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Journal of Cellular Biochemistry

Identification of lysosomal sialidase NEU1 and plasma membrane sialidase NEU3 in human erythrocytes

Authors

  • Francesca D'Avila,

    1. Department of Medical Chemistry, Biochemistry and Biotechnology, University of Milan, F.lli Cervi 93, Segrate, Milan 20090, Italy
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  • Cristina Tringali,

    1. Department of Medical Chemistry, Biochemistry and Biotechnology, University of Milan, F.lli Cervi 93, Segrate, Milan 20090, Italy
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  • Nadia Papini,

    1. Department of Medical Chemistry, Biochemistry and Biotechnology, University of Milan, F.lli Cervi 93, Segrate, Milan 20090, Italy
    2. Laboratory of Stem Cells for Tissue Engineering, IRCCS Policlinico San Donato, San Donato Milanese 20097, Italy
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  • Luigi Anastasia,

    1. Department of Medical Chemistry, Biochemistry and Biotechnology, University of Milan, F.lli Cervi 93, Segrate, Milan 20090, Italy
    2. Laboratory of Stem Cells for Tissue Engineering, IRCCS Policlinico San Donato, San Donato Milanese 20097, Italy
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  • Gianluigi Croci,

    1. Department of Medical Chemistry, Biochemistry and Biotechnology, University of Milan, F.lli Cervi 93, Segrate, Milan 20090, Italy
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  • Luca Massaccesi,

    1. Department of Medical Chemistry, Biochemistry and Biotechnology, University of Milan, F.lli Cervi 93, Segrate, Milan 20090, Italy
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  • Eugenio Monti,

    1. Department of Biomedical Science and Biotechnology, University of Brescia, viale Europa 11, Brescia 25123, Italy
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  • Guido Tettamanti,

    1. Laboratory of Stem Cells for Tissue Engineering, IRCCS Policlinico San Donato, San Donato Milanese 20097, Italy
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  • Bruno Venerando

    Corresponding author
    1. Department of Medical Chemistry, Biochemistry and Biotechnology, University of Milan, F.lli Cervi 93, Segrate, Milan 20090, Italy
    2. Laboratory of Stem Cells for Tissue Engineering, IRCCS Policlinico San Donato, San Donato Milanese 20097, Italy
    • Department of Medical Chemistry, Biochemistry and Biotechnology, University of Milan, via F.lli Cervi 93, Segrate, Milan 20090, Italy.
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  • Francesca D'Avila and Cristina Tringali contributed equally to this work.

Abstract

The sialylation level of molecules, sialoglycoproteins and gangliosides, protruding from plasma membranes regulates multiple facets of erythrocyte function, from interaction with endothelium to cell lifespan. Our results demonstrate that: (a) Both sialidases NEU1 and NEU3 are present on erythrocyte plasma membrane; (b) NEU1 is kept on the plasma membrane in absence of the protective protein/cathepsin A (PPCA); (c) NEU1 and NEU3 are retained on the plasma membrane, as peripheral proteins, associated to the external leaflet and released by alkaline treatments; (d) NEU1 and NEU3 are segregated in Triton X-100 detergent-resistant membrane domains (DRMs); (e) NEU3 shows activity also at neutral pH; and (f) NEU1 and NEU3 are progressively lost during erythrocyte life. Interestingly, sialidase activity released from erythrocyte membranes after an alkaline treatment preserves its functionality and recognizes sialoglycoproteins and gangliosides. On the other hand, the weak anchorage of sialidases to the plasma membrane and their loss during erythrocyte life could be a tool to preserve the cellular sialic acid content in order to avoid the early ageing of erythrocyte and processes of cell aggregation in the capillaries. J. Cell. Biochem. 114: 204–211, 2012. © 2012 Wiley Periodicals, Inc.

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