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Article ; Online: Knockout of the P2Y

Milde, Stefan / Brown, Guy C

International journal of molecular sciences

2022 Volume 23, Issue 4

Abstract: After stroke, there is a delayed neuronal loss in brain areas surrounding the infarct, which may in part be mediated by microglial phagocytosis of stressed neurons. Microglial phagocytosis of stressed or damaged neurons can be mediated by UDP released ... ...

Abstract	After stroke, there is a delayed neuronal loss in brain areas surrounding the infarct, which may in part be mediated by microglial phagocytosis of stressed neurons. Microglial phagocytosis of stressed or damaged neurons can be mediated by UDP released from stressed neurons activating the P2Y
MeSH term(s)	Animals ; Brain/metabolism ; Brain/pathology ; Brain Infarction/metabolism ; Brain Infarction/pathology ; Brain Ischemia/metabolism ; Brain Ischemia/pathology ; Cells, Cultured ; Female ; Male ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Microglia/metabolism ; Microglia/pathology ; Neurons/metabolism ; Neurons/pathology ; Phagocytosis/physiology ; Receptors, Purinergic P2/metabolism ; Stroke/metabolism ; Stroke/pathology
Chemical Substances	Receptors, Purinergic P2 ; purinoceptor P2Y6
Language	English
Publishing date	2022-02-19
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/ijms23042304
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Article ; Online: Imaging Axonal Transport in Ex Vivo Central and Peripheral Nerves.

Gould, Stacey Anne / Adalbert, Robert / Milde, Stefan / Coleman, Michael

Methods in molecular biology (Clifton, N.J.)

2022 Volume 2431, Page(s) 73–93

Abstract: Neurones are highly polarized cells with extensive axonal projections that rely on transport of proteins, RNAs, and organelles in a bidirectional manner to remain healthy. This process, known as axonal transport, can be imaged in real time through ... ...

Abstract	Neurones are highly polarized cells with extensive axonal projections that rely on transport of proteins, RNAs, and organelles in a bidirectional manner to remain healthy. This process, known as axonal transport, can be imaged in real time through epifluorescent imaging of fluorescently labeled proteins, organelles, and other cargoes. While this is most conveniently done in primary neuronal cultures, it is more physiologically relevant when carried out in the context of a developed nerve containing both axons and glia. Here we outline how to image axonal transport ex vivo in sciatic and optic nerves, and the fimbria of the fornix. These methods could be altered to image other fluorescently labeled molecules, as well as different mechanisms of intracellular transport.
MeSH term(s)	Axonal Transport/physiology ; Axons/metabolism ; Neurons ; Optic Nerve/physiology ; Peripheral Nerves/metabolism ; Sciatic Nerve
Language	English
Publishing date	2022-04-12
Publishing country	United States
Document type	Journal Article
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-0716-1990-2_4
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Article ; Online: Identification of palmitoyltransferase and thioesterase enzymes that control the subcellular localization of axon survival factor nicotinamide mononucleotide adenylyltransferase 2 (NMNAT2).

Milde, Stefan / Coleman, Michael P

The Journal of biological chemistry

2014 Volume 289, Issue 47, Page(s) 32858–32870

Abstract: The NAD-synthesizing enzyme nicotinamide mononucleotide adenylyltransferase 2 (NMNAT2) is a critical survival factor for axons and its constant supply from neuronal cell bodies into axons is required for axon survival in primary culture neurites and axon ...

Abstract	The NAD-synthesizing enzyme nicotinamide mononucleotide adenylyltransferase 2 (NMNAT2) is a critical survival factor for axons and its constant supply from neuronal cell bodies into axons is required for axon survival in primary culture neurites and axon extension in vivo. Recently, we showed that palmitoylation is necessary to target NMNAT2 to post-Golgi vesicles, thereby influencing its protein turnover and axon protective capacity. Here we find that NMNAT2 is a substrate for cytosolic thioesterases APT1 and APT2 and that palmitoylation/depalmitoylation dynamics are on a time scale similar to its short half-life. Interestingly, however, depalmitoylation does not release NMNAT2 from membranes. The mechanism of palmitoylation-independent membrane attachment appears to be mediated by the same minimal domain required for palmitoylation itself. Furthermore, we identify several zDHHC palmitoyltransferases that influence NMNAT2 palmitoylation and subcellular localization, among which a role for zDHHC17 (HIP14) in neuronal NMNAT2 palmitoylation is best supported by our data. These findings shed light on the enzymatic regulation of NMNAT2 palmitoylation and highlight individual thioesterases and palmitoyltransferases as potential targets to modulate NMNAT2-dependent axon survival.
MeSH term(s)	Acyltransferases/genetics ; Acyltransferases/metabolism ; Animals ; Axons/metabolism ; Blotting, Western ; Cell Membrane/metabolism ; Cells, Cultured ; HEK293 Cells ; Humans ; Lipoylation/drug effects ; Mice, Inbred C57BL ; Mutation ; Neurons/cytology ; Neurons/drug effects ; Neurons/metabolism ; Nicotinamide-Nucleotide Adenylyltransferase/genetics ; Nicotinamide-Nucleotide Adenylyltransferase/metabolism ; Palmitic Acid/metabolism ; Propiolactone/analogs & derivatives ; Propiolactone/pharmacology ; RNA Interference ; Reverse Transcriptase Polymerase Chain Reaction ; Substrate Specificity ; Thiolester Hydrolases/genetics ; Thiolester Hydrolases/metabolism
Chemical Substances	palmostatin B ; Palmitic Acid (2V16EO95H1) ; Propiolactone (6RC3ZT4HB0) ; Acyltransferases (EC 2.3.-) ; Nicotinamide-Nucleotide Adenylyltransferase (EC 2.7.7.1) ; Nmnat2 protein, mouse (EC 2.7.7.1) ; Lypla1 protein, mouse (EC 3.1.2.-) ; Lypla2 protein, mouse (EC 3.1.2.-) ; Thiolester Hydrolases (EC 3.1.2.-) ; Zdhhc17 protein, mouse (EC 3.2.1.-)
Language	English
Publishing date	2014-09-30
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M114.582338
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Article ; Online: Inflammatory neuronal loss in the substantia nigra induced by systemic lipopolysaccharide is prevented by knockout of the P2Y

Milde, Stefan / van Tartwijk, Francesca W / Vilalta, Anna / Hornik, Tamara C / Dundee, Jacob M / Puigdellívol, Mar / Brown, Guy C

Journal of neuroinflammation

2021 Volume 18, Issue 1, Page(s) 225

Abstract: Inflammation may contribute to multiple brain pathologies. One cause of inflammation is lipopolysaccharide/endotoxin (LPS), the levels of which are elevated in blood and/or brain during bacterial infections, gut dysfunction and neurodegenerative diseases, ...

Abstract	Inflammation may contribute to multiple brain pathologies. One cause of inflammation is lipopolysaccharide/endotoxin (LPS), the levels of which are elevated in blood and/or brain during bacterial infections, gut dysfunction and neurodegenerative diseases, such as Parkinson's disease. How inflammation causes neuronal loss is unclear, but one potential mechanism is microglial phagocytosis of neurons, which is dependent on the microglial P2Y
MeSH term(s)	Animals ; Cell Line, Transformed ; Cells, Cultured ; Dopaminergic Neurons/drug effects ; Dopaminergic Neurons/metabolism ; Dopaminergic Neurons/pathology ; Inflammation/chemically induced ; Inflammation/metabolism ; Inflammation/pathology ; Lipopolysaccharides/toxicity ; Male ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Neurons/drug effects ; Neurons/metabolism ; Neurons/pathology ; Organ Culture Techniques ; PC12 Cells ; Rats ; Receptors, Purinergic P2/deficiency ; Substantia Nigra/drug effects ; Substantia Nigra/metabolism ; Substantia Nigra/pathology
Chemical Substances	Lipopolysaccharides ; Receptors, Purinergic P2 ; purinoceptor P2Y6
Language	English
Publishing date	2021-10-11
Publishing country	England
Document type	Journal Article
ZDB-ID	2156455-3
ISSN	1742-2094 ; 1742-2094
ISSN (online)	1742-2094
ISSN	1742-2094
DOI	10.1186/s12974-021-02280-2
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Article ; Online: Multiparameter phenotypic screening for endogenous TFEB and TFE3 translocation identifies novel chemical series modulating lysosome function.

Carling, Phillippa J / Ryan, Brent J / McGuinness, William / Kataria, Shikha / Humble, Stewart W / Milde, Stefan / Duce, James A / Kapadia, Nirav / Zuercher, William J / Davis, John B / Di Daniel, Elena / Wade-Martins, Richard

Autophagy

2022 Volume 19, Issue 2, Page(s) 692–705

Abstract: The accumulation of toxic protein aggregates in multiple neurodegenerative diseases is associated with defects in the macroautophagy/autophagy-lysosome pathway. The amelioration of disease phenotypes across multiple models of neurodegeneration can be ... ...

Abstract	The accumulation of toxic protein aggregates in multiple neurodegenerative diseases is associated with defects in the macroautophagy/autophagy-lysosome pathway. The amelioration of disease phenotypes across multiple models of neurodegeneration can be achieved through modulating the master regulator of lysosome function, TFEB (transcription factor EB). Using a novel multi-parameter high-throughput screen for cytoplasmic:nuclear translocation of endogenous TFEB and the related transcription factor TFE3, we screened the Published Kinase Inhibitor Set 2 (PKIS2) library as proof of principle and to identify kinase regulators of TFEB and TFE3. Given that TFEB and TFE3 are responsive to cellular stress we have established assays for cellular toxicity and lysosomal function, critical to ensuring the identification of hit compounds with only positive effects on lysosome activity. In addition to AKT inhibitors which regulate TFEB localization, we identified a series of quinazoline-derivative compounds that induced TFEB and TFE3 translocation. A novel series of structurally-related analogs was developed, and several compounds induced TFEB and TFE3 translocation at higher potency than previously screened compounds. KINOME
MeSH term(s)	Autophagy/genetics ; Basic Helix-Loop-Helix Leucine Zipper Transcription Factors/metabolism ; Gene Expression Regulation ; Cell Nucleus/metabolism ; Lysosomes/metabolism
Chemical Substances	Basic Helix-Loop-Helix Leucine Zipper Transcription Factors
Language	English
Publishing date	2022-07-25
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2454135-7
ISSN	1554-8635 ; 1554-8627
ISSN (online)	1554-8635
ISSN	1554-8627
DOI	10.1080/15548627.2022.2095834
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Article ; Online: The microglial P2Y

Puigdellívol, Mar / Milde, Stefan / Vilalta, Anna / Cockram, Tom O J / Allendorf, David H / Lee, Jeffrey Y / Dundee, Jacob M / Pampuščenko, Katryna / Borutaite, Vilmante / Nuthall, Hugh N / Brelstaff, Jack H / Spillantini, Maria Grazia / Brown, Guy C

Cell reports

2021 Volume 37, Issue 13, Page(s) 110148

Abstract: Microglia are implicated in neurodegeneration, potentially by phagocytosing neurons, but it is unclear how to block the detrimental effects of microglia while preserving their beneficial roles. The microglial ... ...

Abstract	Microglia are implicated in neurodegeneration, potentially by phagocytosing neurons, but it is unclear how to block the detrimental effects of microglia while preserving their beneficial roles. The microglial P2Y
Language	English
Publishing date	2021-12-26
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2021.110148
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Article ; Online: Subcellular localization determines the stability and axon protective capacity of axon survival factor Nmnat2.

Milde, Stefan / Gilley, Jonathan / Coleman, Michael P

PLoS biology

2013 Volume 11, Issue 4, Page(s) e1001539

Abstract: Axons require a constant supply of the labile axon survival factor Nmnat2 from their cell bodies to avoid spontaneous axon degeneration. Here we investigate the mechanism of fast axonal transport of Nmnat2 and its site of action for axon maintenance. ... ...

Abstract	Axons require a constant supply of the labile axon survival factor Nmnat2 from their cell bodies to avoid spontaneous axon degeneration. Here we investigate the mechanism of fast axonal transport of Nmnat2 and its site of action for axon maintenance. Using dual-colour live-cell imaging of axonal transport in SCG primary culture neurons, we find that Nmnat2 is bidirectionally trafficked in axons together with markers of the trans-Golgi network and synaptic vesicles. In contrast, there is little co-migration with mitochondria, lysosomes, and active zone precursor vesicles. Residues encoded by the small, centrally located exon 6 are necessary and sufficient for stable membrane association and vesicular axonal transport of Nmnat2. Within this sequence, a double cysteine palmitoylation motif shared with GAP43 and surrounding basic residues are all required for efficient palmitoylation and stable association with axonal transport vesicles. Interestingly, however, disrupting this membrane association increases the ability of axonally localized Nmnat2 to preserve transected neurites in primary culture, while re-targeting the strongly protective cytosolic mutants back to membranes abolishes this increase. Larger deletions within the central domain including exon 6 further enhance Nmnat2 axon protective capacity to levels that exceed that of the slow Wallerian degeneration protein, Wld(S). The mechanism underlying the increase in axon protection appears to involve an increased half-life of the cytosolic forms, suggesting a role for palmitoylation and membrane attachment in Nmnat2 turnover. We conclude that Nmnat2 activity supports axon survival through a site of action distinct from Nmnat2 transport vesicles and that protein stability, a key determinant of axon protection, is enhanced by mutations that disrupt palmitoylation and dissociate Nmnat2 from these vesicles.
MeSH term(s)	Amino Acid Motifs ; Animals ; Axons/physiology ; Cell Survival ; Cells, Cultured ; Exons ; Golgi Apparatus/metabolism ; Half-Life ; Intracellular Membranes/metabolism ; Lipoylation ; Mice ; Mice, Inbred C57BL ; Neurons/physiology ; Nicotinamide-Nucleotide Adenylyltransferase/physiology ; Primary Cell Culture ; Protein Multimerization ; Protein Stability ; Protein Transport ; Single-Cell Analysis ; Time-Lapse Imaging ; Transport Vesicles/metabolism ; Ubiquitination
Chemical Substances	Nicotinamide-Nucleotide Adenylyltransferase (EC 2.7.7.1) ; Nmnat2 protein, mouse (EC 2.7.7.1)
Language	English
Publishing date	2013-04-16
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2126776-5
ISSN	1545-7885 ; 1544-9173
ISSN (online)	1545-7885
ISSN	1544-9173
DOI	10.1371/journal.pbio.1001539
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Article ; Online: Axonal trafficking of NMNAT2 and its roles in axon growth and survival in vivo.

Milde, Stefan / Gilley, Jonathan / Coleman, Michael P

Bioarchitecture

2013 Volume 3, Issue 5, Page(s) 133–140

Abstract: The NAD-synthesizing enzyme NMNAT2 is critical for axon survival in primary culture and its depletion may contribute to axon degeneration in a variety of neurodegenerative disorders. Here we discuss several recent reports from our laboratory that ... ...

Abstract	The NAD-synthesizing enzyme NMNAT2 is critical for axon survival in primary culture and its depletion may contribute to axon degeneration in a variety of neurodegenerative disorders. Here we discuss several recent reports from our laboratory that establish a critical role for NMNAT2 in axon growth in vivo in mice and shed light on the delivery and turnover of this survival factor in axons. In the absence of NMNAT2, axons fail to extend more than a short distance beyond the cell body during embryonic development, implying a requirement for NMNAT2 in axon maintenance even during development. Furthermore, we highlight findings regarding the bidirectional trafficking of NMNAT2 in axons on a vesicle population that undergoes fast axonal transport in primary culture neurites and in mouse sciatic nerve axons in vivo. Surprisingly, loss of vesicle association boosts the axon protective capacity of NMNAT2, an effect that is at least partially mediated by a longer protein half-life of cytosolic NMNAT2 variants. Analysis of wild-type and variant NMNAT2 in mouse sciatic nerves and Drosophila olfactory receptor neuron axons supports the existence of a similar mechanism in vivo, highlighting the potential for regulation of NMNAT2 stability and turnover as a mechanism to modulate axon degeneration in vivo.
MeSH term(s)	Animals ; Axons/metabolism ; Axons/pathology ; Axons/physiology ; Gene Deletion ; Nerve Degeneration/metabolism ; Nerve Degeneration/pathology ; Neurites/pathology ; Nicotinamide-Nucleotide Adenylyltransferase/genetics ; Nicotinamide-Nucleotide Adenylyltransferase/metabolism ; Nicotinamide-Nucleotide Adenylyltransferase/physiology ; Subcellular Fractions/metabolism ; Wallerian Degeneration/pathology ; Wallerian Degeneration/physiopathology
Chemical Substances	Nicotinamide-Nucleotide Adenylyltransferase (EC 2.7.7.1)
Language	English
Publishing date	2013-11-07
Publishing country	United States
Document type	Journal Article ; Comment
ISSN	1949-100X
ISSN (online)	1949-100X
DOI	10.4161/bioa.27049
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Article ; Online: Axonal transport declines with age in two distinct phases separated by a period of relative stability.

Milde, Stefan / Adalbert, Robert / Elaman, M Handan / Coleman, Michael P

Neurobiology of aging

2014 Volume 36, Issue 2, Page(s) 971–981

Abstract: Axonal transport is critical for supplying newly synthesized proteins, organelles, mRNAs, and other cargoes from neuronal cell bodies into axons. Its impairment in many neurodegenerative conditions appears likely to contribute to pathogenesis. Axonal ... ...

Abstract	Axonal transport is critical for supplying newly synthesized proteins, organelles, mRNAs, and other cargoes from neuronal cell bodies into axons. Its impairment in many neurodegenerative conditions appears likely to contribute to pathogenesis. Axonal transport also declines during normal aging, but little is known about the timing of these changes, or about the effect of aging on specific cargoes in individual axons. This is important for understanding mechanisms of age-related axon loss and age-related axonal disorders. Here we use fluorescence live imaging of peripheral nerve and central nervous system tissue explants to investigate vesicular and mitochondrial axonal transport. Interestingly, we identify 2 distinct periods of change, 1 period during young adulthood and the other in old age, separated by a relatively stable plateau during most of adult life. We also find that after tibial nerve regeneration, even in old animals, neurons are able to support higher transport rates of each cargo for a prolonged period. Thus, the age-related decline in axonal transport is not an inevitable consequence of either aging neurons or an aging systemic milieu.
MeSH term(s)	Aging/pathology ; Aging/physiology ; Animals ; Axonal Transport/physiology ; Axons/metabolism ; Axons/pathology ; Female ; Humans ; Male ; Mice, Inbred C57BL ; Mice, Transgenic ; Mitochondria/metabolism ; Molecular Imaging ; Nerve Regeneration ; Neurodegenerative Diseases/etiology ; Neurodegenerative Diseases/metabolism ; Nicotinamide-Nucleotide Adenylyltransferase/physiology ; Optical Imaging ; Peripheral Nerves/metabolism ; Tibial Nerve/physiology
Chemical Substances	Nicotinamide-Nucleotide Adenylyltransferase (EC 2.7.7.1) ; Nmnat2 protein, mouse (EC 2.7.7.1)
Language	English
Publishing date	2014-09-28
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	604505-4
ISSN	1558-1497 ; 0197-4580
ISSN (online)	1558-1497
ISSN	0197-4580
DOI	10.1016/j.neurobiolaging.2014.09.018
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Zs.A 1685: 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: Interaction between a MAPT variant causing frontotemporal dementia and mutant APP affects axonal transport.

Adalbert, Robert / Milde, Stefan / Durrant, Claire / Ando, Kunie / Stygelbout, Virginie / Yilmaz, Zehra / Gould, Stacey / Brion, Jean-Pierre / Coleman, Michael P

Neurobiology of aging

2018 Volume 68, Page(s) 68–75

Abstract: In Alzheimer's disease, many indicators point to a central role for poor axonal transport, but the potential for stimulating axonal transport to alleviate the disease remains largely untested. Previously, we reported enhanced anterograde axonal transport ...

Abstract	In Alzheimer's disease, many indicators point to a central role for poor axonal transport, but the potential for stimulating axonal transport to alleviate the disease remains largely untested. Previously, we reported enhanced anterograde axonal transport of mitochondria in 8- to 11-month-old MAPT
MeSH term(s)	Aging/genetics ; Aging/metabolism ; Aging/physiology ; Alzheimer Disease/etiology ; Alzheimer Disease/genetics ; Alzheimer Disease/metabolism ; Alzheimer Disease/pathology ; Amyloid beta-Peptides/genetics ; Amyloid beta-Peptides/metabolism ; Amyloid beta-Protein Precursor/genetics ; Animals ; Axonal Transport/genetics ; Axonal Transport/physiology ; Brain/metabolism ; Brain/pathology ; Disease Models, Animal ; Frontotemporal Dementia/etiology ; Frontotemporal Dementia/genetics ; Frontotemporal Dementia/metabolism ; Frontotemporal Dementia/pathology ; Genetic Association Studies ; Genetic Variation ; Male ; Mice, Inbred C57BL ; Mice, Transgenic ; Mitochondria/genetics ; Mitochondria/metabolism ; Mutation ; Plaque, Amyloid/metabolism ; tau Proteins/genetics ; tau Proteins/metabolism
Chemical Substances	Amyloid beta-Peptides ; Amyloid beta-Protein Precursor ; MAPT protein, human ; tau Proteins
Language	English
Publishing date	2018-04-05
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	604505-4
ISSN	1558-1497 ; 0197-4580
ISSN (online)	1558-1497
ISSN	0197-4580
DOI	10.1016/j.neurobiolaging.2018.03.033
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