Stim1
Mostrando 1-12 de 26 artigos, teses e dissertações.
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1. Efeitos da privação de sono na homeostase e metabolismo do cálcio em esplenócitos de camundongos / Effects of the sleep deprivation in calcium metabolism and homeostasis on splenocytes from mice
O sono é um importante evento fisiológico que diretamente influencia a saúde e está relacionado com o sistema imunológico no qual o cálcio age como um importante mensageiro. Neste estudo, nós realizamos as medidas de mobilização do cálcio citossólico em células vivas com o objetivo de compreender as mudanças na sinalização deste íon em célul
IBICT - Instituto Brasileiro de Informação em Ciência e Tecnologia. Publicado em: 27/04/2011
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2. STIM1/Orai1-mediated store-operated Ca2+ entry: the tip of the iceberg
Highly efficient mechanisms regulate intracellular calcium (Ca2+) levels. The recent discovery of new components linking intracellular Ca2+ stores to plasma membrane Ca2+ entry channels has brought new insight into the understanding of Ca2+ homeostasis. Stromal interaction molecule 1 (STIM1) was identified as a Ca2+ sensor essential for Ca2+ store depletion-
Brazilian Journal of Medical and Biological Research. Publicado em: 2011-11
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3. Contribuição da via STIM1/Orai1 para as diferenças relacionadas ao sexo na entrada de cálcio em miócitos vasculares durante a hipertensão arterial. / Activation of STIM1/Orai1 mediates sex-differences in the calcium influx in vascular miocytes from hypertensive rats.
Os distúrbios na regulação da concentração de cálcio (Ca2+) citoplasmático contribuem para a patogênese da hipertensão arterial. Evidências sugerem que as moléculas de interação estromal (STIM) atuam como sensores dos estoques intracelulares de Ca2+, enquanto as proteínas Orai representam as subunidades que formam os canais de Ca2+ ativados pel
Publicado em: 2010
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4. The Short N-terminal Domains of STIM1 and STIM2 Control the Activation Kinetics of Orai1 Channels*
STIM1 and STIM2 are dynamic transmembrane endoplasmic reticulum Ca2+ sensors, coupling directly to activate plasma membrane Orai Ca2+ entry channels. Despite extensive sequence homology, the STIM proteins are functionally distinct. We reveal that the short variable N-terminal random coil sequences of STIM1 and STIM2 confer profoundly different activation pro
American Society for Biochemistry and Molecular Biology.
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5. Activation of TRPC1 by STIM1 in ER-PM microdomains involves release of the channel from its scaffold caveolin-1
Store-operated Ca2+ entry (SOCE) is activated by redistribution of STIM1 into puncta in discrete ER-plasma membrane junctional regions where it interacts with and activates store-operated channels (SOCs). The factors involved in precise targeting of the channels and their retention at these specific microdomains are not yet defined. Here we report that caveo
National Academy of Sciences.
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6. Properties of Orai1 mediated store-operated current depend on the expression levels of STIM1 and Orai1 proteins
Two cellular proteins, stromal interaction molecule 1 (STIM1) and Orai1, are recently discovered essential components of the Ca2+ release activated Ca2+ (CRAC) channel. Orai1 polypeptides form the pore of the CRAC channel, while STIM1 plays the role of the endoplasmic reticulum Ca2+ sensor required for activation of CRAC current (ICRAC) by store depletion. I
Blackwell Science Inc.
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7. Molecular Determinants of the Coupling between STIM1 and Orai Channels: DIFFERENTIAL ACTIVATION OF Orai1–3 CHANNELS BY A STIM1 COILED-COIL MUTANT*
STIM1 and Orai1 have been reported to interact upon store depletion culminating in Ca2+ release-activated Ca2+ current activation. Recently, the essential region has been identified within the STIM1 C terminus that includes the second coiled-coil domain C-terminally extended by ∼50 amino acids and exhibits a strong binding to the Orai1 C terminus. Based on
American Society for Biochemistry and Molecular Biology.
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8. TRPC channels function independently of STIM1 and Orai1
Recent studies have defined roles for STIM1 and Orai1 as calcium sensor and calcium channel, respectively, for Ca2+-release activated Ca2+ (CRAC) channels, channels underlying store-operated Ca2+ entry (SOCE). In addition, these proteins have been suggested to function in signalling and constructing other channels with biophysical properties distinct from th
Blackwell Science Inc.
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9. Knockdown of stromal interaction molecule 1 attenuates store-operated Ca2+ entry and Ca2+ responses to acute hypoxia in pulmonary arterial smooth muscle
Stromal interaction molecule 1 (STIM1) is a recently discovered membrane-spanning protein thought to sense lumenal Ca2+ in sarco(endo)plasmic reticulum (SR/ER) and transduce activation of Ca2+-permeable store-operated channels (SOC) in plasmalemma in response to SR/ER Ca2+ depletion. To evaluate the role of STIM1 and a closely related protein, STIM2, in Ca2+
American Physiological Society.
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10. A Ca2+ Release-activated Ca2+ (CRAC) Modulatory Domain (CMD) within STIM1 Mediates Fast Ca2+-dependent Inactivation of ORAI1 Channels*♦
STIM1 and ORAI1, the two limiting components in the Ca2+ release-activated Ca2+ (CRAC) signaling cascade, have been reported to interact upon store depletion, culminating in CRAC current activation. We have recently identified a modulatory domain between amino acids 474 and 485 in the cytosolic part of STIM1 that comprises 7 negatively charged residues. A ST
American Society for Biochemistry and Molecular Biology.
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11. TRPC1 and STIM1 mediate capacitative Ca2+ entry in mouse pulmonary arterial smooth muscle cells
Previous studies in pulmonary arterial smooth muscle cells (PASMCs) showed that the TRPC1 channel mediates capacitative Ca2+ entry (CCE), but the molecular signal(s) that activate TRPC1 in PASMCs remains unknown. The aim of the present study was to determine if TRPC1 mediates CCE through activation of STIM1 protein in mouse PASMCs. In primary cultured mouse
Blackwell Science Inc.
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12. Dependence of STIM1/Orai1-mediated Calcium Entry on Plasma Membrane Phosphoinositides*
Recent studies identified two main components of store-operated calcium entry (SOCE): the endoplasmic reticulum-localized Ca2+ sensor protein, STIM1, and the plasma membrane (PM)-localized Ca2+ channel, Orai1/CRACM1. In the present study, we investigated the phosphoinositide dependence of Orai1 channel activation in the PM and of STIM1 movements from the tub
American Society for Biochemistry and Molecular Biology.