal Transduction
Chemical Substances	Reactive Oxygen Species ; respiratory complex II ; Electron Transport Complex II (EC 1.3.5.1) ; Electron Transport Complex I (EC 1.6.5.3)
Language	English
Publishing date	2015-03-25
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1483836-9
ISSN	1557-7716 ; 1523-0864
ISSN (online)	1557-7716
ISSN	1523-0864
DOI	10.1089/ars.2014.6214
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Article: Shared and Distinctive Ultrastructural Abnormalities Expressed by Megakaryocytes in Bone Marrow and Spleen From Patients With Myelofibrosis.

Zingariello, Maria / Rosti, Vittorio / Vannucchi, Alessandro M / Guglielmelli, Paola / Mazzarini, Maria / Barosi, Giovanni / Genova, Maria Luisa / Migliaccio, Anna Rita

Frontiers in oncology

2020 Volume 10, Page(s) 584541

Abstract: Numerous studies have documented ultrastructural abnormalities in malignant megakaryocytes from bone marrow (BM) of myelofibrosis patients but the morphology of these cells in spleen, an important extramedullary site in this disease, was not investigated ...

Abstract	Numerous studies have documented ultrastructural abnormalities in malignant megakaryocytes from bone marrow (BM) of myelofibrosis patients but the morphology of these cells in spleen, an important extramedullary site in this disease, was not investigated as yet. By transmission-electron microscopy, we compared the ultrastructural features of megakaryocytes from BM and spleen of myelofibrosis patients and healthy controls. The number of megakaryocytes was markedly increased in both BM and spleen. However, while most of BM megakaryocytes are immature, those from spleen appear mature with well-developed demarcation membrane systems (DMS) and platelet territories and are surrounded by platelets. In BM megakaryocytes, paucity of DMS is associated with plasma (thick with protrusions) and nuclear (dilated with large pores) membrane abnormalities and presence of numerous glycosomes, suggesting a skewed metabolism toward insoluble polyglucosan accumulation. By contrast, the membranes of the megakaryocytes from the spleen were normal but these cells show mitochondria with reduced crests, suggesting deficient aerobic energy-metabolism. These distinctive morphological features suggest that malignant megakaryocytes from BM and spleen express distinctive metabolic impairments that may play different roles in the pathogenesis of myelofibrosis.
Language	English
Publishing date	2020-11-16
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2649216-7
ISSN	2234-943X
ISSN	2234-943X
DOI	10.3389/fonc.2020.584541
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Article: Functional role of mitochondrial respiratory supercomplexes.

Genova, Maria Luisa / Lenaz, Giorgio

Biochimica et biophysica acta

2014 Volume 1837, Issue 4, Page(s) 427–443

Abstract: Recent experimental evidence has replaced the random diffusion model of electron transfer with a model of supramolecular organisation based upon specific interactions between individual respiratory complexes. These supercomplexes were found to be ... ...

Abstract	Recent experimental evidence has replaced the random diffusion model of electron transfer with a model of supramolecular organisation based upon specific interactions between individual respiratory complexes. These supercomplexes were found to be functionally relevant by flux control analysis and to confer a kinetic advantage to NAD-linked respiration (channelling). However, the Coenzyme Q pool is still required for FAD-linked oxidations and for the proper equilibrium with Coenzyme Q bound in the supercomplex. Channelling in the cytochrome c region probably also occurs but does not seem to confer a particular kinetic advantage. The supramolecular association of individual complexes strongly depends on membrane lipid amount and composition and is affected by lipid peroxidation; it also seems to be modulated by membrane potential and protein phosphorylation. Additional properties of supercomplexes are stabilisation of Complex I, as evidenced by the destabilising effect on Complex I of mutations in either Complex III or IV, and prevention of excessive generation of reactive oxygen species. The dynamic character of the supercomplexes allows their involvement in metabolic adaptations and in control of cellular signalling pathways. This article is part of a Special Issue entitled: Dynamic and ultrastructure of bioenergetic membranes and their components.
MeSH term(s)	Cell Respiration ; Kinetics ; Membrane Lipids/metabolism ; Mitochondria/metabolism ; Mitochondrial Membranes/metabolism ; Models, Biological ; Multienzyme Complexes/metabolism ; Oxidation-Reduction ; Oxidative Phosphorylation ; Ubiquinone/metabolism
Chemical Substances	Membrane Lipids ; Multienzyme Complexes ; Ubiquinone (1339-63-5)
Language	English
Publishing date	2014-04
Publishing country	Netherlands
Document type	Journal Article ; Review
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbabio.2013.11.002
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Article: Dexamethasone Predisposes Human Erythroblasts Toward Impaired Lipid Metabolism and Renders Their

Zingariello, Maria / Bardelli, Claudio / Sancillo, Laura / Ciaffoni, Fiorella / Genova, Maria Luisa / Girelli, Gabriella / Migliaccio, Anna Rita

Frontiers in physiology

2019 Volume 10, Page(s) 281

Abstract: Cultures of stem cells from discarded sources supplemented with dexamethasone, a synthetic glucocorticoid receptor agonist, generate cultured red blood cells (cRBCs) in numbers sufficient for transfusion. According to the literature, however, ... ...

Abstract	Cultures of stem cells from discarded sources supplemented with dexamethasone, a synthetic glucocorticoid receptor agonist, generate cultured red blood cells (cRBCs) in numbers sufficient for transfusion. According to the literature, however, erythroblasts generated with dexamethasone exhibit low enucleation rates giving rise to cRBCs that survive poorly
Language	English
Publishing date	2019-04-04
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2564217-0
ISSN	1664-042X
ISSN	1664-042X
DOI	10.3389/fphys.2019.00281
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Article ; Online: A critical appraisal of the role of respiratory supercomplexes in mitochondria.

Genova, Maria Luisa / Lenaz, Giorgio

Biological chemistry

2013 Volume 394, Issue 5, Page(s) 631–639

Abstract: Substantial evidence exists that the mitochondrial respiratory chain is organized in supramolecular units called supercomplexes or respirasomes. While the structural evidence of the supercomplexes is overwhelming, fewer studies have focused on their ... ...

Abstract	Substantial evidence exists that the mitochondrial respiratory chain is organized in supramolecular units called supercomplexes or respirasomes. While the structural evidence of the supercomplexes is overwhelming, fewer studies have focused on their functional relevance. Although the presence of coenzyme Q channeling between complexes I and III has been ascertained, no such clear demonstration has been carried out for cytochrome c between complexes III and IV, at least in mammalian mitochondria. This review also discusses the implications concerning the number of respiratory complexes organized in supercomplexes and the possibility that they represent associations in dynamic equilibrium with the individual complexes.
MeSH term(s)	Cell Respiration/physiology ; Cytochromes c/analysis ; Cytochromes c/metabolism ; Electron Transport ; Humans ; Mitochondria/chemistry ; Mitochondria/metabolism ; Ubiquinone/analysis ; Ubiquinone/metabolism
Chemical Substances	Ubiquinone (1339-63-5) ; Cytochromes c (9007-43-6)
Language	English
Publishing date	2013-05
Publishing country	Germany
Document type	Journal Article ; Review
ZDB-ID	1334659-3
ISSN	1437-4315 ; 1431-6730 ; 1432-0355
ISSN (online)	1437-4315
ISSN	1431-6730 ; 1432-0355
DOI	10.1515/hsz-2012-0317
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Article: Functional role of mitochondrial respiratory supercomplexes

Genova, Maria Luisa / Giorgio Lenaz

Biochimica et biophysica acta. 2014 Apr., v. 1837, no. 4

2014

Abstract	Recent experimental evidence has replaced the random diffusion model of electron transfer with a model of supramolecular organisation based upon specific interactions between individual respiratory complexes. These supercomplexes were found to be functionally relevant by flux control analysis and to confer a kinetic advantage to NAD-linked respiration (channelling). However, the Coenzyme Q pool is still required for FAD-linked oxidations and for the proper equilibrium with Coenzyme Q bound in the supercomplex. Channelling in the cytochrome c region probably also occurs but does not seem to confer a particular kinetic advantage. The supramolecular association of individual complexes strongly depends on membrane lipid amount and composition and is affected by lipid peroxidation; it also seems to be modulated by membrane potential and protein phosphorylation. Additional properties of supercomplexes are stabilisation of Complex I, as evidenced by the destabilising effect on Complex I of mutations in either Complex III or IV, and prevention of excessive generation of reactive oxygen species. The dynamic character of the supercomplexes allows their involvement in metabolic adaptations and in control of cellular signalling pathways. This article is part of a Special Issue entitled: Dynamic and ultrastructure of bioenergetic membranes and their components.
Keywords	cytochrome c ; electron transfer ; lipid peroxidation ; lipids ; membrane potential ; mitochondria ; models ; mutation ; protein phosphorylation ; reactive oxygen species ; signal transduction ; ubiquinones ; ultrastructure
Language	English
Dates of publication	2014-04
Size	p. 427-443.
Publishing place	Elsevier B.V.
Document type	Article
ZDB-ID	282711-6
ISSN	0005-2728 ; 0304-4173
ISSN	0005-2728 ; 0304-4173
DOI	10.1016/j.bbabio.2013.11.002
Database	NAL-Catalogue (AGRICOLA)

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Article: Supramolecular organisation of the mitochondrial respiratory chain: a new challenge for the mechanism and control of oxidative phosphorylation.

Lenaz, Giorgio / Genova, Maria Luisa

Advances in experimental medicine and biology

2012 Volume 748, Page(s) 107–144

Abstract: Recent experimental evidence has replaced the random diffusion model of electron transfer with a model of supramolecular organisation based on specific interactions between individual respiratory complexes. These supercomplexes are detected by blue- ... ...

Abstract	Recent experimental evidence has replaced the random diffusion model of electron transfer with a model of supramolecular organisation based on specific interactions between individual respiratory complexes. These supercomplexes are detected by blue-native electrophoresis and are found to be functionally relevant by flux control analysis; moreover, they have been isolated and characterised by single-particle electron microscopy. The supramolecular association of individual complexes strongly depends on membrane lipid amount and composition and is affected by lipid peroxidation; it also seems to be modulated by membrane potential and protein phosphorylation. Supercomplex association confers several new properties with respect to the non-associated respiratory complexes to the respiratory chain: the most obvious is substrate channelling, specifically addressing Coenzyme Q and cytochrome c to interact directly with the partner enzymes without the need of a less efficient random diffusion step; in addition, supramolecular association may provide a further rate advantage by conferring long-range conformational changes to the individual complexes. Additional properties are stabilisation of Complex I, as evidenced by the destabilising effect on Complex I of mutations in either Complex III or Complex IV, and prevention of excessive generation of reactive oxygen species. On the basis of the properties described above, we hypothesise that an oxidative stress acts primarily by disassembling supercomplex associations thereby establishing a vicious circle of oxidative stress and energy failure, ultimately leading to cell damage and disease. We provide evidence that in physiological ageing and in some disease states, characterised by oxidative stress and mitochondrial damage, such as heart failure, neurodegenerative disorders and cancer, a loss of supercomplex association occurs, in line with our working hypothesis.
MeSH term(s)	Aging/metabolism ; Animals ; Electron Transport ; Electron Transport Complex I/chemistry ; Electron Transport Complex I/physiology ; Electron Transport Complex IV/chemistry ; Electron Transport Complex IV/physiology ; Humans ; Membrane Potential, Mitochondrial ; Mitochondria/metabolism ; Multienzyme Complexes/physiology ; Oxidative Phosphorylation
Chemical Substances	Multienzyme Complexes ; Electron Transport Complex I (EC 1.6.5.3) ; Electron Transport Complex IV (EC 1.9.3.1)
Language	English
Publishing date	2012
Publishing country	United States
Document type	Journal Article ; Review
ISSN	2214-8019 ; 0065-2598
ISSN (online)	2214-8019
ISSN	0065-2598
DOI	10.1007/978-1-4614-3573-0_5
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Article ; Online: Biohybrid Bovine Bone Matrix for Controlled Release of Mesenchymal Stem/Stromal Cell Lyosecretome: A Device for Bone Regeneration.

Bari, Elia / Roato, Ilaria / Perale, Giuseppe / Rossi, Filippo / Genova, Tullio / Mussano, Federico / Ferracini, Riccardo / Sorlini, Marzio / Torre, Maria Luisa / Perteghella, Sara

International journal of molecular sciences

2021 Volume 22, Issue 8

Abstract: ... ...

Abstract	SmartBone
MeSH term(s)	Animals ; Bone Matrix/chemistry ; Bone Regeneration/drug effects ; Bone Substitutes/chemistry ; Bone Substitutes/pharmacology ; Cattle ; Cell Differentiation/drug effects ; Delayed-Action Preparations/chemistry ; Delayed-Action Preparations/pharmacology ; Extracellular Vesicles/chemistry ; Extracellular Vesicles/genetics ; Humans ; Mesenchymal Stem Cell Transplantation ; Mesenchymal Stem Cells/chemistry ; Mesenchymal Stem Cells/drug effects ; Osteoblasts/drug effects ; Osteogenesis/drug effects ; Plastic Surgery Procedures/methods
Chemical Substances	Bone Substitutes ; Delayed-Action Preparations
Language	English
Publishing date	2021-04-14
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms22084064
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Article ; Online: New developments on the functions of coenzyme Q in mitochondria.

Genova, Maria Luisa / Lenaz, Giorgio

BioFactors (Oxford, England)

2011 Volume 37, Issue 5, Page(s) 330–354

Abstract: The notion of a mobile pool of coenzyme Q (CoQ) in the lipid bilayer has changed with the discovery of respiratory supramolecular units, in particular the supercomplex comprising complexes I and III; in this model, the electron transfer is thought to be ... ...

Abstract	The notion of a mobile pool of coenzyme Q (CoQ) in the lipid bilayer has changed with the discovery of respiratory supramolecular units, in particular the supercomplex comprising complexes I and III; in this model, the electron transfer is thought to be mediated by tunneling or microdiffusion, with a clear kinetic advantage on the transfer based on random collisions. The CoQ pool, however, has a fundamental function in establishing a dissociation equilibrium with bound quinone, besides being required for electron transfer from other dehydrogenases to complex III. The mechanism of CoQ reduction by complex I is analyzed regarding recent developments on the crystallographic structure of the enzyme, also in relation to the capacity of complex I to generate superoxide. Although the mechanism of the Q-cycle is well established for complex III, involvement of CoQ in proton translocation by complex I is still debated. Some additional roles of CoQ are also examined, such as the antioxidant effect of its reduced form and the capacity to bind the permeability transition pore and the mitochondrial uncoupling proteins. Finally, a working hypothesis is advanced on the establishment of a vicious circle of oxidative stress and supercomplex disorganization in pathological states, as in neurodegeneration and cancer.
MeSH term(s)	Aging/metabolism ; Animals ; Apoptosis ; Electron Transport ; Humans ; Ion Channels/metabolism ; Mitochondria/enzymology ; Mitochondria/metabolism ; Models, Molecular ; Molecular Targeted Therapy ; Multienzyme Complexes/chemistry ; Multienzyme Complexes/metabolism ; Neoplasms/drug therapy ; Neoplasms/metabolism ; Neurodegenerative Diseases/drug therapy ; Neurodegenerative Diseases/metabolism ; Oxidative Stress ; Protein Conformation ; Protein Stability ; Superoxides/metabolism ; Ubiquinone/chemistry ; Ubiquinone/metabolism
Chemical Substances	Ion Channels ; Multienzyme Complexes ; Superoxides (11062-77-4) ; Ubiquinone (1339-63-5)
Language	English
Publishing date	2011-09
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	59230-4
ISSN	1872-8081 ; 0951-6433
ISSN (online)	1872-8081
ISSN	0951-6433
DOI	10.1002/biof.168
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