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Multiple pathways from three types of sugar receptor sites to metabotropic transduction pathways of the blowfly: study by the whole cell-clamp experiments.
Kan, Hideko; Kataoka-Shirasugi, Naoko; Amakawa, Taisaku.
Afiliación
  • Kan H; Graduate School of Human Development and Environment, Kobe University; 3-11, Tsurukabuto, Nada, Kobe 657-8501, Japan.
Article en En | MEDLINE | ID: mdl-21624494
ABSTRACT
Multiple pathways from three types of multiple receptor sites to three types of metabotropic signal transduction pathways were investigated in the whole cell-clamp experiments using isolated labellar sugar receptor neurons (cells) of the adult blowfly, Phormia regina. First, the concentration-response curves of three types of sweet taste components specialized to multiple receptor sites were obtained sucrose for the pyranose sites (P-sites), fructose for the furanose sites (F-sites), and l-valine for the alkyl sites (R-sites). Next, the effects of inhibitors such as 2', 5'-dideoxyadenosine on adenylyl cyclase in the cAMP pathway, LY 83583 on guanylyl cyclase in the cGMP pathway, and U-73122 on phospholipase C in the IP3 pathway were examined. The results showed that all of the inhibitors affected each specific target in the second-messenger transduction pathways. The obtained results verified that the P-site corresponded to the cAMP, the F-site to the cGMP, and the R-site to the IP3 transduction pathway, and that these three signal pathways did not have crossing points.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Gusto / Transducción de Señal / Células Quimiorreceptoras / Dípteros Límite: Animals Idioma: En Revista: Comp Biochem Physiol A Mol Integr Physiol Asunto de la revista: BIOLOGIA MOLECULAR / FISIOLOGIA Año: 2011 Tipo del documento: Article País de afiliación: Japón

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Gusto / Transducción de Señal / Células Quimiorreceptoras / Dípteros Límite: Animals Idioma: En Revista: Comp Biochem Physiol A Mol Integr Physiol Asunto de la revista: BIOLOGIA MOLECULAR / FISIOLOGIA Año: 2011 Tipo del documento: Article País de afiliación: Japón