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  1. Article ; Online: Modulation and Pharmacology of the Mitochondrial Permeability Transition

    Andrea Carrer / Claudio Laquatra / Ludovica Tommasin / Michela Carraro

    Molecules, Vol 26, Iss 6463, p

    A Journey from F-ATP Synthase to ANT

    2021  Volume 6463

    Abstract: The permeability transition (PT) is an increased permeation of the inner mitochondrial membrane due to the opening of the PT pore (PTP), a Ca 2+ -activated high conductance channel involved in Ca 2+ homeostasis and cell death. Alterations of the PTP have ...

    Abstract The permeability transition (PT) is an increased permeation of the inner mitochondrial membrane due to the opening of the PT pore (PTP), a Ca 2+ -activated high conductance channel involved in Ca 2+ homeostasis and cell death. Alterations of the PTP have been associated with many pathological conditions and its targeting represents an incessant challenge in the field. Although the modulation of the PTP has been extensively explored, the lack of a clear picture of its molecular nature increases the degree of complexity for any target-based approach. Recent advances suggest the existence of at least two mitochondrial permeability pathways mediated by the F-ATP synthase and the ANT, although the exact molecular mechanism leading to channel formation remains elusive for both. A full comprehension of this to-pore conversion will help to assist in drug design and to develop pharmacological treatments for a fine-tuned PT regulation. Here, we will focus on regulatory mechanisms that impinge on the PTP and discuss the relevant literature of PTP targeting compounds with particular attention to F-ATP synthase and ANT.
    Keywords permeability transition ; calcium ; F-ATP synthase ; adenine nucleotide translocator ; cyclophilin D ; mitochondrial channels ; Organic chemistry ; QD241-441
    Language English
    Publishing date 2021-10-01T00:00:00Z
    Publisher MDPI AG
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  2. Article ; Online: Analogies between COVID-19 and Preeclampsia

    Valentina Giardini / Carlo Gambacorti-Passerini / Marco Casati / Andrea Carrer / Patrizia Vergani

    International Journal of Translational Medicine, Vol 3, Iss 15, Pp 203-

    Focus on Therapies

    2023  Volume 216

    Abstract: Preeclampsia is an obstetric pathology with striking similarities to COVID-19. The renin-angiotensin system plays a key role in the pathogenesis of both diseases. This report reviews the pharmacological strategies that have been suggested for the ... ...

    Abstract Preeclampsia is an obstetric pathology with striking similarities to COVID-19. The renin-angiotensin system plays a key role in the pathogenesis of both diseases. This report reviews the pharmacological strategies that have been suggested for the prevention and treatment of preeclampsia and that are potentially useful also in the treatment of COVID-19. Of note, both pathologies have in common an Angiotensin II-mediated endothelial dysfunction secondary to an angiogenic imbalance, with effects on vasculature, coagulation, and inflammation. These considerations are drawn from cases of the initial SARS-CoV-2 primary infection and may not apply to more recent SARS-CoV-2 variants or infections after COVID vaccination. The treatment options discussed included albumin infusion, aspirin, corticosteroids, the monoclonal antibody eculizumab, hydroxychloroquine, low molecular weight heparin, magnesium, melatonin, metformin, nitric oxide, proton pump inhibitors, statins, therapeutic apheresis, and vitamin D.
    Keywords COVID-19 ; SARS-CoV-2 ; preeclampsia ; renin-angiotensin system ; angiogenic factors ; PlGF ; Computer applications to medicine. Medical informatics ; R858-859.7
    Subject code 610
    Language English
    Publishing date 2023-04-01T00:00:00Z
    Publisher MDPI AG
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  3. Article ; Online: Mitochondrial Ion Channels of the Inner Membrane and Their Regulation in Cell Death Signaling

    Andrea Urbani / Elena Prosdocimi / Andrea Carrer / Vanessa Checchetto / Ildikò Szabò

    Frontiers in Cell and Developmental Biology, Vol

    2021  Volume 8

    Abstract: Mitochondria are bioenergetic organelles with a plethora of fundamental functions ranging from metabolism and ATP production to modulation of signaling events leading to cell survival or cell death. Ion channels located in the outer and inner ... ...

    Abstract Mitochondria are bioenergetic organelles with a plethora of fundamental functions ranging from metabolism and ATP production to modulation of signaling events leading to cell survival or cell death. Ion channels located in the outer and inner mitochondrial membranes critically control mitochondrial function and, as a consequence, also cell fate. Opening or closure of mitochondrial ion channels allow the fine-tuning of mitochondrial membrane potential, ROS production, and function of the respiratory chain complexes. In this review, we critically discuss the intracellular regulatory factors that affect channel activity in the inner membrane of mitochondria and, indirectly, contribute to cell death. These factors include various ligands, kinases, second messengers, and lipids. Comprehension of mitochondrial ion channels regulation in cell death pathways might reveal new therapeutic targets in mitochondria-linked pathologies like cancer, ischemia, reperfusion injury, and neurological disorders.
    Keywords mitochondria ; ion channel ; cell death ; cell signaling ; apoptosis ; Biology (General) ; QH301-705.5
    Language English
    Publishing date 2021-01-01T00:00:00Z
    Publisher Frontiers Media S.A.
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  4. Article ; Online: Vitamin B12 deficiency-induced pseudothrombotic microangiopathy without macrocytosis presenting with acute renal failure

    Jennifer Vanoli / Andrea Carrer / Roberto Martorana / Guido Grassi / Michele Bombelli

    Journal of Medical Case Reports, Vol 12, Iss 1, Pp 1-

    a case report

    2018  Volume 5

    Abstract: Abstract Background Vitamin B12 deficiency-induced thrombotic microangiopathy, known as pseudothrombotic microangiopathy, is a rare condition which resembles the clinical features of thrombotic thrombocytopenic purpura but requires a markedly different ... ...

    Abstract Abstract Background Vitamin B12 deficiency-induced thrombotic microangiopathy, known as pseudothrombotic microangiopathy, is a rare condition which resembles the clinical features of thrombotic thrombocytopenic purpura but requires a markedly different treatment. Most cases of vitamin B12 deficiency have only mild hematological findings, but in approximately 10% of patients life-threatening conditions have been reported. Case presentation We report a case of a 46-year-old Moroccan man presenting with severe hemolytic anemia, thrombocytopenia, and renal failure in absence of macrocytosis, thus mimicking a genuine thrombotic thrombocytopenic purpura. Rapid improvement of renal function observed with only hydration and transfusions of packed red blood cells and the presence of pancytopenia suggested a bone marrow deficiency associated to a hemolytic component of unclear origin. Detection of low levels of vitamin B12 and rapid restitutio ad integrum with its replacement supported the diagnosis of pseudothrombotic thrombocytopenic purpura caused by vitamin B12 deficiency. Conclusions Diagnosis of pseudothrombotic thrombocytopenic purpura caused by vitamin B12 deficiency might be difficult. Awareness of clinicians toward this differential diagnosis might spare patients from unnecessary therapeutic plasma exchange that is burdened by morbidity and mortality.
    Keywords Pseudothrombotic thrombocytopenic purpura ; Vitamin B12 deficiency ; Hemolytic anemia ; Thrombocytopenia ; Medicine ; R
    Subject code 610
    Language English
    Publishing date 2018-10-01T00:00:00Z
    Publisher BMC
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  5. Article ; Online: Defining the molecular mechanisms of the mitochondrial permeability transition through genetic manipulation of F-ATP synthase

    Andrea Carrer / Ludovica Tommasin / Justina Šileikytė / Francesco Ciscato / Riccardo Filadi / Andrea Urbani / Michael Forte / Andrea Rasola / Ildikò Szabò / Michela Carraro / Paolo Bernardi

    Nature Communications, Vol 12, Iss 1, Pp 1-

    2021  Volume 12

    Abstract: The nature of the mitochondrial permeability transition pore (PTP) is still under debate. Here, through genetically modified F-ATP synthase, the authors show that PTP formation can be mediated by F-ATP synthase or by adenine nucleotide translocator, ... ...

    Abstract The nature of the mitochondrial permeability transition pore (PTP) is still under debate. Here, through genetically modified F-ATP synthase, the authors show that PTP formation can be mediated by F-ATP synthase or by adenine nucleotide translocator, suggesting the existence of distinct but related permeability pathways.
    Keywords Science ; Q
    Language English
    Publishing date 2021-08-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  6. Article ; Online: Corrigendum to “Insight into the mechanism of cytotoxicity of membrane-permeant psoralenic Kv1.3 channel inhibitors by chemical dissection of a novel member of the family” [Redox Biol. 37 (2020 Sep 6) 101705–101721]

    Roberta Peruzzo / Andrea Mattarei / Michele Azzolini / Katrin Anne Becker-Flegler / Matteo Romio / Giovanni Rigoni / Andrea Carrer / Lucia Biasutto / Sofia Parrasia / Stephanie Kadow / Antonella Managò / Andrea Urbani / Andrea Rossa / Gianpietro Semenzato / Maria Eugenia Soriano / Livio Trentin / Syed Ahmad / Michael Edwards / Erich Gulbins /
    Cristina Paradisi / Mario Zoratti / Luigi Leanza / Ildikò Szabò

    Redox Biology, Vol 45, Iss , Pp 102036- (2021)

    2021  

    Keywords Medicine (General) ; R5-920 ; Biology (General) ; QH301-705.5
    Language English
    Publishing date 2021-09-01T00:00:00Z
    Publisher Elsevier
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  7. Article ; Online: Purified F-ATP synthase forms a Ca2+-dependent high-conductance channel matching the mitochondrial permeability transition pore

    Andrea Urbani / Valentina Giorgio / Andrea Carrer / Cinzia Franchin / Giorgio Arrigoni / Chimari Jiko / Kazuhiro Abe / Shintaro Maeda / Kyoko Shinzawa-Itoh / Janna F. M. Bogers / Duncan G. G. McMillan / Christoph Gerle / Ildikò Szabò / Paolo Bernardi

    Nature Communications, Vol 10, Iss 1, Pp 1-

    2019  Volume 11

    Abstract: The molecular identity of the mitochondrial megachannel (MMC)/permeability transition pore (PTP), a key effector of cell death, remains controversial. Here authors demonstrate that the membrane embedded bovine F-ATP synthase elicits Ca2 + -dependent ... ...

    Abstract The molecular identity of the mitochondrial megachannel (MMC)/permeability transition pore (PTP), a key effector of cell death, remains controversial. Here authors demonstrate that the membrane embedded bovine F-ATP synthase elicits Ca2 + -dependent currents matching those of the MMC/PTP.
    Keywords Science ; Q
    Language English
    Publishing date 2019-09-01T00:00:00Z
    Publisher Nature Publishing Group
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  8. Article ; Online: Purified F-ATP synthase forms a Ca2+-dependent high-conductance channel matching the mitochondrial permeability transition pore

    Andrea Urbani / Valentina Giorgio / Andrea Carrer / Cinzia Franchin / Giorgio Arrigoni / Chimari Jiko / Kazuhiro Abe / Shintaro Maeda / Kyoko Shinzawa-Itoh / Janna F. M. Bogers / Duncan G. G. McMillan / Christoph Gerle / Ildikò Szabò / Paolo Bernardi

    Nature Communications, Vol 10, Iss 1, Pp 1-

    2019  Volume 11

    Abstract: The molecular identity of the mitochondrial megachannel (MMC)/permeability transition pore (PTP), a key effector of cell death, remains controversial. Here authors demonstrate that the membrane embedded bovine F-ATP synthase elicits Ca2 + -dependent ... ...

    Abstract The molecular identity of the mitochondrial megachannel (MMC)/permeability transition pore (PTP), a key effector of cell death, remains controversial. Here authors demonstrate that the membrane embedded bovine F-ATP synthase elicits Ca2 + -dependent currents matching those of the MMC/PTP.
    Keywords Science ; Q
    Language English
    Publishing date 2019-09-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  9. Article ; Online: Insight into the mechanism of cytotoxicity of membrane-permeant psoralenic Kv1.3 channel inhibitors by chemical dissection of a novel member of the family

    Roberta Peruzzo / Andrea Mattarei / Michele Azzolini / Katrin Anne Becker-Flegler / Matteo Romio / Giovanni Rigoni / Andrea Carrer / Lucia Biasutto / Sofia Parrasia / Stephanie Kadow / Antonella Managò / Andrea Urbani / Andrea Rossa / Gianpietro Semenzato / Maria Eugenia Soriano / Livio Trentin / Syed Ahmad / Michael Edwards / Erich Gulbins /
    Cristina Paradisi / Mario Zoratti / Luigi Leanza / Ildikò Szabò

    Redox Biology, Vol 37, Iss , Pp 101705- (2020)

    2020  

    Abstract: The potassium channel Kv1.3, involved in several important pathologies, is the target of a family of psoralen-based drugs whose mechanism of action is not fully understood. Here we provide evidence for a physical interaction of the mitochondria-located ... ...

    Abstract The potassium channel Kv1.3, involved in several important pathologies, is the target of a family of psoralen-based drugs whose mechanism of action is not fully understood. Here we provide evidence for a physical interaction of the mitochondria-located Kv1.3 (mtKv1.3) and Complex I of the respiratory chain and show that this proximity underlies the death-inducing ability of psoralenic Kv1.3 inhibitors. The effects of PAP-1-MHEG (PAP-1, a Kv1.3 inhibitor, with six monomeric ethylene glycol units attached to the phenyl ring of PAP-1), a more soluble novel derivative of PAP-1 and of its various portions on mitochondrial physiology indicate that the psoralenic moiety of PAP-1 bound to mtKv1.3 facilitates the diversion of electrons from Complex I to molecular oxygen. The resulting massive production of toxic Reactive Oxygen Species leads to death of cancer cells expressing Kv1.3. In vivo, PAP-1-MHEG significantly decreased melanoma volume. In summary, PAP-1-MHEG offers insights into the mechanisms of cytotoxicity of this family of compounds and may represent a valuable clinical tool.
    Keywords Kv1.3 potassium channel ; Psoralenic compounds ; Mitochondria ; Complex I ; Reactive oxygen species ; Melanoma ; Medicine (General) ; R5-920 ; Biology (General) ; QH301-705.5
    Language English
    Publishing date 2020-10-01T00:00:00Z
    Publisher Elsevier
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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