Association of two pertussis toxin-sensitive G-proteins with the D2-dopamine receptor from bovine striatum.
AUTOR(ES)
Elazar, Z
RESUMO
The solubilized D2-dopamine receptor from bovine striatum exhibits high and low affinity states for dopaminergic agonists. Guanine nucleotides and pertussis toxin convert the solubilized receptor from a high affinity state to a low one. A D2-receptor preparation partially purified by affinity chromatography on a haloperidol adsorbent, exhibited agonist-stimulated GTPase activity. [32P]ADP-ribosylation by pertussis toxin of this receptor preparation resulted in the specific labeling of two protein bands corresponding to mol. wts of 39 and 41 kd, in SDS-PAGE. Association of these G-proteins with the receptor was specifically inhibited by Gpp(NH)p. Immunoblot analysis of these G-proteins indicated that the 41- and 39-kd protein bands are analogous to brain Gi and Go respectively. These experiments demonstrate that two distinct pertussis toxin-sensitive G-proteins are functionally associated with bovine striatum D2-dopamine receptor.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=401169Documentos Relacionados
- Coupling of a purified goldfish brain kainate receptor with a pertussis toxin-sensitive G protein.
- Pertussis toxin–sensitive G proteins regulate lymphoid lineage specification in multipotent hematopoietic progenitors
- Pertussis toxin-sensitive G proteins are transported toward synaptic terminals by fast axonal transport.
- Pertussis toxin-sensitive activation of p21ras by G protein-coupled receptor agonists in fibroblasts.
- Regulation of Myogenesis by Fibroblast Growth Factors Requires Beta-Gamma Subunits of Pertussis Toxin-Sensitive G Proteins