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Article ; Online: Cellular senescence at the crossroads of inflammation and Alzheimer's disease.

Guerrero, Ana / De Strooper, Bart / Arancibia-Cárcamo, I Lorena

2021 Volume 44, Issue 9, Page(s) 714–727

Abstract: Aging is a key risk factor for Alzheimer's disease (AD), but the reasons for this association are not well understood. Senescent cells accumulate in aged tissues and have been shown to play causal roles in age-related pathologies through their ... ...

Abstract	Aging is a key risk factor for Alzheimer's disease (AD), but the reasons for this association are not well understood. Senescent cells accumulate in aged tissues and have been shown to play causal roles in age-related pathologies through their proinflammatory secretome. The question arises whether senescence-induced inflammation might contribute to AD and bridge the gap between aging and AD. Here, we highlight the role of cellular senescence as a driver of the aging phenotype, and discuss the current evidence that connects senescence with AD and neurodegeneration.
MeSH term(s)	Aged ; Aging ; Alzheimer Disease ; Cellular Senescence ; Humans ; Inflammation ; Phenotype
Language	English
Publishing date	2021-08-05
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	282488-7
ISSN	1878-108X ; 0378-5912 ; 0166-2236
ISSN (online)	1878-108X
ISSN	0378-5912 ; 0166-2236
DOI	10.1016/j.tins.2021.06.007
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Article ; Online: Astrocyte Ca

Lezmy, Jonathan / Arancibia-Cárcamo, I Lorena / Quintela-López, Tania / Sherman, Diane L / Brophy, Peter J / Attwell, David

Science (New York, N.Y.)

2021 Volume 374, Issue 6565, Page(s) eabh2858

Abstract: In the brain’s gray matter, astrocytes regulate synapse properties, but their role is unclear for the white matter, where myelinated axons rapidly transmit information between gray matter areas. We found that in rodents, neuronal activity raised the ... ...

Abstract	In the brain’s gray matter, astrocytes regulate synapse properties, but their role is unclear for the white matter, where myelinated axons rapidly transmit information between gray matter areas. We found that in rodents, neuronal activity raised the intracellular calcium concentration ([Ca
MeSH term(s)	Action Potentials ; Adenosine Triphosphate/metabolism ; Animals ; Astrocytes/physiology ; Axons/physiology ; Calcium/physiology ; Cortical Excitability ; Mice ; Mice, Transgenic ; Neural Conduction ; Patch-Clamp Techniques ; Rats, Sprague-Dawley ; Rats
Chemical Substances	Adenosine Triphosphate (8L70Q75FXE) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2021-10-15
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	128410-1
ISSN	1095-9203 ; 0036-8075
ISSN (online)	1095-9203
ISSN	0036-8075
DOI	10.1126/science.abh2858
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Zs.A 27: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Node of Ranvier length as a potential regulator of myelinated axon conduction speed.

Arancibia-Cárcamo, I Lorena / Ford, Marc C / Cossell, Lee / Ishida, Kinji / Tohyama, Koujiro / Attwell, David

eLife

2017 Volume 6

Abstract: Myelination speeds conduction of the nerve impulse, enhancing cognitive power. Changes of white matter structure contribute to learning, and are often assumed to reflect an altered number of myelin wraps. We now show that, in rat optic nerve and cerebral ...

Abstract	Myelination speeds conduction of the nerve impulse, enhancing cognitive power. Changes of white matter structure contribute to learning, and are often assumed to reflect an altered number of myelin wraps. We now show that, in rat optic nerve and cerebral cortical axons, the node of Ranvier length varies over a 4.4-fold and 8.7-fold range respectively and that variation of the node length is much less along axons than between axons. Modelling predicts that these node length differences will alter conduction speed by ~20%, similar to the changes produced by altering the number of myelin wraps or the internode length. For a given change of conduction speed, the membrane area change needed at the node is >270-fold less than that needed in the myelin sheath. Thus, axon-specific adjustment of node of Ranvier length is potentially an energy-efficient and rapid mechanism for tuning the arrival time of information in the CNS.
MeSH term(s)	Animals ; Axons/physiology ; Biostatistics ; Cerebral Cortex/cytology ; Cerebral Cortex/physiology ; Models, Biological ; Neural Conduction ; Optic Nerve/cytology ; Optic Nerve/physiology ; Ranvier's Nodes/physiology ; Rats
Language	English
Publishing date	2017--28
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2687154-3
ISSN	2050-084X ; 2050-084X
ISSN (online)	2050-084X
ISSN	2050-084X
DOI	10.7554/eLife.23329
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Article ; Online: Effects of the ecto-ATPase apyrase on microglial ramification and surveillance reflect cell depolarization, not ATP depletion.

Madry, Christian / Arancibia-Cárcamo, I Lorena / Kyrargyri, Vasiliki / Chan, Victor T T / Hamilton, Nicola B / Attwell, David

Proceedings of the National Academy of Sciences of the United States of America

2018 Volume 115, Issue 7, Page(s) E1608–E1617

Abstract: Microglia, the brain's innate immune cells, have highly motile processes which constantly survey the brain to detect infection, remove dying cells, and prune synapses during brain development. ATP released by tissue damage is known to attract microglial ... ...

Abstract	Microglia, the brain's innate immune cells, have highly motile processes which constantly survey the brain to detect infection, remove dying cells, and prune synapses during brain development. ATP released by tissue damage is known to attract microglial processes, but it is controversial whether an ambient level of ATP is needed to promote constant microglial surveillance in the normal brain. Applying the ATPase apyrase, an enzyme which hydrolyzes ATP and ADP, reduces microglial process ramification and surveillance, suggesting that ambient ATP/ADP maintains microglial surveillance. However, attempting to raise the level of ATP/ADP by blocking the endogenous ecto-ATPase (termed NTPDase1/CD39), which also hydrolyzes ATP/ADP, does not affect the cells' ramification or surveillance, nor their membrane currents, which respond to even small rises of extracellular [ATP] or [ADP] with the activation of K
MeSH term(s)	Adenosine Diphosphate/metabolism ; Adenosine Triphosphatases/metabolism ; Adenosine Triphosphate/metabolism ; Animals ; Apyrase/metabolism ; Brain/enzymology ; Brain/physiology ; Female ; Male ; Microglia/chemistry ; Microglia/enzymology ; Microglia/physiology ; Potassium/metabolism ; Rats ; Rats, Sprague-Dawley
Chemical Substances	Adenosine Diphosphate (61D2G4IYVH) ; Adenosine Triphosphate (8L70Q75FXE) ; Adenosine Triphosphatases (EC 3.6.1.-) ; ectoATPase (EC 3.6.1.-) ; Apyrase (EC 3.6.1.5) ; Potassium (RWP5GA015D)
Language	English
Publishing date	2018-01-30
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.1715354115
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Article ; Online: The node of Ranvier in CNS pathology.

Arancibia-Carcamo, I Lorena / Attwell, David

Acta neuropathologica

2014 Volume 128, Issue 2, Page(s) 161–175

Abstract: Healthy nodes of Ranvier are crucial for action potential propagation along myelinated axons, both in the central and in the peripheral nervous system. Surprisingly, the node of Ranvier has often been neglected when describing CNS disorders, with most ... ...

Abstract	Healthy nodes of Ranvier are crucial for action potential propagation along myelinated axons, both in the central and in the peripheral nervous system. Surprisingly, the node of Ranvier has often been neglected when describing CNS disorders, with most pathologies classified simply as being due to neuronal defects in the grey matter or due to oligodendrocyte damage in the white matter. However, recent studies have highlighted changes that occur in pathological conditions at the node of Ranvier, and at the associated paranodal and juxtaparanodal regions where neurons and myelinating glial cells interact. Lengthening of the node of Ranvier, failure of the electrically resistive seal between the myelin and the axon at the paranode, and retraction of myelin to expose voltage-gated K(+) channels in the juxtaparanode, may contribute to altering the function of myelinated axons in a wide range of diseases, including stroke, spinal cord injury and multiple sclerosis. Here, we review the principles by which the node of Ranvier operates and its molecular structure, and thus explain how defects at the node and paranode contribute to neurological disorders.
MeSH term(s)	Animals ; Brain/pathology ; Brain/physiopathology ; Humans ; Myelin Sheath/pathology ; Myelin Sheath/physiology ; Ranvier's Nodes/pathology ; Ranvier's Nodes/physiology ; Spinal Cord/pathology ; Spinal Cord/physiopathology
Language	English
Publishing date	2014-06-10
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1079-0
ISSN	1432-0533 ; 0001-6322
ISSN (online)	1432-0533
ISSN	0001-6322
DOI	10.1007/s00401-014-1305-z
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Article ; Online: Microglial Ramification, Surveillance, and Interleukin-1β Release Are Regulated by the Two-Pore Domain K

Madry, Christian / Kyrargyri, Vasiliki / Arancibia-Cárcamo, I Lorena / Jolivet, Renaud / Kohsaka, Shinichi / Bryan, Robert M / Attwell, David

Neuron

2017 Volume 97, Issue 2, Page(s) 299–312.e6

Abstract: Microglia exhibit two modes of motility: they constantly extend and retract their processes to survey the brain, but they also send out targeted processes to envelop sites of tissue damage. We now show that these motility modes differ mechanistically. We ...

Abstract	Microglia exhibit two modes of motility: they constantly extend and retract their processes to survey the brain, but they also send out targeted processes to envelop sites of tissue damage. We now show that these motility modes differ mechanistically. We identify the two-pore domain channel THIK-1 as the main K
MeSH term(s)	Adenosine Triphosphate/pharmacology ; Animals ; Cell Movement ; Cell Polarity ; Cell Shape ; Cell Surface Extensions/physiology ; Chemotaxis/physiology ; Inflammasomes/metabolism ; Interleukin-1beta/physiology ; Membrane Potentials ; Mice ; Mice, Knockout ; Microglia/drug effects ; Microglia/physiology ; Potassium/physiology ; Potassium Channels, Tandem Pore Domain/antagonists & inhibitors ; Potassium Channels, Tandem Pore Domain/deficiency ; Potassium Channels, Tandem Pore Domain/physiology ; Rats ; Rats, Sprague-Dawley ; Receptors, Purinergic P2Y12/physiology ; Transcriptome
Chemical Substances	Inflammasomes ; Interleukin-1beta ; Kcnk13 protein, mouse ; Kcnk13 protein, rat ; P2ry12 protein, mouse ; Potassium Channels, Tandem Pore Domain ; Receptors, Purinergic P2Y12 ; Adenosine Triphosphate (8L70Q75FXE) ; Potassium (RWP5GA015D)
Language	English
Publishing date	2017-12-28
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	808167-0
ISSN	1097-4199 ; 0896-6273
ISSN (online)	1097-4199
ISSN	0896-6273
DOI	10.1016/j.neuron.2017.12.002
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Zs.A 2496: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MG 92: Show issues

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Article ; Online: Miro1-dependent mitochondrial dynamics in parvalbumin interneurons.

Kontou, Georgina / Antonoudiou, Pantelis / Podpolny, Marina / Szulc, Blanka R / Arancibia-Carcamo, I Lorena / Higgs, Nathalie F / Lopez-Domenech, Guillermo / Salinas, Patricia C / Mann, Edward O / Kittler, Josef T

eLife

2021 Volume 10

Abstract: The spatiotemporal distribution of mitochondria is crucial for precise ATP provision and calcium buffering required to support neuronal signaling. Fast-spiking GABAergic interneurons expressing parvalbumin (PV+) have a high mitochondrial content ... ...

Abstract	The spatiotemporal distribution of mitochondria is crucial for precise ATP provision and calcium buffering required to support neuronal signaling. Fast-spiking GABAergic interneurons expressing parvalbumin (PV+) have a high mitochondrial content reflecting their large energy utilization. The importance for correct trafficking and precise mitochondrial positioning remains poorly elucidated in inhibitory neurons. Miro1 is a Ca²
MeSH term(s)	Animals ; Animals, Newborn ; Behavior, Animal ; Female ; Genotype ; Hippocampus ; Interneurons/physiology ; Male ; Mice ; Mice, Knockout ; Mice, Transgenic ; Mitochondria/physiology ; Parvalbumins/genetics ; Parvalbumins/metabolism ; rho GTP-Binding Proteins/genetics ; rho GTP-Binding Proteins/metabolism
Chemical Substances	Miro-1 protein, mouse ; Parvalbumins ; rho GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2021-06-30
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2687154-3
ISSN	2050-084X ; 2050-084X
ISSN (online)	2050-084X
ISSN	2050-084X
DOI	10.7554/eLife.65215
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Article ; Online: Miro clusters regulate ER-mitochondria contact sites and link cristae organization to the mitochondrial transport machinery.

Modi, Souvik / López-Doménech, Guillermo / Halff, Elise F / Covill-Cooke, Christian / Ivankovic, Davor / Melandri, Daniela / Arancibia-Cárcamo, I Lorena / Burden, Jemima J / Lowe, Alan R / Kittler, Josef T

Nature communications

2019 Volume 10, Issue 1, Page(s) 4399

Abstract: Mitochondrial Rho (Miro) GTPases localize to the outer mitochondrial membrane and are essential machinery for the regulated trafficking of mitochondria to defined subcellular locations. However, their sub-mitochondrial localization and relationship with ... ...

Abstract	Mitochondrial Rho (Miro) GTPases localize to the outer mitochondrial membrane and are essential machinery for the regulated trafficking of mitochondria to defined subcellular locations. However, their sub-mitochondrial localization and relationship with other critical mitochondrial complexes remains poorly understood. Here, using super-resolution fluorescence microscopy, we report that Miro proteins form nanometer-sized clusters along the mitochondrial outer membrane in association with the Mitochondrial Contact Site and Cristae Organizing System (MICOS). Using knockout mouse embryonic fibroblasts we show that Miro1 and Miro2 are required for normal mitochondrial cristae architecture and Endoplasmic Reticulum-Mitochondria Contacts Sites (ERMCS). Further, we show that Miro couples MICOS to TRAK motor protein adaptors to ensure the concerted transport of the two mitochondrial membranes and the correct distribution of cristae on the mitochondrial membrane. The Miro nanoscale organization, association with MICOS complex and regulation of ERMCS reveal new levels of control of the Miro GTPases on mitochondrial functionality.
MeSH term(s)	Animals ; Binding Sites ; Biological Transport ; Cells, Cultured ; Embryo, Mammalian/cytology ; Endoplasmic Reticulum/metabolism ; Endoplasmic Reticulum/ultrastructure ; Fibroblasts/cytology ; Fibroblasts/metabolism ; HeLa Cells ; Humans ; Mice, Knockout ; Microscopy, Confocal ; Microscopy, Electron, Transmission ; Mitochondria/metabolism ; Mitochondria/ultrastructure ; Mitochondrial Membranes/metabolism ; Mitochondrial Membranes/ultrastructure ; Mitochondrial Proteins/genetics ; Mitochondrial Proteins/metabolism ; Protein Binding ; Rats ; rho GTP-Binding Proteins/genetics ; rho GTP-Binding Proteins/metabolism
Chemical Substances	Miro-1 protein, mouse ; Mitochondrial Proteins ; Rhot2 protein, mouse (EC 3.6.1.-) ; rho GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2019-09-27
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-019-12382-4
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Article ; Online: Regulation of GABA(A) receptor membrane trafficking and synaptic localization.

Arancibia-Cárcamo, I Lorena / Kittler, Josef T

Pharmacology & therapeutics

2009 Volume 123, Issue 1, Page(s) 17–31

Abstract: Synaptic inhibition plays a key role in regulating neuronal excitability and information processing in the brain. The strength of synaptic inhibition is therefore an important determinant of both cellular and network activity levels in the central ... ...

Abstract	Synaptic inhibition plays a key role in regulating neuronal excitability and information processing in the brain. The strength of synaptic inhibition is therefore an important determinant of both cellular and network activity levels in the central nervous system (CNS). gamma-aminobutyric acid type A (GABA(A)) receptors are the major sites for fast inhibitory neurotransmission in the CNS and alterations in their trafficking, synaptic accumulation and function play a key role in regulating neuronal excitability. Synaptic receptor number is determined by the trafficking of GABA(A) receptors to and away from inhibitory synapses and by their stability and localization at the inhibitory postsynaptic domain. Here we discuss advances that have led to an improved understanding of the mechanisms that regulate the delivery and stabilization of GABA(A) receptors at inhibitory synapses and address the role of GABA(A) receptor trafficking, GABA(A) receptor associated proteins and post-translational modifications in regulating this process.
MeSH term(s)	Animals ; Brain/metabolism ; Cell Membrane/metabolism ; Humans ; Models, Molecular ; Protein Processing, Post-Translational ; Protein Transport ; Receptors, GABA-A/chemistry ; Receptors, GABA-A/metabolism ; Receptors, GABA-A/physiology ; Synaptic Transmission/physiology
Chemical Substances	Receptors, GABA-A
Language	English
Publishing date	2009-04-15
Publishing country	England
Document type	Journal Article
ZDB-ID	194735-7
ISSN	1879-016X ; 0163-7258
ISSN (online)	1879-016X
ISSN	0163-7258
DOI	10.1016/j.pharmthera.2009.03.012
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Article ; Online: Loss of Dendritic Complexity Precedes Neurodegeneration in a Mouse Model with Disrupted Mitochondrial Distribution in Mature Dendrites.

López-Doménech, Guillermo / Higgs, Nathalie F / Vaccaro, Victoria / Roš, Hana / Arancibia-Cárcamo, I Lorena / MacAskill, Andrew F / Kittler, Josef T

Cell reports

2016 Volume 17, Issue 2, Page(s) 317–327

Abstract: Correct mitochondrial distribution is critical for satisfying local energy demands and calcium buffering requirements and supporting key cellular processes. The mitochondrially targeted proteins Miro1 and Miro2 are important components of the ... ...

Abstract	Correct mitochondrial distribution is critical for satisfying local energy demands and calcium buffering requirements and supporting key cellular processes. The mitochondrially targeted proteins Miro1 and Miro2 are important components of the mitochondrial transport machinery, but their specific roles in neuronal development, maintenance, and survival remain poorly understood. Using mouse knockout strategies, we demonstrate that Miro1, as opposed to Miro2, is the primary regulator of mitochondrial transport in both axons and dendrites. Miro1 deletion leads to depletion of mitochondria from distal dendrites but not axons, accompanied by a marked reduction in dendritic complexity. Disrupting postnatal mitochondrial distribution in vivo by deleting Miro1 in mature neurons causes a progressive loss of distal dendrites and compromises neuronal survival. Thus, the local availability of mitochondrial mass is critical for generating and sustaining dendritic arbors, and disruption of mitochondrial distribution in mature neurons is associated with neurodegeneration.
MeSH term(s)	Animals ; Axons/metabolism ; Axons/pathology ; Dendrites/genetics ; Dendrites/metabolism ; Disease Models, Animal ; Humans ; Mice ; Mice, Knockout ; Mitochondria/genetics ; Mitochondria/metabolism ; Mitochondrial Proteins/genetics ; Nerve Degeneration/genetics ; Nerve Degeneration/metabolism ; Nerve Degeneration/pathology ; Neurogenesis/genetics ; Neurons/metabolism ; Neurons/pathology ; rho GTP-Binding Proteins/genetics
Chemical Substances	Miro-1 protein, mouse ; Mitochondrial Proteins ; Rhot2 protein, mouse (EC 3.6.1.-) ; rho GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2016-10-04
Publishing country	United States
Document type	Journal Article
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2016.09.004
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