Francesca D'Avila and Cristina Tringali contributed equally to this work.
Identification of lysosomal sialidase NEU1 and plasma membrane sialidase NEU3 in human erythrocytes†
Article first published online: 14 NOV 2012
Copyright © 2012 Wiley Periodicals, Inc.
Journal of Cellular Biochemistry
Volume 114, Issue 1, pages 204–211, January 2013
How to Cite
D'Avila, F., Tringali, C., Papini, N., Anastasia, L., Croci, G., Massaccesi, L., Monti, E., Tettamanti, G. and Venerando, B. (2013), Identification of lysosomal sialidase NEU1 and plasma membrane sialidase NEU3 in human erythrocytes. J. Cell. Biochem., 114: 204–211. doi: 10.1002/jcb.24355
- Issue published online: 14 NOV 2012
- Article first published online: 14 NOV 2012
- Accepted manuscript online: 17 AUG 2012 08:30AM EST
- Manuscript Accepted: 7 AUG 2012
- Manuscript Received: 10 MAY 2012
- MIUR. Grant Number: PRIN 2008
- Fondazione Cariplo. Grant Number: 2010-0700
- PERIPHERAL PROTEINS
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.