NR AHYG
AU Martins,V.R.; Graner,E.; Garcia-Abreu,J.; de Souza,S.J.; Mercadante,A.F.; Veiga,S.S.; Zanata,S.M.; Neto,V.M.; Brentani,R.R.
TI Complementary hydropathy identifies a cellular prion protein receptor
QU Nature Medicine 1997 Dec; 3(12): 1376-82
KI Nat Med. 1997 Dec;3(12):1322. PMID: 9396598
PT journal article
AB Prions, the etiological agents for infectious degenerative encephalopathies, act by entering the cell and inducing conformational changes in PrPc (a normal cell membrane sialoglycoprotein), which result in cell death. A specific cell-surface receptor to mediate PrPc and prion endocytosis has been predicted. Complementary hydropathy let us generate a hypothetical peptide mimicking the receptor binding site. Antibodies raised against this peptide stain the surface of mouse neurons and recognize a 66-kDa membrane protein that binds PrPc both in vitro and in vivo. Furthermore, both the complementary prion peptide and antiserum against it inhibit the toxicity of a prion-derived peptide toward neuronal cells in culture. Such reagents might therefore have therapeutic applications.
MH Amino Acid Sequence; Animal; Antibodies/immunology; Cells, Cultured; Genetic Techniques; Human; Mice; Molecular Sequence Data; Neurons/cytology; PrPc Proteins/immunology/*metabolism/toxicity; Rats; Receptors, Cell Surface/*analysis/chemistry/*metabolism; Support, Non-U.S. Gov't; Tumor Cells, Cultured
AD Fundacao Antonio Prudente, Sao Paulo, Brazil.
SP englisch
PO USA