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  1. Article: Mature primary human osteocytes in mini organotypic cultures secrete FGF23 and PTH1-34-regulated sclerostin.

    Knowles, Helen J / Chanalaris, Anastasios / Koutsikouni, Argyro / Cribbs, Adam P / Grover, Liam M / Hulley, Philippa A

    Frontiers in endocrinology

    2023  Volume 14, Page(s) 1167734

    Abstract: Introduction: For decades, functional primary human osteocyte cultures have been crucially needed for understanding their role in bone anabolic processes and in endocrine phosphate regulation via the bone-kidney axis. Mature osteocyte proteins ( ... ...

    Abstract Introduction: For decades, functional primary human osteocyte cultures have been crucially needed for understanding their role in bone anabolic processes and in endocrine phosphate regulation via the bone-kidney axis. Mature osteocyte proteins (sclerostin, DMP1, Phex and FGF23) play a key role in various systemic diseases and are targeted by successful bone anabolic drugs (anti-sclerostin antibody and teriparatide (PTH1-34)). However, cell lines available to study osteocytes produce very little sclerostin and low levels of mature osteocyte markers. We have developed a primary human 3D organotypic culture system that replicates the formation of mature osteocytes in bone.
    Methods: Primary human osteoblasts were seeded in a fibrinogen / thrombin gel around 3D-printed hanging posts. Following contraction of the gel around the posts, cells were cultured in osteogenic media and conditioned media was collected for analysis of secreted markers of osteocyte formation.
    Results: The organoids were viable for at least 6 months, allowing co-culture with different cell types and testing of bone anabolic drugs. Bulk RNAseq data displayed the developing marker trajectory of ossification and human primary osteocyte formation
    Discussion: This 3D organotypic culture system provides a stable, long-lived, and regulated population of mature human primary osteocytes for a variety of research applications.
    MeSH term(s) Humans ; Microphysiological Systems ; Osteocytes ; Organoids ; Osteoblasts ; Biological Transport
    Language English
    Publishing date 2023-05-08
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2592084-4
    ISSN 1664-2392
    ISSN 1664-2392
    DOI 10.3389/fendo.2023.1167734
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Heparan Sulfate Proteoglycan Synthesis Is Dysregulated in Human Osteoarthritic Cartilage.

    Chanalaris, Anastasios / Clarke, Hannah / Guimond, Scott E / Vincent, Tonia L / Turnbull, Jeremy E / Troeberg, Linda

    The American journal of pathology

    2018  Volume 189, Issue 3, Page(s) 632–647

    Abstract: Osteoarthritis (OA) is a common degenerative joint disease, characterized by cartilage loss and subchondral bone remodeling in response to abnormal mechanical load. Heparan sulfate (HS) proteoglycans bind to many proteins that regulate cartilage ... ...

    Abstract Osteoarthritis (OA) is a common degenerative joint disease, characterized by cartilage loss and subchondral bone remodeling in response to abnormal mechanical load. Heparan sulfate (HS) proteoglycans bind to many proteins that regulate cartilage homeostasis, including growth factors, morphogens, proteases, and their inhibitors, and modulate their localization, retention, and biological activity. Changes in HS expression and structure may thus have important consequences for joint health. We analyzed normal and osteoarthritic human knee cartilage, and found HS biosynthesis was markedly disrupted in OA, with 45% of the 38 genes analyzed differentially regulated in diseased cartilage. The expression of several HS core proteins, biosynthesis, and modification enzymes was increased in OA cartilage, whereas the expression of the HS proteoglycans syndecan 4 and betaglycan was reduced. The structure of HS was also altered, with increased levels of 6-O-sulfation in osteoarthritic samples, which correlated with increased expression of HS6ST1, a 6-O-sulfotransferase, and GLCE, an epimerase that promotes 6-O-sulfation. siRNA silencing of HS6ST1 expression in primary OA chondrocytes inhibited extracellular signal-regulated kinase phosphorylation in response to fibroblast growth factor 2, showing that changes in 6-O-sulfation impact a key cartilage signaling pathway. Given the broad range of homeostatic and repair pathways that HS regulates, these changes in proteoglycan expression and HS structure are likely to have significant effects on joint health and progression of OA.
    MeSH term(s) Cartilage/metabolism ; Cartilage/pathology ; Chondrocytes/metabolism ; Chondrocytes/pathology ; Female ; Fibroblast Growth Factor 2/metabolism ; Gene Expression Regulation ; Humans ; Knee Joint/metabolism ; Knee Joint/pathology ; MAP Kinase Signaling System ; Male ; Osteoarthritis, Knee/metabolism ; Osteoarthritis, Knee/pathology ; Sulfotransferases/biosynthesis ; Syndecan-4/biosynthesis
    Chemical Substances SDC4 protein, human ; Syndecan-4 ; Fibroblast Growth Factor 2 (103107-01-3) ; Sulfotransferases (EC 2.8.2.-) ; heparan sulfate 6-O-sulfotransferase (EC 2.8.2.-)
    Language English
    Publishing date 2018-12-14
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2943-9
    ISSN 1525-2191 ; 0002-9440
    ISSN (online) 1525-2191
    ISSN 0002-9440
    DOI 10.1016/j.ajpath.2018.11.011
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  3. 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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  4. Article ; Online: TSG-6 Is Weakly Chondroprotective in Murine OA but Does not Account for FGF2-Mediated Joint Protection.

    Zhu, Linyi / Donhou, Shannah / Burleigh, Annika / Miotla Zarebska, Jadwiga / Curtinha, Marcia / Parisi, Ida / Khan, Sumayya Nafisa / Dell'Accio, Francesco / Chanalaris, Anastasios / Vincent, Tonia L

    ACR open rheumatology

    2020  Volume 2, Issue 10, Page(s) 605–615

    Abstract: Objective: Tumor necrosis factor α-stimulated gene 6 (TSG-6) is an anti-inflammatory protein highly expressed in osteoarthritis (OA), but its influence on the course of OA is unknown.: Methods: Cartilage injury was assessed by murine hip avulsion or ... ...

    Abstract Objective: Tumor necrosis factor α-stimulated gene 6 (TSG-6) is an anti-inflammatory protein highly expressed in osteoarthritis (OA), but its influence on the course of OA is unknown.
    Methods: Cartilage injury was assessed by murine hip avulsion or by recutting rested explants. Forty-two previously validated injury genes were quantified by real-time polymerase chain reaction in whole joints following destabilization of the medial meniscus (DMM) (6 hours and 7 days). Joint pathology was assessed at 8 and 12 weeks following DMM in 10-week-old male and female fibroblast growth factor 2 (FGF2)
    Results: TSG-6 messenger RNA upregulation was strongly FGF2-dependent upon injury in vitro and in vivo. Fifteeen inflammatory genes were significantly increased in TSG-6
    Conclusion: TSG-6 influences early gene regulation in the destabilized joint and exerts a modest late chondroprotective effect. Although strongly FGF2 dependent, TSG-6 does not explain the strong chondroprotective effect of FGF2.
    Language English
    Publishing date 2020-10-07
    Publishing country United States
    Document type Journal Article
    ISSN 2578-5745
    ISSN (online) 2578-5745
    DOI 10.1002/acr2.11176
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. 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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  6. Article ; Online: Variants in

    Zhu, Linyi / Kamalathevan, Pragash / Koneva, Lada A / Zarebska, Jadwiga Miotla / Chanalaris, Anastasios / Ismail, Heba / Wiberg, Akira / Ng, Michael / Muhammad, Hayat / Walsby-Tickle, John / McCullagh, James S O / Watt, Fiona E / Sansom, Stephen N / Furniss, Dominic / Gardiner, Matthew D / Vincent, Tonia L / Riley, Nick / Spiteri, Michelle / McNab, Ian /
    Little, Christopher / Cogswell, Lucy / Critchley, Paul / Giele, Henk / Shirley, Rebecca

    Science translational medicine

    2022  Volume 14, Issue 676, Page(s) eabm4054

    Abstract: More than 40% of individuals will develop osteoarthritis (OA) during their lifetime, yet there are currently no licensed disease-modifying treatments for this disabling condition. Common polymorphic variants ... ...

    Abstract More than 40% of individuals will develop osteoarthritis (OA) during their lifetime, yet there are currently no licensed disease-modifying treatments for this disabling condition. Common polymorphic variants in
    MeSH term(s) Mice ; Animals ; Tretinoin/pharmacology ; Tretinoin/therapeutic use ; Tretinoin/metabolism ; Osteoarthritis/drug therapy ; Osteoarthritis/genetics ; Osteoarthritis/metabolism ; Cartilage, Articular/metabolism ; Knee Joint ; Anti-Inflammatory Agents ; Chondrocytes/metabolism ; Aldehyde Dehydrogenase 1 Family/metabolism ; Retinal Dehydrogenase/metabolism
    Chemical Substances Tretinoin (5688UTC01R) ; Anti-Inflammatory Agents ; Aldh1a2 protein, mouse (EC 1.2.1.36) ; Aldehyde Dehydrogenase 1 Family (EC 1.2.1) ; Retinal Dehydrogenase (EC 1.2.1.36)
    Language English
    Publishing date 2022-12-21
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2518854-9
    ISSN 1946-6242 ; 1946-6234
    ISSN (online) 1946-6242
    ISSN 1946-6234
    DOI 10.1126/scitranslmed.abm4054
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  7. Article ; Online: Suramin Inhibits Osteoarthritic Cartilage Degradation by Increasing Extracellular Levels of Chondroprotective Tissue Inhibitor of Metalloproteinases 3.

    Chanalaris, Anastasios / Doherty, Christine / Marsden, Brian D / Bambridge, Gabriel / Wren, Stephen P / Nagase, Hideaki / Troeberg, Linda

    Molecular pharmacology

    2017  Volume 92, Issue 4, Page(s) 459–468

    Abstract: Osteoarthritis is a common degenerative joint disease for which no disease-modifying drugs are currently available. Attempts to treat the disease with small molecule inhibitors of the metalloproteinases that degrade the cartilage matrix have been ... ...

    Abstract Osteoarthritis is a common degenerative joint disease for which no disease-modifying drugs are currently available. Attempts to treat the disease with small molecule inhibitors of the metalloproteinases that degrade the cartilage matrix have been hampered by a lack of specificity. We aimed to inhibit cartilage degradation by augmenting levels of the endogenous metalloproteinase inhibitor, tissue inhibitor of metalloproteinases (TIMP)-3, through blocking its interaction with the endocytic scavenger receptor, low-density lipoprotein receptor-related protein 1 (LRP1). We discovered that suramin (C
    MeSH term(s) Animals ; Cartilage/drug effects ; Cartilage/metabolism ; Cartilage/pathology ; Cell Line, Tumor ; Chondrocytes/drug effects ; Chondrocytes/metabolism ; Chondrocytes/pathology ; Dose-Response Relationship, Drug ; Extracellular Space/drug effects ; Extracellular Space/metabolism ; HEK293 Cells ; Humans ; Organ Culture Techniques ; Osteoarthritis/drug therapy ; Osteoarthritis/metabolism ; Osteoarthritis/pathology ; Protein Binding/physiology ; Suramin/pharmacology ; Suramin/therapeutic use ; Swine ; Tissue Inhibitor of Metalloproteinase-3/metabolism
    Chemical Substances TIMP3 protein, human ; Tissue Inhibitor of Metalloproteinase-3 ; Suramin (6032D45BEM)
    Language English
    Publishing date 2017-08-10
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 124034-1
    ISSN 1521-0111 ; 0026-895X
    ISSN (online) 1521-0111
    ISSN 0026-895X
    DOI 10.1124/mol.117.109397
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: Nociceptive Sensitizers Are Regulated in Damaged Joint Tissues, Including Articular Cartilage, When Osteoarthritic Mice Display Pain Behavior.

    Driscoll, Clare / Chanalaris, Anastasios / Knights, Chancie / Ismail, Heba / Sacitharan, Pradeep K / Gentry, Clive / Bevan, Stuart / Vincent, Tonia L

    Arthritis & rheumatology (Hoboken, N.J.)

    2016  Volume 68, Issue 4, Page(s) 857–867

    Abstract: Objective: Pain is the most common symptom of osteoarthritis (OA), yet where it originates in the joint and how it is driven are unknown. The aim of this study was to identify pain-sensitizing molecules that are regulated in the joint when mice ... ...

    Abstract Objective: Pain is the most common symptom of osteoarthritis (OA), yet where it originates in the joint and how it is driven are unknown. The aim of this study was to identify pain-sensitizing molecules that are regulated in the joint when mice subjected to surgical joint destabilization develop OA-related pain behavior, the tissues in which these molecules are being regulated, and the factors that control their regulation.
    Methods: Ten-week-old mice underwent sham surgery, partial meniscectomy, or surgical destabilization of the medial meniscus (DMM). Pain-related behavior as determined by a variety of methods (testing of responses to von Frey filaments, cold plate testing for cold sensitivity, analgesiometry, incapacitance testing, and forced flexion testing) was assessed weekly. Once pain-related behavior was established, RNA was extracted from either whole joints or microdissected tissue samples (articular cartilage, meniscus, and bone). Reverse transcription-polymerase chain reaction analysis was performed to analyze the expression of 54 genes known to regulate pain sensitization. Cartilage injury assays were performed using avulsed immature hips from wild-type or genetically modified mice or by explanting articular cartilage from porcine joints preinjected with pharmacologic inhibitors. Levels of nerve growth factor (NGF) protein were measured by enzyme-linked immunosorbent assay.
    Results: Mice developed pain-related behavior 8 weeks after undergoing partial meniscectomy or 12 weeks after undergoing DMM. NGF, bradykinin receptors B1 and B2, tachykinin, and tachykinin receptor 1 were significantly regulated in the joints of mice displaying pain-related behavior. Little regulation of inflammatory cytokines, leukocyte activation markers, or chemokines was observed. When tissue samples from articular cartilage, meniscus, and bone were analyzed separately, NGF was consistently regulated in the articular cartilage. The other pain sensitizers were also largely regulated in the articular cartilage, although there were some differences between the 2 models. NGF and tachykinin were strongly regulated by simple mechanical injury of cartilage in vitro in a transforming growth factor β-activated kinase 1-, fibroblast growth factor 2-, and Src kinase-dependent manner.
    Conclusion: Damaged joint tissues produce proalgesic molecules, including NGF, in murine OA.
    MeSH term(s) Animals ; Behavior, Animal ; Bone and Bones/metabolism ; Cartilage, Articular/metabolism ; Disease Models, Animal ; Enzyme-Linked Immunosorbent Assay ; Fibroblast Growth Factor 2 ; Gene Expression Regulation ; MAP Kinase Kinase Kinases ; Menisci, Tibial/metabolism ; Mice ; Nerve Growth Factor/genetics ; Nociceptive Pain/genetics ; Nociceptive Pain/metabolism ; Osteoarthritis, Knee ; Pain/genetics ; Pain/metabolism ; Receptor, Bradykinin B1/genetics ; Receptor, Bradykinin B2/genetics ; Receptors, Neurokinin-1/genetics ; Reverse Transcriptase Polymerase Chain Reaction ; Swine ; Tachykinins/genetics ; Tibial Meniscus Injuries ; src-Family Kinases
    Chemical Substances Receptor, Bradykinin B1 ; Receptor, Bradykinin B2 ; Receptors, Neurokinin-1 ; Tachykinins ; Fibroblast Growth Factor 2 (103107-01-3) ; Nerve Growth Factor (9061-61-4) ; src-Family Kinases (EC 2.7.10.2) ; MAP Kinase Kinase Kinases (EC 2.7.11.25) ; MAP kinase kinase kinase 7 (EC 2.7.11.25)
    Language English
    Publishing date 2016-04
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2756371-6
    ISSN 2326-5205 ; 2326-5191
    ISSN (online) 2326-5205
    ISSN 2326-5191
    DOI 10.1002/art.39523
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  9. Article ; Online: Establishment of computational biology in Greece and Cyprus: Past, present, and future.

    Chasapi, Anastasia / Aivaliotis, Michalis / Angelis, Lefteris / Chanalaris, Anastasios / Iliopoulos, Ioannis / Kappas, Ilias / Karapiperis, Christos / Kyrpides, Nikos C / Pafilis, Evangelos / Panteris, Eleftherios / Topalis, Pantelis / Tsiamis, George / Vizirianakis, Ioannis S / Vlassi, Metaxia / Promponas, Vasilis J / Ouzounis, Christos A

    PLoS computational biology

    2019  Volume 15, Issue 12, Page(s) e1007532

    MeSH term(s) Computational Biology/education ; Computational Biology/history ; Computational Biology/trends ; Cyprus ; Greece ; History, 20th Century ; History, 21st Century ; Humans ; Publications/statistics & numerical data
    Language English
    Publishing date 2019-12-19
    Publishing country United States
    Document type Historical Article ; Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2193340-6
    ISSN 1553-7358 ; 1553-734X
    ISSN (online) 1553-7358
    ISSN 1553-734X
    DOI 10.1371/journal.pcbi.1007532
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Cyclic mechanical load causes global translational arrest in articular chondrocytes: a process which is partially dependent upon PKR phosphorylation.

    Lomas, Cara / Tang, Xiaodi D / Chanalaris, Anastasios / Saklatvala, Jeremy / Vincent, Tonia L

    European cells & materials

    2011  Volume 22, Page(s) 178–189

    Abstract: The cellular mechanisms by which articular cartilage responds to load are poorly understood, but such responses may involve regulation at the level of protein translation rather than synthesis of mRNA. We investigated the role of translational control in ...

    Abstract The cellular mechanisms by which articular cartilage responds to load are poorly understood, but such responses may involve regulation at the level of protein translation rather than synthesis of mRNA. We investigated the role of translational control in cyclically (0.5 Hz, 0.1 Hz and 0.05 Hz) and statically loaded porcine articular cartilage explants. Messenger RNA was extracted for real time polymerase chain reaction (RT-PCR) and newly synthesised proteins were measured by their incorporation of radiolabelled 35S[methionine/cysteine] or 35SO4. Some medium from loaded and unloaded explants was immunoblotted for type II collagen, CTGF and TIMP3. The pathways that control protein translation were investigated by immunoblotting explant lysates for PKR, PERK (PKR like endoplasmic reticulum kinase), eIF2a (eukaryotic initiation factor 2a), eEFs (eukaryotic elongation factors), and AMP-dependent kinase. Explants were also loaded in the presence of inhibitors of PKR, the fibroblast growth factor (FGF) receptor and PI3 kinase. Cyclic loading caused complete global translational arrest as evidenced by a total suppression of new protein synthesis whilst maintaining mRNA levels. Translational arrest did not occur following static loading and was partly dependent upon the load frequency. There was a rebound increase in protein synthesis when labelling was performed after load had been withdrawn. Phosphorylation of PKR occurred in explants following cyclic load and inhibition of PKR modestly reversed suppression of newly synthesised proteins suggesting that PKR, at least in part, was responsible for loading induced translational arrest. These results show that translational control provides a rapid and potentially important mechanism for controlling the synthetic responses of articular chondrocytes in response to different types of mechanical load.
    MeSH term(s) Animals ; Cartilage, Articular/cytology ; Cartilage, Articular/metabolism ; Cartilage, Articular/physiology ; Cells, Cultured ; Chondrocytes/metabolism ; Chondrocytes/physiology ; Elongation Factor 2 Kinase/biosynthesis ; Extracellular Matrix Proteins/genetics ; Extracellular Matrix Proteins/metabolism ; Intracellular Signaling Peptides and Proteins/metabolism ; Phosphatidylinositol 3-Kinases/antagonists & inhibitors ; Phosphorylation ; Protein Biosynthesis ; RNA, Messenger/biosynthesis ; Real-Time Polymerase Chain Reaction ; Receptors, Fibroblast Growth Factor/antagonists & inhibitors ; Signal Transduction ; Stress, Mechanical ; Swine ; eIF-2 Kinase/biosynthesis ; eIF-2 Kinase/metabolism
    Chemical Substances Extracellular Matrix Proteins ; Intracellular Signaling Peptides and Proteins ; RNA, Messenger ; Receptors, Fibroblast Growth Factor ; Phosphatidylinositol 3-Kinases (EC 2.7.1.-) ; PERK kinase (EC 2.7.11.1) ; eIF-2 Kinase (EC 2.7.11.1) ; Elongation Factor 2 Kinase (EC 2.7.11.20)
    Language English
    Publishing date 2011-09-20
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2046669-9
    ISSN 1473-2262 ; 1473-2262
    ISSN (online) 1473-2262
    ISSN 1473-2262
    DOI 10.22203/ecm.v022a14
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