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Activation of p38 and Smads mediates BMP-2 effects on human trabecular bone-derived osteoblasts.

Activation of p38 and Smads mediates BMP-2 effects on human trabecular bone-derived osteoblasts. Research Abstract Details 

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  • Activation of p38 and Smads mediates BMP-2 effects on human trabecular bone-derived osteoblasts. Abstract Text:

    ulrich Ulrich ,richard tuliRichard Tuli,reza seghatoleslamiReza Seghatoleslami,michael howardMichael Howard,asit shahAsit Shah,david j hallDavid J Hall,noreen j hickokNoreen J Hickok,rocky s tuanRocky S Tuan,

    The bone morphogenetic proteins (BMPs) are potent osteoinductive factors that accelerate osteoblast maturation, accompanied by increased cell-substrate adhesion. BMP-2 treatment of osteoblastic cells increases phosphorylation of the cytoplasmic BMP-2 signaling molecules, Smad1 and Smad5. We have previously reported that BMP-2 treatment increase cytoskeletal organization of human trabecular bone-derived osteoblast-like cells (osteoblasts), which is also accompanied by an activation of the focal adhesion kinase p125(FAK). We report here that activation of p125(FAK) occurs with the same kinetics as the phosphorylation of Smad1, suggesting that BMP-2 initiates cross-talk between Smad signaling and the adhesion-mediated signaling pathway. As an adjunct to these effects, we examined activation of mitogen-activated protein (MAP) kinase family members in response to focal adhesion contact formation. Although phosphorylated forms of all three kinases were apparent, only SAPK2alpha/p38 (p38) was activated in response to BMP-2 treatment. Inhibition of p38 kinase activity suppressed BMP-2 induced Smad1 phosphorylation, as well as its translocation to the nucleus, suggesting the integration of p38 activation with Smad1 signaling. Finally, inhibition of p38 in osteoblasts also led to the complete abrogation of BMP-2 induced osteocalcin gene expression and matrix mineralization. These findings suggest that BMP-2 must activate p38 in order to mediate osteogenic differentiation and maturation.

    Activation of p38 and Smads mediates BMP-2 effects on human trabecular bone-derived osteoblasts. Publishing Authors By Initials

    u U ,r tuliR Tuli,r seghatoleslamiR Seghatoleslami,m howardM Howard,a shahA Shah,dj hallDJ Hall,nj hickokNJ Hickok,rs tuanRS Tuan,

    For similar enzymes and coenzymes: enzymes: transferases: phosphotransferases: phosphotransferases (alcohol group acceptor): protein kinases: protein-serine-threonine kinases: mitogen-activated protein kinases: p38 mitogen-activated protein kinases research abstracts see: enzymes and coenzymes: enzymes: transferases: phosphotransferases: phosphotransferases (alcohol group acceptor): protein kinases: protein-serine-threonine kinases: mitogen-activated protein kinases: p38 mitogen-activated protein kinases research

    PUBMED ID PMID:

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    Activation of p38 and Smads mediates BMP-2 effects on human trabecular bone-derived osteoblasts. Journal Published:

    PUBLICATION TYPE: Research Support, U.S. Gov't,

    Journal: Experimental cell research

    VOLUME: 291

    Page Numbers: 201-11

    Journal Abbreviation: Exp. Cell Res.

    ISSN: 0014-4827

    DAY: 15

    MONTH: Nov

    YEAR: 2003

    Activation of p38 and Smads mediates BMP-2 effects on human trabecular bone-derived osteoblasts. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 373226

    Activation of p38 and Smads mediates BMP-2 effects on human trabecular bone-derived osteoblasts. Keywords Mesh Terms:

    KEYWORDS: p38 Mitogen-Activated Protein Kinases

    MESH TERMS: metabolism

    Chemical & Substance for Abstract: Activation of p38 and Smads mediates BMP-2 effects on human trabecular bone-derived osteoblasts. Information

    Substance Name: p38 Mitogen-Activated Protein Kinases

    Registry Number: EC 2.7.1.37

    Grant and Affiliation Information for Activation of p38 and Smads mediates BMP-2 effects on human trabecular bone-derived osteoblasts.

    AFFILIATION: Department of Orthopaedic Surgery, Thomas Jefferson University, Philadelphia, PA 19107, USA.

    Country: United States

    United States Research PublicationUnited States Research Publication

    AGENCY: United States NIDCR

    GRANT: DE 16865

    ACRONYM: DE

    MEDLINETA: Exp Cell Res

    REFSOURCE:

    DATABASENAME:

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