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Titolo:
Differential assembly of rat purinergic P2X(7) receptor in immune cells ofthe brain and periphery
Autore:
Kim, M; Spelta, V; Sim, J; North, RA; Surprenant, A;
Indirizzi:
Univ Sheffield, Inst Mol Physiol, Sheffield S10 2TN, S Yorkshire, England Univ Sheffield Sheffield S Yorkshire England S10 2TN S Yorkshire, England
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 26, volume: 276, anno: 2001,
pagine: 23262 - 23267
SICI:
0021-9258(20010629)276:26<23262:DAORPP>2.0.ZU;2-0
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN B-LYMPHOCYTES; GATED ION-CHANNEL; MICROGLIAL CELLS; XENOPUS OOCYTES; PURINOCEPTORS; EXPRESSION; SUBUNITS; RELEASE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
34
Recensione:
Indirizzi per estratti:
Indirizzo: Surprenant, A Univ Sheffield, Inst Mol Physiol, Alfred Denny Bldg,Western Bank, Sheffield S10 2TN, S Yorkshire, England Univ Sheffield Alfred Denny Bldg,Western Bank Sheffield S Yorkshire England S10 2TN
Citazione:
M. Kim et al., "Differential assembly of rat purinergic P2X(7) receptor in immune cells ofthe brain and periphery", J BIOL CHEM, 276(26), 2001, pp. 23262-23267

Abstract

ATP-gated P2X(7) purinoceptors are found in most immune cells of the periphery and the brain where their activation leads to multiple downstream events such as cell permeabilization, apoptosis, and/or cytokine release. P2X(7) receptors do not form heteromeric receptors with any of the other six P2Xsubunits, and it is not known what type of homomeric assemblies the P2X(7)subunit makes. We constructed and purified an ectodomain protein of the rat P2X(7) receptor (amino acids 60-323) and used this to generate a monoclonal antibody (Ab) with which to probe P2X(7) receptors in central and peripheral immune cells. In HEK cells expressing rat P2X(7) receptors, the Ab increased the maximum current evoked by BzATP by 3-8-fold with a 5-fold leftward shift in EC50 concentration. This Ab recognized only a nondenatured, multimeric form of the receptor on blue native-PAGE but did not recognize the denatured form on SDS-PAGE. A C-terminaI polyclonal P2X(7) Ab recognized both monomeric subunits on SDS-PAGE and a multimeric complex on blue native-PAGE in this heterologous expression system. With Western blotting using these two Abs, native P2X(7) receptors in peritoneal macrophage and bone marrow cells are shown to exist as a strongly bound multimeric complex, whereas P2X(7) receptors in brain glia and/or astrocytes appear to form only as monomeric subunits.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 10/04/20 alle ore 00:37:26