U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination
    • Showing Current items.

    Mepe matrix extracellular phosphoglycoprotein with ASARM motif (bone) [ Mus musculus (house mouse) ]

    Gene ID: 94111, updated on 9-Dec-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Mepe(-/-) molars exhibited increased thickness of predentin, dentin, and enamel over controls and decreased gene expression of Enam, Bsp, Dmp1, Dspp, and Opn by RT-PCR.

    MEPE Localization in the Craniofacial Complex and Function in Tooth Dentin Formation.
    Gullard A, Gluhak-Heinrich J, Papagerakis S, Sohn P, Unterbrink A, Chen S, MacDougall M., Free PMC Article

    08/13/2016
    An in situ hybridization study of perlecan, DMP1, and MEPE in developing condylar cartilage of the fetal mouse mandible and limb bud cartilage.

    An in situ hybridization study of perlecan, DMP1, and MEPE in developing condylar cartilage of the fetal mouse mandible and limb bud cartilage.
    Fujikawa K, Yokohama-Tamaki T, Morita T, Baba O, Qin C, Shibata S., Free PMC Article

    07/16/2016
    The C-terminal ASARM-motif plays a major role in regulating bone-mass and cancellous structure as mice age

    Age dependent regulation of bone-mass and renal function by the MEPE ASARM-motif.
    Zelenchuk LV, Hedge AM, Rowe PS., Free PMC Article

    05/14/2016
    MEPE is an important regulator of growth plate chondrocyte matrix mineralization through its cleavage to an ASARM peptide.

    MEPE is a novel regulator of growth plate cartilage mineralization.
    Staines KA, Mackenzie NC, Clarkin CE, Zelenchuk L, Rowe PS, MacRae VE, Farquharson C., Free PMC Article

    12/22/2012
    The temporal-spatial specific pattern and unique co-localization of Dspp, Mepe, Mimecan and Versican suggest they play complementary roles during odontogenesis.

    Developmental changes and regional localization of Dspp, Mepe, Mimecan and Versican in postnatal developing mouse teeth.
    Hou C, Liu ZX, Tang KL, Wang MG, Sun J, Wang J, Li S.

    05/19/2012
    Wnt3a stimulates Mepe transcription directly by a canonical Wnt signaling pathway through beta-catenin and Lef-1 and indirectly through the activation of a Bmp-2 autocrine loop.

    Wnt3a stimulates Mepe, matrix extracellular phosphoglycoprotein, expression directly by the activation of the canonical Wnt signaling pathway and indirectly through the stimulation of autocrine Bmp-2 expression.
    Cho YD, Kim WJ, Yoon WJ, Woo KM, Baek JH, Lee G, Kim GS, Ryoo HM.

    04/21/2012
    MEPE might be an important signaling molecule involved in the regulation of osteoblast and osteoclast activity during bone remodeling.

    Inhibition of osteoclastogenesis by mechanically loaded osteocytes: involvement of MEPE.
    Kulkarni RN, Bakker AD, Everts V, Klein-Nulend J., Free PMC Article

    09/3/2011
    the C-terminal fragment of MEPE containing an RGD sequence, cleaved in odontoblasts, appeared to be the active form of MEPE, which may play important roles in dentinogenesis and pulpal homeostasis by keeping the odontoblasts in immature condition.

    Differentiation of odontoblasts is negatively regulated by MEPE via its C-terminal fragment.
    Wang H, Kawashima N, Iwata T, Xu J, Takahashi S, Sugiyama T, Suda H.

    09/13/2010
    MEPE expression is bone cell-specific and induced by the BMP-2 signaling pathway

    Molecular regulation of matrix extracellular phosphoglycoprotein expression by bone morphogenetic protein-2.
    Cho YD, Yoon WJ, Woo KM, Baek JH, Lee G, Cho JY, Ryoo HM., Free PMC Article

    01/21/2010
    MEPE and MEPE-phosphate-regulating gene with homologies to endopeptidases on the X chromosome (MEPE-PHEX) interactions are components to an age-diet-dependent pathway that regulates bone turnover and mineralization and suppresses renal calcification.

    Matrix extracellular phosphoglycoprotein (MEPE) is a new bone renal hormone and vascularization modulator.
    David V, Martin A, Hedge AM, Rowe PS., Free PMC Article

    01/21/2010
    results, showing that pASARM inhibits mineralization provide a mechanism explaining how loss of PHEX activity can lead to extracellular matrix accumulation of ASARM resulting in the osteomalacia of X-linked hypophosphatemia

    MEPE-ASARM peptides control extracellular matrix mineralization by binding to hydroxyapatite: an inhibition regulated by PHEX cleavage of ASARM.
    Addison WN, Nakano Y, Loisel T, Crine P, McKee MD.

    01/21/2010
    degradation of MEPE and DMP-1 and release of ASARM peptides are chiefly responsible for the HYP mineralization defect and changes in osteoblast-osteoclast differentiation.

    Degradation of MEPE, DMP1, and release of SIBLING ASARM-peptides (minhibins): ASARM-peptide(s) are directly responsible for defective mineralization in HYP.
    Martin A, David V, Laurence JS, Schwarz PM, Lafer EM, Hedge AM, Rowe PS., Free PMC Article

    01/21/2010
    MEPE may be involved in the pathogenesis defective mineralization due to Phex deficiency in X-linked hypophosphatemia (XLH) and the Hyp-mouse.

    Inhibition of MEPE cleavage by Phex.
    Guo R, Rowe PS, Liu S, Simpson LG, Xiao ZS, Quarles LD.

    01/21/2010
    Mepe appears to play a role in both long bone regeneration and the latter stages of skeletogenesis.

    Mepe is expressed during skeletal development and regeneration.
    Lu C, Huang S, Miclau T, Helms JA, Colnot C., Free PMC Article

    01/21/2010
    firstprevious page of 1 nextlast