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  1. Article ; Online: Polycystin-2 Is Required for Chondrocyte Mechanotransduction and Traffics to the Primary Cilium in Response to Mechanical Stimulation.

    Thompson, Clare L / McFie, Megan / Chapple, J Paul / Beales, Philip / Knight, Martin M

    International journal of molecular sciences

    2021  Volume 22, Issue 9

    Abstract: Primary cilia and associated intraflagellar transport are essential for skeletal development, joint homeostasis, and the response to mechanical stimuli, although the mechanisms remain unclear. Polycystin-2 (PC2) is a member of the transient receptor ... ...

    Abstract Primary cilia and associated intraflagellar transport are essential for skeletal development, joint homeostasis, and the response to mechanical stimuli, although the mechanisms remain unclear. Polycystin-2 (PC2) is a member of the transient receptor potential polycystic (TRPP) family of cation channels, and together with Polycystin-1 (PC1), it has been implicated in cilia-mediated mechanotransduction in epithelial cells. The current study investigates the effect of mechanical stimulation on the localization of ciliary polycystins in chondrocytes and tests the hypothesis that they are required in chondrocyte mechanosignaling. Isolated chondrocytes were subjected to mechanical stimulation in the form of uniaxial cyclic tensile strain (CTS) in order to examine the effects on PC2 ciliary localization and matrix gene expression. In the absence of strain, PC2 localizes to the chondrocyte ciliary membrane and neither PC1 nor PC2 are required for ciliogenesis. Cartilage matrix gene expression (
    MeSH term(s) Animals ; Calcium/metabolism ; Cattle ; Chondrocytes/cytology ; Chondrocytes/metabolism ; Chondrocytes/physiology ; Cilia/metabolism ; Mechanotransduction, Cellular ; Protein Transport ; TRPP Cation Channels/metabolism
    Chemical Substances TRPP Cation Channels ; polycystic kidney disease 1 protein ; polycystic kidney disease 2 protein ; Calcium (SY7Q814VUP)
    Language English
    Publishing date 2021-04-21
    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/ijms22094313
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Cilia protein IFT88 regulates extracellular protease activity by optimizing LRP-1-mediated endocytosis.

    Coveney, Clarissa R / Collins, Isabella / Mc Fie, Megan / Chanalaris, Anastasios / Yamamoto, Kazuhiro / Wann, Angus K T

    FASEB journal : official publication of the Federation of American Societies for Experimental Biology

    2018  , Page(s) fj201800334

    Abstract: Matrix protease activity is fundamental to developmental tissue patterning and remains influential in adult homeostasis. In cartilage, the principal matrix proteoglycan is aggrecan, the protease-mediated catabolism of which defines arthritis; however, ... ...

    Abstract Matrix protease activity is fundamental to developmental tissue patterning and remains influential in adult homeostasis. In cartilage, the principal matrix proteoglycan is aggrecan, the protease-mediated catabolism of which defines arthritis; however, the pathophysiologic mechanisms that drive aberrant aggrecanolytic activity remain unclear. Human ciliopathies exhibit altered matrix, which has been proposed to be the result of dysregulated hedgehog signaling that is tuned within the primary cilium. Here, we report that disruption of intraflagellar transport protein 88 (IFT88), a core ciliary trafficking protein, increases chondrocyte aggrecanase activity in vitro. We find that the receptor for protease endocytosis in chondrocytes, LDL receptor-related protein 1 (LRP-1), is unevenly distributed over the cell membrane, often concentrated at the site of cilia assembly. Hypomorphic mutation of IFT88 disturbs this apparent hot spot for protease uptake, increases receptor shedding, and results in a reduced rate of protease clearance from the extracellular space. We propose that IFT88 and/or the cilium regulates the extracellular remodeling of matrix-independently of Hedgehog regulation-by enabling rapid LRP-1-mediated endocytosis of proteases, potentially by supporting the creation of a ciliary pocket. This result highlights new roles for the cilium's machinery in matrix turnover and LRP-1 function, with potential relevance in a range of diseases.-Coveney, C. R., Collins, I., Mc Fie, M., Chanalaris, A., Yamamoto, K., Wann, A. K. T. Cilia protein IFT88 regulates extracellular protease activity by optimizing LRP-1-mediated endocytosis.
    Language English
    Publishing date 2018-06-19
    Publishing country United States
    Document type Journal Article
    ZDB-ID 639186-2
    ISSN 1530-6860 ; 0892-6638
    ISSN (online) 1530-6860
    ISSN 0892-6638
    DOI 10.1096/fj.201800334
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 2266: 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)
    Zs.MO 296: Show issues

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  3. Article ; Online: Ciliary proteins specify the cell inflammatory response by tuning NFκB signalling, independently of primary cilia.

    Mc Fie, Megan / Koneva, Lada / Collins, Isabella / Coveney, Clarissa R / Clube, Aisling M / Chanalaris, Anastasios / Vincent, Tonia L / Bezbradica, Jelena S / Sansom, Stephen N / Wann, Angus K T

    Journal of cell science

    2020  Volume 133, Issue 13

    Abstract: Complex inflammatory signalling cascades define the response to tissue injury but also control development and homeostasis, limiting the potential for these pathways to be targeted therapeutically. Primary cilia are subcellular regulators of cellular ... ...

    Abstract Complex inflammatory signalling cascades define the response to tissue injury but also control development and homeostasis, limiting the potential for these pathways to be targeted therapeutically. Primary cilia are subcellular regulators of cellular signalling, controlling how signalling is organized, encoded and, in some instances, driving or influencing pathogenesis. Our previous research revealed that disruption of ciliary intraflagellar transport (IFT), altered the cell response to IL-1β, supporting a putative link emerging between cilia and inflammation. Here, we show that IFT88 depletion affects specific cytokine-regulated behaviours, changing cytosolic NFκB translocation dynamics but leaving MAPK signalling unaffected. RNA-seq analysis indicates that IFT88 regulates one third of the genome-wide targets, including the pro-inflammatory genes
    MeSH term(s) Cilia/metabolism ; Flagella/metabolism ; NF-kappa B/genetics ; NF-kappa B/metabolism ; Protein Transport ; Signal Transduction
    Chemical Substances NF-kappa B
    Language English
    Publishing date 2020-07-08
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2993-2
    ISSN 1477-9137 ; 0021-9533
    ISSN (online) 1477-9137
    ISSN 0021-9533
    DOI 10.1242/jcs.239871
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1200: 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)
    Zs.MG 14: Show issues

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  4. Article ; Online: Abnormal pro-gly-pro pathway and airway neutrophilia in pediatric cystic fibrosis.

    Turnbull, Andrew R / Pyle, Chloe J / Patel, Dhiren F / Jackson, Patricia L / Hilliard, Tom N / Regamey, Nicolas / Tan, Hui-Leng / Brown, Sarah / Thursfield, Rebecca / Short, Christopher / Mc Fie, Megan / Alton, Eric W F W / Gaggar, Amit / Blalock, J Edwin / Lloyd, Clare M / Bush, Andrew / Davies, Jane C / Snelgrove, Robert J

    Journal of cystic fibrosis : official journal of the European Cystic Fibrosis Society

    2019  Volume 19, Issue 1, Page(s) 40–48

    Abstract: Background: Proline-glycine-proline (PGP) is a bioactive fragment of collagen generated by the action of matrix metalloproteinase-9 (MMP-9) and prolylendopeptidase (PE), and capable of eliciting neutrophil chemotaxis and epithelial remodelling. PGP is ... ...

    Abstract Background: Proline-glycine-proline (PGP) is a bioactive fragment of collagen generated by the action of matrix metalloproteinase-9 (MMP-9) and prolylendopeptidase (PE), and capable of eliciting neutrophil chemotaxis and epithelial remodelling. PGP is normally then degraded by leukotriene A
    Methods: Broncho-alveolar lavage (BAL) fluid was obtained from 38 CF (9 newborns and 29 older children) and 24 non-CF children. BAL cell differentials and levels of PGP, MMP-9, PE and LTA
    Results: Whilst PGP was present in all but one of the older CF children tested, it was absent in non-CF controls and the vast majority of CF newborns. BAL levels of MMP-9 and PE were elevated in older children with CF relative to CF newborns and non-CF controls, correlating with airway neutrophilia and supportive of PGP generation. Furthermore, despite extracellular LTA
    Conclusions: A striking imbalance between PGP-generating and -degrading enzymes enables PGP accumulation in CF children from early life and potentially supports airway neutrophilia.
    MeSH term(s) Airway Remodeling/immunology ; Bronchoalveolar Lavage Fluid/immunology ; Bronchoscopy/methods ; Chemotaxis, Leukocyte/immunology ; Child ; Cystic Fibrosis/diagnosis ; Cystic Fibrosis/immunology ; Cystic Fibrosis/physiopathology ; Female ; Humans ; Infant, Newborn ; Inflammation/metabolism ; Leukocyte Elastase/metabolism ; Male ; Matrix Metalloproteinase 9/metabolism ; Neutrophils/immunology ; Neutrophils/pathology ; Oligopeptides/metabolism ; Proline/analogs & derivatives ; Proline/metabolism ; Prolyl Oligopeptidases/metabolism ; Sputum/immunology
    Chemical Substances Oligopeptides ; prolyl-glycyl-proline ; Proline (9DLQ4CIU6V) ; Prolyl Oligopeptidases (EC 3.4.21.26) ; Leukocyte Elastase (EC 3.4.21.37) ; Matrix Metalloproteinase 9 (EC 3.4.24.35)
    Language English
    Publishing date 2019-06-05
    Publishing country Netherlands
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 2084724-5
    ISSN 1873-5010 ; 1569-1993
    ISSN (online) 1873-5010
    ISSN 1569-1993
    DOI 10.1016/j.jcf.2019.05.017
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 6028: Show issues Location:
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    Zs.MO 459: Show issues

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