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

Francesca D'Avila, Cristina Tringali, Nadia Papini, Luigi Anastasia, Gianluigi Croci, Luca Massaccesi, Eugenio Monti, Guido Tettamanti, Bruno Venerando

Research output: Contribution to journalArticlepeer-review


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.

Original languageEnglish
Pages (from-to)204-211
Number of pages8
JournalJournal of Cellular Biochemistry
Issue number1
Publication statusPublished - Jan 2013



ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology


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