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Peptide-based Identification of Functional Motifs and their Binding Partners
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Antibodies binding the ADAM10 substrate recognition domain inhibit Eph function.

Lakmali Atapattu1, Nayanendu Saha, Carmen Llerena

  • 1Department of Biochemistry and Molecular Biology, Monash University, Victoria 3800, Australia.

Journal of Cell Science
|October 31, 2012
PubMed
Summary
This summary is machine-generated.

Researchers developed antibodies targeting the ADAM10 enzyme

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Medicine

Background:

  • ADAM10 is a metalloprotease that cleaves cell surface proteins, including ephrins, which are ligands for Eph receptors.
  • Ephrin cleavage by ADAM10 regulates cell-cell adhesion and segregation, processes critical in development and implicated in cancer metastasis.
  • Previous work identified a substrate-binding pocket in ADAM10 that interacts with EphA/ephrin-A complexes.

Purpose of the Study:

  • To generate monoclonal antibodies targeting the ADAM10 substrate-recognition pocket.
  • To investigate the functional consequences of inhibiting ephrin cleavage by ADAM10.
  • To assess the therapeutic potential of these antibodies in modulating Eph/ephrin signaling.

Main Methods:

  • Generation of monoclonal antibodies against the ADAM10 substrate-binding region.
  • Assays to measure ephrin cleavage.
  • Functional assays assessing Eph/ephrin-mediated cell adhesion, segregation, receptor internalization, and phosphorylation.

Main Results:

  • Monoclonal antibodies were generated that specifically recognize the ADAM10 substrate-recognition pocket.
  • These antibodies effectively inhibited ADAM10-mediated ephrin cleavage.
  • Antibodies blocked Eph/ephrin-mediated cell functions, including receptor internalization, phosphorylation, and cell segregation.

Conclusions:

  • ADAM10 plays a crucial role in cell-cell interactions mediated by both A- and B-type Eph receptors.
  • Antibodies targeting the ADAM10 substrate-recognition pocket are promising therapeutic agents.
  • These antibodies inhibit ephrin cleavage and may target other ADAM10 substrates, offering a novel therapeutic strategy.