Your browser doesn't support javascript.
loading
Mostrar: 20 | 50 | 100
Resultados 1 - 5 de 5
Filtrar
Mais filtros

Base de dados
Tipo de documento
Assunto da revista
País de afiliação
Intervalo de ano de publicação
1.
Eur J Pharmacol ; 362(2-3): 221-7, 1998 Dec 04.
Artigo em Inglês | MEDLINE | ID: mdl-9874174

RESUMO

The pyrimidine nucleotide, uridine triphosphate (UTP), was tested with skinned skeletal muscle fibers in order to investigate the UTP-sensitive pathway of Ca2+ release from the sarcoplasmic reticulum. The presence of ryanodine (200 microM), ruthenium red (10 microM) or heparin (2.5 mg/ml) did not affect the tension elicited in the presence of UTP, demonstrating that the UTP-induced Ca2+ release involved neither ryanodine nor inositol triphosphate-sensitive channels. Drugs such as compound 48/80 or cyclopiazonic acid used to inhibit Ca2+-ATPase in its reverse function appeared to be, respectively, non-specific or without any inhibitory effect on the tension induced by UTP. Finally, the UTP-induced tension as well as the trifluoperazine-induced tension were abolished in the presence of spermidine (50 mM), supporting the hypothesis that the UTP-sensitive pathway of the SR Ca2+ release might occur through the uncoupled calcium ATPase.


Assuntos
Cálcio/metabolismo , Contração Muscular/efeitos dos fármacos , Músculo Esquelético/efeitos dos fármacos , Uridina Trifosfato/farmacologia , Animais , Anticoagulantes/farmacologia , Corantes/farmacologia , Interações Medicamentosas , Inibidores Enzimáticos/farmacologia , Heparina/farmacologia , Indóis/farmacologia , Músculo Esquelético/metabolismo , Ratos , Rutênio Vermelho/farmacologia , Rianodina/farmacologia , Retículo Sarcoplasmático/efeitos dos fármacos , Retículo Sarcoplasmático/metabolismo , Espermidina/farmacologia , p-Metoxi-N-metilfenetilamina/farmacologia
2.
J Gravit Physiol ; 3(2): 54-7, 1996 Sep.
Artigo em Inglês | MEDLINE | ID: mdl-11540282

RESUMO

NASA: Soleus, vastus intermedius, tibialis anterior, and extensor digitorum longus muscles were removed from rats following space flight onboard the SLS-2 mission and from control animals. Muscle tissues were studied for their calcium and strontium activated tension characteristics and for structural changes. Muscles were also examined for myosin composition using electrophoresis. Results indicate that changes occurred in structural and functional muscle characteristics in both slow and fast muscle fiber types. These results are detailed and discussed.^ieng


Assuntos
Contração Muscular/fisiologia , Músculo Esquelético/fisiopatologia , Atrofia Muscular/fisiopatologia , Voo Espacial , Ausência de Peso/efeitos adversos , Adaptação Fisiológica , Animais , Cálcio/farmacologia , Masculino , Contração Muscular/efeitos dos fármacos , Fibras Musculares de Contração Rápida/metabolismo , Fibras Musculares de Contração Rápida/patologia , Fibras Musculares de Contração Lenta/metabolismo , Fibras Musculares de Contração Lenta/patologia , Músculo Esquelético/metabolismo , Músculo Esquelético/patologia , Músculo Esquelético/fisiologia , Atrofia Muscular/etiologia , Atrofia Muscular/metabolismo , Atrofia Muscular/patologia , Cadeias Pesadas de Miosina/metabolismo , Cadeias Leves de Miosina/metabolismo , Ratos , Ratos Sprague-Dawley , Estrôncio/farmacologia
3.
Acta Physiol Scand ; 160(3): 199-205, 1997 Jul.
Artigo em Inglês | MEDLINE | ID: mdl-9246382

RESUMO

The effect of bovine serum albumin (BSA) on the activity of the calcium release channel of the sarcoplasmic reticulum from rabbit skeletal muscle was investigated using both tension recording from skinned fibres and electrophysiological recording of unitary channel currents from planar lipid membranes. BSA had no effect on the Ca2+ affinity of the contractile proteins, elicited no tension per se in Ca(2+)-loaded skinned fibres, but potentiated caffeine-induced tension. Maximum potentiation was observed with 0.05-0.5% BSA. BSA (0.1%) had no detectable effect on the basal activity of the Ca(2+)-release channel incorporated in lipid bilayer. However, channel stimulation elicited by either caffeine (2 mM) or ATP (60 microM) was further enhanced by BSA (0.1%), as indicated by significant increases in Po, the open probability of the channel. These results suggest that BSA can modulate the response of the skeletal muscle SR Ca(2+)-release channel to different activators such as caffeine and ATP.


Assuntos
Canais de Cálcio/efeitos dos fármacos , Músculo Esquelético/metabolismo , Retículo Sarcoplasmático/metabolismo , Soroalbumina Bovina/farmacologia , Trifosfato de Adenosina/farmacologia , Animais , Cafeína/farmacologia , Canais de Cálcio/ultraestrutura , Bovinos , Técnicas In Vitro , Ativação do Canal Iônico/fisiologia , Cinética , Contração Muscular/efeitos dos fármacos , Músculo Esquelético/efeitos dos fármacos , Músculo Esquelético/ultraestrutura , Inibidores de Fosfodiesterase/farmacologia , Coelhos , Retículo Sarcoplasmático/efeitos dos fármacos , Retículo Sarcoplasmático/ultraestrutura
4.
Can J Physiol Pharmacol ; 73(10): 1451-7, 1995 Oct.
Artigo em Inglês | MEDLINE | ID: mdl-8748937

RESUMO

Chemically skinned muscle fibers from rat extensor digitorum longus muscle were used to study the effects of uridine triphosphate (UTP) on Ca2+ uptake and release by the sarcoplasmic reticulum (SR) and on Ca2+-activated tensions. Total replacement (2.5 mM) of adenosine triphosphate (ATP) with UTP (i) increased submaximal Ca2+-induced tension (pCa 6.2-5.8) but diminished Po, the maximum tension elicited by pCa 4.2, by ca. 15%, (ii) markedly reduced Ca2+ uptake by the SR (evaluated by caffeine-elicited tension); and (iii) induced tension in Ca2+-loaded fibers. The UTP-induced tension averaged 55% of Po and its rates of development and decay were considerably slower than those of caffeine-evoked tension. The UTP-induced tension (i) depended on the Ca2+-loading conditions; (ii) was reversibly blocked by brief (15 s) exposures of Ca2+-loaded fibers to 5 mM EGTA or by pretreatment with caffeine; (iii) was abolished by functional disruption of the SR with the nonionic detergent Brij-58; and (iv) persisted after blockade of the SR Ca2+ release channels with ruthenium red. Exposure of Ca2+-loaded fibers to UTP depressed the tension elicited subsequently by caffeine, and enhanced the rate of depletion of caffeine-sensitive Ca2+ stores during soaking in relaxing solutions containing 5 mM EGTA. The UTP-induced tension is attributed to increased release of Ca2+ from the SR, via a ruthenium red insensitive pathway(s), combined with reduced Ca2+ uptake by the SR and increased Ca2+ affinity of the contractile proteins.


Assuntos
Cálcio/farmacocinética , Fibras Musculares Esqueléticas/efeitos dos fármacos , Uridina Trifosfato/farmacologia , Trifosfato de Adenosina/farmacologia , Animais , Cafeína/farmacologia , Estimulantes do Sistema Nervoso Central/farmacologia , Corantes , Interações Medicamentosas , Ratos , Rutênio Vermelho/farmacologia , Retículo Sarcoplasmático/efeitos dos fármacos , Retículo Sarcoplasmático/metabolismo
SELEÇÃO DE REFERÊNCIAS
DETALHE DA PESQUISA