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    Adam10 ADAM metallopeptidase domain 10 [ Rattus norvegicus (Norway rat) ]

    Gene ID: 29650, updated on 9-Dec-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Extracellular-Signal-Regulated Kinase Inhibition Switches APP Processing from beta- to alpha-Secretase under Oxidative Stress: Modulation of ADAM10 by SIRT1/NF-kappaB Signaling.

    Extracellular-Signal-Regulated Kinase Inhibition Switches APP Processing from β- to α-Secretase under Oxidative Stress: Modulation of ADAM10 by SIRT1/NF-κB Signaling.
    Thonda S, Puttapaka SN, Kona SV, Kalivendi SV.

    12/4/2021
    Abeta1-42 oligomers trigger an aberrant plasticity mechanism according to which Abeta1-42 oligomers can downregulate Abeta generation through the modulation of ADAM10 synaptic availability.

    Amyloid-β Oligomers Regulate ADAM10 Synaptic Localization Through Aberrant Plasticity Phenomena.
    Marcello E, Musardo S, Vandermeulen L, Pelucchi S, Gardoni F, Santo N, Antonucci F, Di Luca M., Free PMC Article

    02/1/2020
    This study demonstrates the involvement of ADAM10 and PI3K/Akt signaling in mediating RLX-induced Notch-1 activation.

    Relaxin induces up-regulation of ADAM10 metalloprotease in RXFP1-expressing cells by PI3K/AKT signaling.
    Boccalini G, Sassoli C, Bani D, Nistri S.

    04/27/2019
    our results indicate a positive role of PLD1 in synaptogenesis by inhibiting the ADAM10 mediated N-cadherin cleavage and provide new therapeutic clues for some neurological diseases.

    PLD1 promotes dendritic spine development by inhibiting ADAM10-mediated N-cadherin cleavage.
    Luo LD, Li G, Wang Y., Free PMC Article

    02/2/2019
    In this study, we demonstrated that ADAM10 plays an important role in PAX2-induced EMT in the renal tubular epithelia

    PAX2 may induce ADAM10 expression in renal tubular epithelial cells and contribute to epithelial-to-mesenchymal transition.
    Hou L, Du Y, Zhao C, Wu Y., Free PMC Article

    12/22/2018
    Our findings indicate that neuron-derived ADAM10 production stimulates peripheral nerve injury-induced neuropathic pain by cleaving E-cadherin in satellite glial cells.

    Neuron-Derived ADAM10 Production Stimulates Peripheral Nerve Injury-Induced Neuropathic Pain by Cleavage of E-Cadherin in Satellite Glial Cells.
    Li J, Ouyang Q, Chen CW, Chen QB, Li XN, Xiang ZH, Yuan HB.

    06/2/2018
    These results demonstrated the localization of VDR on the neuronal plasma membrane and the co-localization of VDR and APP or ADAM10 or Nicastrin and limited co-localization of VDR and PS1.

    Vitamin D receptor is present on the neuronal plasma membrane and is co-localized with amyloid precursor protein, ADAM10 or Nicastrin.
    Dursun E, Gezen-Ak D., Free PMC Article

    12/23/2017
    TGF-beta stimulation of renal cells results in a significant up-regulation of Adams 10, 17, 12, and 19

    Canonical transforming growth factor-β signaling regulates disintegrin metalloprotease expression in experimental renal fibrosis via miR-29.
    Ramdas V, McBride M, Denby L, Baker AH., Free PMC Article

    07/5/2014
    Time- and injury-dependent expression of MT5-MMP, ADAM-10, and N-cadherin are confirmed during reactive synaptogenesis.

    MT5-MMP, ADAM-10, and N-cadherin act in concert to facilitate synapse reorganization after traumatic brain injury.
    Warren KM, Reeves TM, Phillips LL., Free PMC Article

    05/25/2013
    PACAP38 is involved in the modulation of dendritic spine morphology in hippocampal neurons; the ADAM10-N-cadherin signaling pathway plays a crucial role in this modification of the excitatory glutamatergic synapse.

    The neuropeptide PACAP38 induces dendritic spine remodeling through ADAM10-N-cadherin signaling pathway.
    Gardoni F, Saraceno C, Malinverno M, Marcello E, Verpelli C, Sala C, Di Luca M.

    02/16/2013
    These results strongly suggest that TACE/ADAM17 participates in in vivo apoptosis of male germ cells induced by DNA damage.

    Involvement of TACE/ADAM17 and ADAM10 in etoposide-induced apoptosis of germ cells in rat spermatogenesis.
    Lizama C, Rojas-Benitez D, Antonelli M, Ludwig A, Moreno RD.

    02/4/2012
    alpha- and gamma-secretase processing of nectin-1 is a Ca(2+)/calmodulin-regulated event that occurs under conditions of activity-dependent synaptic plasticity and ADAM10 and gamma-secretase are responsible for these cleavage events.

    Activity-dependent alpha-cleavage of nectin-1 is mediated by a disintegrin and metalloprotease 10 (ADAM10).
    Kim J, Lilliehook C, Dudak A, Prox J, Saftig P, Federoff HJ, Lim ST., Free PMC Article

    08/23/2010
    Elevation of ADAM10 is associated with thoracic aortic aneurysm.

    Elevation of ADAM10, ADAM17, MMP-2 and MMP-9 expression with media degeneration features CaCl2-induced thoracic aortic aneurysm in a rat model.
    Geng L, Wang W, Chen Y, Cao J, Lu L, Chen Q, He R, Shen W.

    08/9/2010
    during the process of myelin formation, ADAM10 is highly upregulated and appears to be critically involved in axonal outgrowth that is a requirement for myelination in the peripheral nerve.

    Involvement of ADAM10 in axonal outgrowth and myelination of the peripheral nerve.
    Jangouk P, Dehmel T, Meyer Zu Hörste G, Ludwig A, Lehmann HC, Kieseier BC.

    01/21/2010
    ADAM10 expression was induced in dentate gyrus of hippocampus. The spatiotemporal expression of ADAM10 suggests that its regulation after the KA-induced status epilepticus could be related to neuroprotection.

    ADAM9, ADAM10, and ADAM15 mRNA levels in the rat brain after kainic acid-induced status epilepticus.
    Ortiz RM, Kärkkäinen I, Huovila AP, Honkaniemi J.

    01/21/2010
    experiments establish amyloid precursor protein, nicastrin, and presenilin-1 as resident lysosomal membrane proteins and indicate that gamma-secretase is a lysosomal protease

    Presenilin-1, nicastrin, amyloid precursor protein, and gamma-secretase activity are co-localized in the lysosomal membrane.
    Pasternak SH, Bagshaw RD, Guiral M, Zhang S, Ackerley CA, Pak BJ, Callahan JW, Mahuran DJ.

    01/21/2010
    gamma-secretase activation and ErbB4 intracellular domain nuclear translocation are required for oligodendrocyte maturation induced by neuregulin

    Implication of gamma-secretase in neuregulin-induced maturation of oligodendrocytes.
    Lai C, Feng L.

    01/21/2010
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