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Immunoseparation of Prion protein‐enriched domains from other detergent‐resistant membrane fractions, isolated from neuronal cells
Author(s) -
Botto Laura,
Masserini Massimo,
Cassetti Arianna,
Palestini Paola
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)01463-7
Subject(s) - lipid raft , immunoprecipitation , fyn , membrane , microbiology and biotechnology , membrane protein , stress granule , chemistry , fluorescence microscope , biochemistry , biology , phosphorylation , fluorescence , messenger rna , proto oncogene tyrosine protein kinase src , gene , physics , translation (biology) , quantum mechanics
The possibility of coexistence of different subtypes of membrane lipid rafts has been investigated in cerebellar granule cells, by submitting detergent‐resistant membrane fractions to immunoprecipitation. Among the proteins and lipids present in detergent‐resistant fractions, almost all Prion protein, GAP43 and PKC were present in the immunoprecipitate obtained with anti‐GAP43 or anti‐Prion protein antibody at 4°C, together with a small fraction of cholesterol and sphingolipids, suggesting that they belong to a distinct subset of membranes. On the contrary, all Fyn and almost all MARCKS remained in the supernatant. Fluorescence microscopy experiments showed that Fyn and Prion protein were mostly not colocalized within a single neuron. Our results suggest that granule cells membranes contains different subtypes of detergent‐resistant fractions, possibly deriving from different lipid rafts.