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1.
Biochem Biophys Res Commun ; 519(3): 547-552, 2019 11 12.
Artigo em Inglês | MEDLINE | ID: mdl-31537386

RESUMO

This study investigated dopaminergic function in the lateral hypothalamus (LH) in the regulation of feeding behavior. Refeeding increased dopamine levels in the LH. Glucose injection also increased dopamine levels in the LH. When the retrograde tracer Fluoro-Gold (FG) was injected into the LH, FG-positive cells were found in the ventral tegmental area (VTA) and the substantia nigra pars compacta (SNC), which were mostly tyrosine hydroxylase-positive. Injection of the dopamine D1 receptor agonist SKF 38393, but not the antagonist SCH 23390, into the LH increased food intake. Similarly, injection of the dopamine D2 receptor agonist quinpirole, but not the antagonist l-sulpiride, into the LH increased food intake. The effect of each agonist was blocked by its respective antagonist. Furthermore, injection of quinpirole, but not SKF 38393, decreased the mRNA level of preproorexin. In addition, injection of SKF 38393 decreased the mRNA levels of neuropeptide Y and agouti-related peptide, whereas the injection of quinpirole increased the mRNA level of proopiomelanocortin. These results indicate that food intake activates dopamine neurons projecting from the VTA/SNC to the LH through an increase in blood glucose levels, which terminates food intake by stimulation of dopamine D1 and D2 receptors. It is also possible that stimulation of dopamine D1 and D2 receptors in the LH inhibits feeding behavior through different neuropeptides.


Assuntos
Dopaminérgicos/farmacologia , Dopamina/farmacologia , Comportamento Alimentar/efeitos dos fármacos , Região Hipotalâmica Lateral/efeitos dos fármacos , Hipotálamo/efeitos dos fármacos , Neuropeptídeos/farmacologia , Receptores de Dopamina D1/antagonistas & inibidores , 2,3,4,5-Tetra-Hidro-7,8-Di-Hidroxi-1-Fenil-1H-3-Benzazepina/farmacologia , Animais , Agonistas de Dopamina/farmacologia , Região Hipotalâmica Lateral/metabolismo , Hipotálamo/metabolismo , Masculino , Camundongos , Camundongos Endogâmicos ICR , Quimpirol/farmacologia , Ratos , Ratos Wistar , Receptores de Dopamina D1/agonistas , Receptores de Dopamina D1/metabolismo , Receptores de Dopamina D2/agonistas , Receptores de Dopamina D2/metabolismo
2.
Proc Natl Acad Sci U S A ; 116(40): 19945-19951, 2019 10 01.
Artigo em Inglês | MEDLINE | ID: mdl-31533957

RESUMO

Cytochrome c oxidase (CcO), a membrane enzyme in the respiratory chain, catalyzes oxygen reduction by coupling electron and proton transfer through the enzyme with a proton pump across the membrane. In all crystals reported to date, bovine CcO exists as a dimer with the same intermonomer contacts, whereas CcOs and related enzymes from prokaryotes exist as monomers. Recent structural analyses of the mitochondrial respiratory supercomplex revealed that CcO monomer associates with complex I and complex III, indicating that the monomeric state is functionally important. In this study, we prepared monomeric and dimeric bovine CcO, stabilized using amphipol, and showed that the monomer had high activity. In addition, using a newly synthesized detergent, we determined the oxidized and reduced structures of monomer with resolutions of 1.85 and 1.95 Å, respectively. Structural comparison of the monomer and dimer revealed that a hydrogen bond network of water molecules is formed at the entry surface of the proton transfer pathway, termed the K-pathway, in monomeric CcO, whereas this network is altered in dimeric CcO. Based on these results, we propose that the monomer is the activated form, whereas the dimer can be regarded as a physiological standby form in the mitochondrial membrane. We also determined phospholipid structures based on electron density together with the anomalous scattering effect of phosphorus atoms. Two cardiolipins are found at the interface region of the supercomplex. We discuss formation of the monomeric CcO, dimeric CcO, and supercomplex, as well as their role in regulation of CcO activity.


Assuntos
Complexo IV da Cadeia de Transporte de Elétrons/química , Mitocôndrias Cardíacas/enzimologia , Animais , Cardiolipinas/química , Bovinos , Cristalografia por Raios X , Digitonina/química , Transporte de Elétrons , Complexo I de Transporte de Elétrons/química , Ligação de Hidrogênio , Concentração de Íons de Hidrogênio , Membranas Mitocondriais/enzimologia , Conformação Molecular , Oxirredução , Oxigênio/química , Fosfolipídeos/química , Fósforo/química , Ligação Proteica , Conformação Proteica , Multimerização Proteica
3.
Quintessence Int ; 39(1): 11-6, 2008 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-18551211

RESUMO

Fluorescence, opalescence, and translucency are critical for restorative materials to mimic the optical properties and appearance of natural teeth. This case report describes the restoration of multiple anterior teeth with CAD/CAM-fabricated glass-infiltrated aluminum oxide ceramic (In-Ceram Alumina, Vita Zahnfabrik) crowns and illustrates the technical steps to achieve an adequate amount of fluorescence in the ceramic veneering material. CAD/CAM aluminum oxide ceramic copings and frameworks can be predictable and successful when replacing missing tooth structure and imitating optical properties of natural teeth. A modified layering technique enhances fluorescence within the veneering ceramic and provides an esthetic appearance of glass-infiltrated aluminum oxide ceramic restorations.


Assuntos
Óxido de Alumínio/química , Coroas , Porcelana Dentária/química , Planejamento de Prótese Dentária , Vidro/química , Adulto , Desenho Assistido por Computador , Cárie Dentária/terapia , Facetas Dentárias , Estética Dentária , Feminino , Fluorescência , Humanos , Incisivo/patologia , Óptica e Fotônica , Técnica para Retentor Intrarradicular , Descoloração de Dente/terapia
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