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  1. Article ; Online: Cell-contact-mediated assembly of contractile airway smooth muscle rings.

    Tjong, Jonathan / Pendlmayr, Stefan / Barter, Jena / Chen, Julie / Maksym, Geoffrey N / Quinn, T Alexander / Frampton, John P

    Biomedical materials (Bristol, England)

    2023  Volume 18, Issue 2

    Abstract: Microtissues in the shape of toroidal rings provide an ideal geometry to better represent the structure and function of the airway smooth muscle present in the small airways, and to better understand diseases such as asthma. Here, polydimethylsiloxane ... ...

    Abstract Microtissues in the shape of toroidal rings provide an ideal geometry to better represent the structure and function of the airway smooth muscle present in the small airways, and to better understand diseases such as asthma. Here, polydimethylsiloxane devices consisting of a series of circular channels surrounding central mandrels are used to form microtissues in the shape of toroidal rings by way of the self-aggregation and -assembly of airway smooth muscle cell (ASMC) suspensions. Over time, the ASMCs present in the rings become spindle-shaped and axially align along the ring circumference. Ring strength and elastic modulus increase over 14 d in culture, without significant changes in ring size. Gene expression analysis indicates stable expression of mRNA for extracellular matrix-associated proteins, including collagen I and laminins
    MeSH term(s) Humans ; Cells, Cultured ; Muscle, Smooth/metabolism ; Transforming Growth Factor beta1/metabolism ; Asthma/metabolism ; Extracellular Matrix Proteins ; Myocytes, Smooth Muscle ; RNA, Messenger/metabolism
    Chemical Substances Transforming Growth Factor beta1 ; Extracellular Matrix Proteins ; RNA, Messenger
    Language English
    Publishing date 2023-03-01
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2265222-X
    ISSN 1748-605X ; 1748-6041
    ISSN (online) 1748-605X
    ISSN 1748-6041
    DOI 10.1088/1748-605X/acbd09
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 6626: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

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  2. Article ; Online: The micro-architecture of mitochondria at active zones: electron tomography reveals novel anchoring scaffolds and cristae structured for high-rate metabolism.

    Perkins, Guy A / Tjong, Jonathan / Brown, Joshua M / Poquiz, Patrick H / Scott, Raymond T / Kolson, Douglas R / Ellisman, Mark H / Spirou, George A

    The Journal of neuroscience : the official journal of the Society for Neuroscience

    2010  Volume 30, Issue 3, Page(s) 1015–1026

    Abstract: Mitochondria are integral elements of many nerve terminals. They must be appropriately positioned to regulate microdomains of Ca(2+) concentration and metabolic demand, but structures that anchor them in place have not been described. By applying the ... ...

    Abstract Mitochondria are integral elements of many nerve terminals. They must be appropriately positioned to regulate microdomains of Ca(2+) concentration and metabolic demand, but structures that anchor them in place have not been described. By applying the high resolution of electron tomography (ET) to the study of a central terminal, the calyx of Held, we revealed an elaborate cytoskeletal superstructure that connected a subset of mitochondria to the presynaptic membrane near active zones. This cytoskeletal network extended laterally and was well integrated into the nerve terminal cytoskeleton, which included filamentous linkages among synaptic vesicles. ET revealed novel features of inner membrane for these mitochondria. Crista structure was polarized in that crista junctions, circular openings of the inner membrane under the outer membrane, were aligned with the cytoskeletal superstructure and occurred at higher density in mitochondrial membrane facing the presynaptic membrane. These characteristics represent the first instance where a subcomponent of an organelle is shown to have a specific orientation relative to the polarized structure of a cell. The ratio of cristae to outer membrane surface area is large in these mitochondria relative to other tissues, indicating a high metabolic capacity. These observations suggest general principles for cytoskeletal anchoring of mitochondria in all tissues, reveal potential routes for nonsynaptic communication between presynaptic and postsynaptic partners using this novel cytoskeletal framework, and indicate that crista structure can be specialized for particular functions within cellular microdomains.
    MeSH term(s) Animals ; Biotin/analogs & derivatives ; Biotin/metabolism ; Cats ; Cyclooxygenase 1/metabolism ; Cytoskeleton/ultrastructure ; Dextrans/metabolism ; Electron Microscope Tomography/methods ; Image Processing, Computer-Assisted ; Microtubule-Associated Proteins/metabolism ; Mitochondria/metabolism ; Mitochondria/ultrastructure ; Pons/ultrastructure ; Presynaptic Terminals/ultrastructure ; Synapses/ultrastructure ; Synaptic Vesicles/ultrastructure ; Vesicular Glutamate Transport Proteins/metabolism
    Chemical Substances Dextrans ; Microtubule-Associated Proteins ; Vesicular Glutamate Transport Proteins ; biotinylated dextran amine ; Biotin (6SO6U10H04) ; Cyclooxygenase 1 (EC 1.14.99.1)
    Language English
    Publishing date 2010-01-20
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 604637-x
    ISSN 1529-2401 ; 0270-6474
    ISSN (online) 1529-2401
    ISSN 0270-6474
    DOI 10.1523/JNEUROSCI.1517-09.2010
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1668: 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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  3. Article ; Online: Ultrastructural modifications in the mitochondria of hypoxia-adapted Drosophila melanogaster.

    Perkins, Guy / Hsiao, Yu-hsin / Yin, Songyue / Tjong, Jonathan / Tran, My T / Lau, Jenna / Xue, Jin / Liu, Siqi / Ellisman, Mark H / Zhou, Dan

    PloS one

    2012  Volume 7, Issue 9, Page(s) e45344

    Abstract: Chronic hypoxia (CH) occurs under certain physiological or pathological conditions, including in people who reside at high altitude or suffer chronic cardiovascular or pulmonary diseases. As mitochondria are the predominant oxygen-consuming organelles to ...

    Abstract Chronic hypoxia (CH) occurs under certain physiological or pathological conditions, including in people who reside at high altitude or suffer chronic cardiovascular or pulmonary diseases. As mitochondria are the predominant oxygen-consuming organelles to generate ATP through oxidative phosphorylation in cells, their responses, through structural or molecular modifications, to limited oxygen supply play an important role in the overall functional adaptation to hypoxia. Here, we report the adaptive mitochondrial ultrastructural modifications and the functional impacts in a recently generated hypoxia-adapted Drosophila melanogaster strain that survives severe, otherwise lethal, hypoxic conditions. Using electron tomography, we discovered increased mitochondrial volume density and cristae abundance, yet also cristae fragmentation and a unique honeycomb-like structure in the mitochondria of hypoxia-adapted flies. The homeostatic levels of adenylate and energy charge were similar between hypoxia-adapted and naïve control flies and the hypoxia-adapted flies remained active under severe hypoxia as quantified by negative geotaxis behavior. The equilibrium ATP level was lower in hypoxia-adapted flies than those of the naïve controls tested under severe hypoxia that inhibited the motion of control flies. Our results suggest that the structural rearrangement in the mitochondria of hypoxia-adapted flies may be an important adaptive mechanism that plays a critical role in preserving adenylate homeostasis and metabolism as well as muscle function under chronic hypoxic conditions.
    MeSH term(s) Adaptation, Physiological/physiology ; Adenosine Triphosphate/metabolism ; Animals ; Drosophila melanogaster/physiology ; Drosophila melanogaster/ultrastructure ; Hypoxia/physiopathology ; Mitochondria/physiology ; Mitochondria/ultrastructure ; Oxidative Stress/physiology
    Chemical Substances Adenosine Triphosphate (8L70Q75FXE)
    Language English
    Publishing date 2012-09-19
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ISSN 1932-6203
    ISSN (online) 1932-6203
    DOI 10.1371/journal.pone.0045344
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Mitochondrial rejuvenation after induced pluripotency.

    Suhr, Steven T / Chang, Eun Ah / Tjong, Jonathan / Alcasid, Nathan / Perkins, Guy A / Goissis, Marcelo D / Ellisman, Mark H / Perez, Gloria I / Cibelli, Jose B

    PloS one

    2010  Volume 5, Issue 11, Page(s) e14095

    Abstract: Background: As stem cells of the early embryo mature and differentiate into all tissues, the mitochondrial complement undergoes dramatic functional improvement. Mitochondrial activity is low to minimize generation of DNA-damaging reactive oxygen species ...

    Abstract Background: As stem cells of the early embryo mature and differentiate into all tissues, the mitochondrial complement undergoes dramatic functional improvement. Mitochondrial activity is low to minimize generation of DNA-damaging reactive oxygen species during pre-implantation development and increases following implantation and differentiation to meet higher metabolic demands. It has recently been reported that when the stem cell type known as induced pluripotent stem cells (IPSCs) are re-differentiated for several weeks in vitro, the mitochondrial complement progressively re-acquires properties approximating input fibroblasts, suggesting that despite the observation that IPSC conversion "resets" some parameters of cellular aging such as telomere length, it may have little impact on other age-affected cellular systems such as mitochondria in IPSC-derived cells.
    Methodology/principal findings: We have examined the properties of mitochondria in two fibroblast lines, corresponding IPSCs, and fibroblasts re-derived from IPSCs using biochemical methods and electron microscopy, and found a dramatic improvement in the quality and function of the mitochondrial complement of the re-derived fibroblasts compared to input fibroblasts. This observation likely stems from two aspects of our experimental design: 1) that the input cell lines used were of advanced cellular age and contained an inefficient mitochondrial complement, and 2) the re-derived fibroblasts were produced using an extensive differentiation regimen that may more closely mimic the degree of growth and maturation found in a developing mammal.
    Conclusions/significance: These results - coupled with earlier data from our laboratory - suggest that IPSC conversion not only resets the "biological clock", but can also rejuvenate the energetic capacity of derived cells.
    MeSH term(s) Adenosine Diphosphate/metabolism ; Adenosine Triphosphate/metabolism ; Cell Differentiation/physiology ; Cell Line ; Energy Metabolism/physiology ; Fibroblasts/cytology ; Fibroblasts/metabolism ; Fibroblasts/physiology ; Humans ; Induced Pluripotent Stem Cells/cytology ; Induced Pluripotent Stem Cells/physiology ; Membrane Potential, Mitochondrial/physiology ; Microscopy, Electron ; Mitochondria/metabolism ; Mitochondria/physiology ; Mitochondria/ultrastructure
    Chemical Substances Adenosine Diphosphate (61D2G4IYVH) ; Adenosine Triphosphate (8L70Q75FXE)
    Language English
    Publishing date 2010-11-23
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ISSN 1932-6203
    ISSN (online) 1932-6203
    DOI 10.1371/journal.pone.0014095
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Mutant huntingtin binds the mitochondrial fission GTPase dynamin-related protein-1 and increases its enzymatic activity.

    Song, Wenjun / Chen, Jin / Petrilli, Alejandra / Liot, Geraldine / Klinglmayr, Eva / Zhou, Yue / Poquiz, Patrick / Tjong, Jonathan / Pouladi, Mahmoud A / Hayden, Michael R / Masliah, Eliezer / Ellisman, Mark / Rouiller, Isabelle / Schwarzenbacher, Robert / Bossy, Blaise / Perkins, Guy / Bossy-Wetzel, Ella

    Nature medicine

    2011  Volume 17, Issue 3, Page(s) 377–382

    Abstract: Huntington's disease is an inherited and incurable neurodegenerative disorder caused by an abnormal polyglutamine (polyQ) expansion in huntingtin (encoded by HTT). PolyQ length determines disease onset and severity, with a longer expansion causing ... ...

    Abstract Huntington's disease is an inherited and incurable neurodegenerative disorder caused by an abnormal polyglutamine (polyQ) expansion in huntingtin (encoded by HTT). PolyQ length determines disease onset and severity, with a longer expansion causing earlier onset. The mechanisms of mutant huntingtin-mediated neurotoxicity remain unclear; however, mitochondrial dysfunction is a key event in Huntington's disease pathogenesis. Here we tested whether mutant huntingtin impairs the mitochondrial fission-fusion balance and thereby causes neuronal injury. We show that mutant huntingtin triggers mitochondrial fragmentation in rat neurons and fibroblasts of individuals with Huntington's disease in vitro and in a mouse model of Huntington's disease in vivo before the presence of neurological deficits and huntingtin aggregates. Mutant huntingtin abnormally interacts with the mitochondrial fission GTPase dynamin-related protein-1 (DRP1) in mice and humans with Huntington's disease, which, in turn, stimulates its enzymatic activity. Mutant huntingtin-mediated mitochondrial fragmentation, defects in anterograde and retrograde mitochondrial transport and neuronal cell death are all rescued by reducing DRP1 GTPase activity with the dominant-negative DRP1 K38A mutant. Thus, DRP1 might represent a new therapeutic target to combat neurodegeneration in Huntington's disease.
    MeSH term(s) Animals ; Disease Models, Animal ; Dynamins ; GTP Phosphohydrolases/metabolism ; Humans ; Huntingtin Protein ; Mice ; Microtubule-Associated Proteins/metabolism ; Mitochondria/enzymology ; Mitochondria/metabolism ; Mitochondrial Proteins/metabolism ; Mutation ; Nerve Tissue Proteins/genetics ; Nerve Tissue Proteins/metabolism ; Nuclear Proteins/genetics ; Nuclear Proteins/metabolism ; Protein Binding
    Chemical Substances HTT protein, human ; Huntingtin Protein ; Microtubule-Associated Proteins ; Mitochondrial Proteins ; Nerve Tissue Proteins ; Nuclear Proteins ; GTP Phosphohydrolases (EC 3.6.1.-) ; DNM1L protein, human (EC 3.6.5.5) ; Dynamins (EC 3.6.5.5)
    Language English
    Publishing date 2011-02-20
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 1220066-9
    ISSN 1546-170X ; 1078-8956
    ISSN (online) 1546-170X
    ISSN 1078-8956
    DOI 10.1038/nm.2313
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 4212: Show issues Location:
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    Jg. 1995 - 2021: Lesesall (2.OG)
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    Zs.MG 39: Show issues

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