• Login
    View Item 
    •   Home
    • UMass Chan Departments, Programs and Centers
    • Orthopedics and Physical Rehabilitation Publications
    • View Item
    •   Home
    • UMass Chan Departments, Programs and Centers
    • Orthopedics and Physical Rehabilitation Publications
    • View Item
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    Browse

    All of eScholarship@UMassChanCommunitiesPublication DateAuthorsUMass Chan AffiliationsTitlesDocument TypesKeywordsThis CollectionPublication DateAuthorsUMass Chan AffiliationsTitlesDocument TypesKeywords

    My Account

    LoginRegister

    Help

    AboutSubmission GuidelinesData Deposit PolicySearchingAccessibilityTerms of UseWebsite Migration FAQ

    Statistics

    Most Popular ItemsStatistics by CountryMost Popular Authors

    Mechanical regulation of mitogen-activated protein kinase signaling in articular cartilage

    • CSV
    • RefMan
    • EndNote
    • BibTex
    • RefWorks
    Authors
    Fanning, Paul J.
    Emkey, Gregory
    Smith, Robert J.
    Grodzinsky, Alan J.
    Szasz, Nora
    Trippel, Stephen B.
    UMass Chan Affiliations
    Department of Orthopedics and Physical Rehabilitation
    Document Type
    Journal Article
    Publication Date
    2003-09-04
    Keywords
    Animals
    Animals, Newborn
    Biomechanics
    Cartilage, Articular
    Cattle
    Insulin-Like Growth Factor I
    JNK Mitogen-Activated Protein Kinases
    MAP Kinase Signaling System
    Mechanotransduction, Cellular
    Mitogen-Activated Protein Kinase 3
    Mitogen-Activated Protein Kinase Kinases
    Mitogen-Activated Protein Kinases
    Phosphorylation
    Time Factors
    p38 Mitogen-Activated Protein Kinases
    Orthopedics
    Rehabilitation and Therapy
    Show allShow less
    
    Metadata
    Show full item record
    Link to Full Text
    http://dx.doi.org/10.1074/jbc.M305107200
    Abstract
    Articular chondrocytes respond to mechanical forces by alterations in gene expression, proliferative status, and metabolic functions. Little is known concerning the cell signaling systems that receive, transduce, and convey mechanical information to the chondrocyte interior. Here, we show that ex vivo cartilage compression stimulates the phosphorylation of ERK1/2, p38 MAPK, and SAPK/ERK kinase-1 (SEK1) of the JNK pathway. Mechanical compression induced a phased phosphorylation of ERK consisting of a rapid induction of ERK1/2 phosphorylation at 10 min, a rapid decay, and a sustained level of ERK2 phosphorylation that persisted for at least 24 h. Mechanical compression also induced the phosphorylation of p38 MAPK in strictly a transient fashion, with maximal phosphorylation occurring at 10 min. Mechanical compression stimulated SEK1 phosphorylation, with a maximum at the relatively delayed time point of 1 h and with a higher amplitude than ERK1/2 and p38 MAPK phosphorylation. These data demonstrate that mechanical compression alone activates MAPK signaling in intact cartilage. In addition, these data demonstrate distinct temporal patterns of MAPK signaling in response to mechanical loading and to the anabolic insulin-like growth factor-I. Finally, the data indicate that compression coactivates distinct signaling pathways that may help define the nature of mechanotransduction in cartilage.
    Source
    J Biol Chem. 2003 Dec 19;278(51):50940-8. Epub 2003 Sep 2. Link to article on publisher's site
    DOI
    10.1074/jbc.M305107200
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/43069
    PubMed ID
    12952976
    Related Resources
    Link to Article in PubMed
    ae974a485f413a2113503eed53cd6c53
    10.1074/jbc.M305107200
    Scopus Count
    Collections
    UMass Chan Faculty and Researcher Publications
    Orthopedics and Physical Rehabilitation Publications

    entitlement

    Related items

    Showing items related by title, author, creator and subject.

    • Thumbnail

      A mammalian scaffold complex that selectively mediates MAP kinase activation

      Whitmarsh, Alan J.; Cavanagh, Julie; Tournier, Cathy; Yasuda, Jun; Davis, Roger J. (1998-09-11)
      The c-Jun NH2-terminal kinase (JNK) group of mitogen-activated protein (MAP) kinases is activated by the exposure of cells to multiple forms of stress. A putative scaffold protein was identified that interacts with multiple components of the JNK signaling pathway, including the mixed-lineage group of MAP kinase kinase kinases (MLK), the MAP kinase kinase MKK7, and the MAP kinase JNK. This scaffold protein selectively enhanced JNK activation by the MLK signaling pathway. These data establish that a mammalian scaffold protein can mediate activation of a MAP kinase signaling pathway.
    • Thumbnail

      Molecular determinants that mediate selective activation of p38 MAP kinase isoforms

      Enslen, Herve; Brancho, Deborah Marie; Davis, Roger J. (2000-03-16)
      The p38 mitogen-activated protein kinase (MAPK) group is represented by four isoforms in mammals (p38alpha, p38beta2, p38gamma and p38delta). These p38 MAPK isoforms appear to mediate distinct functions in vivo due, in part, to differences in substrate phosphorylation by individual p38 MAPKs and also to selective activation by MAPK kinases (MAPKKs). Here we report the identification of two factors that contribute to the specificity of p38 MAPK activation. One mechanism of specificity is the selective formation of functional complexes between MAPKK and different p38 MAPKs. The formation of these complexes requires the presence of a MAPK docking site in the N-terminus of the MAPKK. The second mechanism that confers signaling specificity is the selective recognition of the activation loop (T-loop) of p38 MAPK isoforms. Together, these processes provide a mechanism that enables the selective activation of p38 MAPK in response to activated MAPKK.
    • Thumbnail

      Selective activation of p38 mitogen-activated protein (MAP) kinase isoforms by the MAP kinase kinases MKK3 and MKK6

      Enslen, Herve; Raingeaud, Joel; Davis, Roger J. (1998-01-27)
      The cellular response to treatment with proinflammatory cytokines or exposure to environmental stress is mediated, in part, by the p38 group of mitogen-activated protein (MAP) kinases. We report the molecular cloning of a novel isoform of p38 MAP kinase, p38 beta 2. This p38 MAP kinase, like p38 alpha, is inhibited by the pyridinyl imidazole drug SB203580. The p38 MAP kinase kinase MKK6 is identified as a common activator of p38 alpha, p38 beta 2, and p38 gamma MAP kinase isoforms, while MKK3 activates only p38 alpha and p38 gamma MAP kinase isoforms. The MKK3 and MKK6 signal transduction pathways are therefore coupled to distinct, but overlapping, groups of p38 MAP kinases.
    DSpace software (copyright © 2002 - 2023)  DuraSpace
    Lamar Soutter Library, UMass Chan Medical School | 55 Lake Avenue North | Worcester, MA 01655 USA
    Quick Guide | escholarship@umassmed.edu
    Open Repository is a service operated by 
    Atmire NV
     

    Export search results

    The export option will allow you to export the current search results of the entered query to a file. Different formats are available for download. To export the items, click on the button corresponding with the preferred download format.

    By default, clicking on the export buttons will result in a download of the allowed maximum amount of items.

    To select a subset of the search results, click "Selective Export" button and make a selection of the items you want to export. The amount of items that can be exported at once is similarly restricted as the full export.

    After making a selection, click one of the export format buttons. The amount of items that will be exported is indicated in the bubble next to export format.