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- W2337807589 abstract "3695 The inappropriate activation or overexpression of members of the epidermal growth factor family of receptors (ErbB) is associated with the development and severity of many cancers, particularly breast cancer. The extracellular domain of ErbB2 is released by proteolytic cleavage in both breast cancer tissue culture cell lines and in patients with metastatic breast cancer where its serum levels correlate with increased metastasis and decreased survival. However, the enzyme responsible for ErbB2 ectodomain shedding is unknown. To better understand the role of ErbB2 shedding and its role in regulating ErbB signaling, we have used a tumor xenograft model system derived from MMTV-ErbB2 transgenic animals. Using a bioinformatics and biochemical approach, we have identified a candidate ErbB2 sheddase, MT2-MMP, a member of the membrane-associated matrix metalloprotease family. Purified MT2-MMP cleaves ErbB2 near the juxtamembrane domain in vitro and a catalytically dead mutant of MT2-MMP co-immunoprecipitates ErbB2 from transfected cell lysates. However, MT1-MMP, a structurally related metalloprotease, does not cleave or interact with ErbB2. Downregulating MT2-MMP protein levels by RNA interference reduces ErbB2 ectodomain shedding in cultured breast cancer cell lines and reduces cell growth. Overexpression of MT2-MMP, or a soluble form of the protease, augments ErbB2 receptor shedding. The product of receptor shedding, a truncated form of the ErbB2 receptor, is constitutively phosphorylated and heterodimerizes with EGFR and ErbB3 in a ligand-dependent manner. These observations suggest a novel role of MT2-MMP in regulating ErbB2 receptor signaling." @default.
- W2337807589 created "2016-06-24" @default.
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- W2337807589 date "2005-05-01" @default.
- W2337807589 modified "2023-10-03" @default.
- W2337807589 title "ErbB2/Her2 ectodomain shedding is regulated by a membrane-associated metalloprotease" @default.
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