• Open Access

Identification of Annexin A1 interacting proteins in chronic myeloid leukemia KCL22 cells

Authors

  • Irene Colavita,

    1. CEINGE-Biotecnologie Avanzate scarl, Napoli, Italy
    2. Fondazione SDN-IRCCS, Napoli, Italy
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  • Nicola Esposito,

    1. CEINGE-Biotecnologie Avanzate scarl, Napoli, Italy
    2. Dipartimento di Medicina Molecolare e Biotecnologie Mediche, Università di Napoli “Federico II”, Napoli, Italy
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  • Concetta Quintarelli,

    1. CEINGE-Biotecnologie Avanzate scarl, Napoli, Italy
    2. Dipartimento di Medicina Molecolare e Biotecnologie Mediche, Università di Napoli “Federico II”, Napoli, Italy
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  • Ersilia Nigro,

    1. CEINGE-Biotecnologie Avanzate scarl, Napoli, Italy
    2. Fondazione SDN-IRCCS, Napoli, Italy
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  • Fabrizio Pane,

    1. CEINGE-Biotecnologie Avanzate scarl, Napoli, Italy
    2. Dipartimento di Medicina Molecolare e Biotecnologie Mediche, Università di Napoli “Federico II”, Napoli, Italy
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  • Margherita Ruoppolo,

    1. CEINGE-Biotecnologie Avanzate scarl, Napoli, Italy
    2. Dipartimento di Medicina Molecolare e Biotecnologie Mediche, Università di Napoli “Federico II”, Napoli, Italy
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  • Francesco Salvatore

    Corresponding author
    1. Fondazione SDN-IRCCS, Napoli, Italy
    • CEINGE-Biotecnologie Avanzate scarl, Napoli, Italy
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Correspondence: Professor Francesco Salvatore, CEINGE–Biotecnologie Avanzate Scarl c/o Università di Napoli “Federico II,” Via S. Pansini 5, 80131 Naples, Italy

E-mail: salvator@unina.it

Fax: +0039-081-7463650

Abstract

In the present study, we used a functional proteomic approach to identify Annexin A1 (Anxa1) interacting proteins in the Philadelphia-positive KCL22 cell line. We focused on Anxa1 because it is one of the major proteins upregulated in imatinib-sensitive KCL22S cells versus imatinib-resistant KCL22R. Our proteomic strategy revealed 21 interactors. Bioinformatic analysis showed that most of these proteins are involved in cell death processes. Among the proteins identified, we studied the interaction of Anxa1 with two phosphatases, Shp1 and Shp2, which were recently identified as biomarkers of imatinib sensitivity in patients affected by chronic myeloid leukemia. Our data open new perspectives in the search for annexin-mediated signaling pathways and may shed light on mechanisms of resistance to imatinib that are unrelated to Bcr-Abl activity. All mass spectrometry data have been deposited in the ProteomeXchange with identifier PXD000030.

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