Role of galectin-3 in prion infections of the CNS
- Project Neurodegenerative Diseases, Robert-Koch-Institut, Nordufer 20, 13353 Berlin (Germany)
- Center for Biological Safety 4, Robert-Koch-Institut, Nordufer 20, 13353 Berlin (Germany)
- Department of Dermatology, School of Medicine, University of California-Davis, Sacramento, CA 95817 (United States)
Galectin-3 is a multi-functional protein and participates in mediating inflammatory reactions. The pronounced overexpression of galectin-3 in prion-infected brain tissue prompted us to study the role of this protein in a murine prion model. Immunofluorescence double-labelling identified microglia as the major cell type expressing galectin-3. Ablation of galectin-3 did not affect PrP{sup Sc}-deposition and development of gliosis. However, galectin-3{sup -/-}-mice showed prolonged survival times upon intracerebral and peripheral scrapie infections. Moreover, protein levels of the lysosomal activation marker LAMP-2 were markedly reduced in prion-infected galectin-3{sup -/-}-mice suggesting a role of galectin-3 in regulation of lysosomal functions. Lower mRNA levels of Beclin-1 and Atg5 in prion-infected wild-type and galectin-3{sup -/-}-mice indicated an impairment of autophagy although autophagosome formation was unchanged. The results point towards a detrimental role of galectin-3 in prion infections of the CNS and suggest that endo-/lysosomal dysfunction in combination with reduced autophagy may contribute to disease development.
- OSTI ID:
- 20991472
- Journal Information:
- Biochemical and Biophysical Research Communications, Vol. 359, Issue 3; Other Information: DOI: 10.1016/j.bbrc.2007.05.163; PII: S0006-291X(07)01140-0; Copyright (c) 2007 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
- Country of Publication:
- United States
- Language:
- English
Similar Records
An assessment of the long-term persistence of prion infectivity in aquatic environments
Reduction of prion infectivity in packed red blood cells