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ADAM Protein

The Experts below are selected from a list of 105 Experts worldwide ranked by ideXlab platform

Iva Greenwald – 1st expert on this subject based on the ideXlab platform

  • Evidence for functional redundancy between C. elegans ADAM Proteins SUP-17/Kuzbanian and ADM-4/TACE
    Developmental Biology, 2005
    Co-Authors: Sophie Jarriault, Iva Greenwald

    Abstract:

    Abstract The ectodomain of LIN-12/Notch Proteins is cleaved and shed upon ligand binding. In Caenorhabditis elegans, genetic evidence has implicated SUP-17, the ortholog of Drosophila Kuzbanian and mammalian ADAM10, as the protease that mediates this event. In mammals, however, biochemical evidence has implicated TACE, a different ADAM Protein. We have investigated potential functional redundancy of sup-17 and the C. elegans ortholog of TACE, adm-4, by exploring their roles in cell fate decisions mediated by lin-12/Notch genes. We found that reduced adm-4 activity, like reduced sup-17 activity, suppresses an allele of glp-1 that encodes a constitutively active receptor. Furthermore, concomitant reduction of adm-4 and sup-17 activity causes the production of two anchor cells in the hermaphrodite gonad, instead of one—a phenotype associated with loss of lin-12 activity. Concomitant reduction of both sup-17 and adm-4 activity in hermaphrodites results in highly penetrant synthetic sterility, which appears to reflect a defect in the spermatheca. Expression of a truncated form of LIN-12 that mimics the product of ectodomain shedding rescues this fertility defect, suggesting that sup-17 and adm-4 may mediate ectodomain shedding of LIN-12 and/or GLP-1. Our results are consistent with the possibility that sup-17 and adm-4 are functionally redundant for at least a subset of LIN-12/Notch-mediated decisions in C. elegans.

  • sup 17 a caenorhabditis elegans ADAM Protein related to drosophila kuzbanian and its role in lin 12 notch signalling
    Development, 1997
    Co-Authors: Mark M Metzstein, Iva Greenwald

    Abstract:

    LIN-12/NOTCH Proteins mediate cell-cell interactions that specify cell fates. Previous work suggested that sup-17 facilitates lin-12 signalling in Caenorhabditis elegans. Here, we show that sup-17 encodes a member of the ADAM family of metalloproteases. SUP-17 is highly similar to Drosophila KUZBANIAN, which functions in Drosophila neurogenesis, and the vertebrate ADAM10 Protein. Furthermore, we show by genetic analysis that the extracellular domain of LIN-12 appears to be necessary for sup-17 to facilitate lin-12 signalling and that sup-17 does not act downstream of lin-12. Finally, we show by cell ablation experiments that sup-17 can act cell autonomously to facilitate lin-12 activity. We discuss the implications of our observations for LIN-12/NOTCH signalling and how our results complement and extend results obtained from genetic analysis of kuz in Drosophila.

  • SUP-17, a Caenorhabditis elegans ADAM Protein related to Drosophila KUZBANIAN, and its role in LIN-12/NOTCH signalling
    Development, 1997
    Co-Authors: Mark M Metzstein, Iva Greenwald

    Abstract:

    LIN-12/NOTCH Proteins mediate cell-cell interactions that specify cell fates. Previous work suggested that sup-17 facilitates lin-12 signalling in Caenorhabditis elegans. Here, we show that sup-17 encodes a member of the ADAM family of metalloproteases. SUP-17 is highly similar to Drosophila KUZBANIAN, which functions in Drosophila neurogenesis, and the vertebrate ADAM10 Protein. Furthermore, we show by genetic analysis that the extracellular domain of LIN-12 appears to be necessary for sup-17 to facilitate lin-12 signalling and that sup-17 does not act downstream of lin-12. Finally, we show by cell ablation experiments that sup-17 can act cell autonomously to facilitate lin-12 activity. We discuss the implications of our observations for LIN-12/NOTCH signalling and how our results complement and extend results obtained from genetic analysis of kuz in Drosophila.

Mark M Metzstein – 2nd expert on this subject based on the ideXlab platform

  • sup 17 a caenorhabditis elegans ADAM Protein related to drosophila kuzbanian and its role in lin 12 notch signalling
    Development, 1997
    Co-Authors: Mark M Metzstein, Iva Greenwald

    Abstract:

    LIN-12/NOTCH Proteins mediate cell-cell interactions that specify cell fates. Previous work suggested that sup-17 facilitates lin-12 signalling in Caenorhabditis elegans. Here, we show that sup-17 encodes a member of the ADAM family of metalloproteases. SUP-17 is highly similar to Drosophila KUZBANIAN, which functions in Drosophila neurogenesis, and the vertebrate ADAM10 Protein. Furthermore, we show by genetic analysis that the extracellular domain of LIN-12 appears to be necessary for sup-17 to facilitate lin-12 signalling and that sup-17 does not act downstream of lin-12. Finally, we show by cell ablation experiments that sup-17 can act cell autonomously to facilitate lin-12 activity. We discuss the implications of our observations for LIN-12/NOTCH signalling and how our results complement and extend results obtained from genetic analysis of kuz in Drosophila.

  • SUP-17, a Caenorhabditis elegans ADAM Protein related to Drosophila KUZBANIAN, and its role in LIN-12/NOTCH signalling
    Development, 1997
    Co-Authors: Mark M Metzstein, Iva Greenwald

    Abstract:

    LIN-12/NOTCH Proteins mediate cell-cell interactions that specify cell fates. Previous work suggested that sup-17 facilitates lin-12 signalling in Caenorhabditis elegans. Here, we show that sup-17 encodes a member of the ADAM family of metalloproteases. SUP-17 is highly similar to Drosophila KUZBANIAN, which functions in Drosophila neurogenesis, and the vertebrate ADAM10 Protein. Furthermore, we show by genetic analysis that the extracellular domain of LIN-12 appears to be necessary for sup-17 to facilitate lin-12 signalling and that sup-17 does not act downstream of lin-12. Finally, we show by cell ablation experiments that sup-17 can act cell autonomously to facilitate lin-12 activity. We discuss the implications of our observations for LIN-12/NOTCH signalling and how our results complement and extend results obtained from genetic analysis of kuz in Drosophila.

Nicole S Sampson – 3rd expert on this subject based on the ideXlab platform

  • polymeric ADAM Protein mimics interrogate mammalian sperm egg binding
    ChemBioChem, 2009
    Co-Authors: Nicole S Sampson

    Abstract:

    : The sperm Proteins ADAM2 and ADAM3, members of the ADAM family of Proteins, have been implicated in mammalian sperm-egg binding. However, elucidating their roles is complex because of the interdependence of ADAM Protein expression in the testis. Hence, multivalent probes containing the three-amino acid binding sequence of ADAM2, glutamate-cysteine-aspartate (ECD), and ADAM3, glutamine-cysteine-aspartate (QCD), were designed, synthesized, and tested to investigate gamete interactions. In this work, ECD polymer mimics were synthesized by ring-opening metathesis polymerization with a faster initiating ruthenium catalyst than previously used. Polymers containing 100 copies of the ECD peptide mimic were found to be the best inhibitors of fertilization. The multivalent QCD polymers were also tested as inhibitors of fertilization. The structure-activity profile was the same as ECD polymers, but the overall potency was lower. Both ECD and QCD polymers require the presence of beta(1) integrin to inhibit fertilization. Next, triblock ABA and ABC copolymers containing both ECD and QCD ligands were synthesized with 96 monomer spacers as their B blocks. Although these polymers had lower densities of ECD and QCD peptides, their potencies correlated with the potencies of their corresponding homopolymers. In addition, no synergy between ECD and QCD mimics was observed. All the data suggest that QCD and ECD bind to the same complex of Proteins that includes beta(1) integrin.

  • A Facile Synthetic Method to Prepare Fluorescently Labeled ROMP Polymers
    Organic Letters, 2004
    Co-Authors: Kenny S. Roberts, Nicole S Sampson

    Abstract:

    To probe the activities of sperm ADAM Protein (fertilinβ), we devised a general synthetic strategy to generate fluorescently labeled fertilinβ oligopeptide polymers. Immunofluorescence studies with these polymers demonstrated that fertilinβ polymers bind specifically to a Protein receptor on the mouse egg plasma membrane.