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Seihai-to (TJ-90)-Induced Activation of Airway Ciliary Beatings of Mice: Ca Modulation of cAMP-Stimulated Ciliary Beatings via PDE1.

Sei-hai-to (TJ-90, Qing Fei Tang), a Chinese traditional medicine, increases ciliary beat frequency (CBF) and ciliary bend angle (CBA) mediated via cAMP (3',5'-cyclic adenosine monophosphate) accumulation modulated by Ca-activated phosphodiesterase 1 (PDE1A). A high concentration of TJ-90 (≥40 μg/mL) induced two types of CBF increases, a transient increase (an initial increase, followed by a decrease) and a sustained increase without any decline, while it only sustained the CBA increase. Upon inhibiting increases in intracellular Ca concentration ([Ca]) by 10 μM BAPTA-AM (Ca-chelator, 1,2-Bis(2-aminophenoxy)ethane-N,N,N',N'-tetraacetic acid tetrakis(acetoxymethyl ester) or Ca/calmodulin-dependent PDE1 by 8MmIBMX (a selective PDE1 inhibitor), TJ-90 (400 μg/mL) induced only the sustained CBF increase without any transient CBF increase. The two types of the CBF increase (the transient increase and the sustained increase) induced by TJ-90 (≥40 μg/mL) were mimicked by the stimulation with both procaterol (100 pM) and ionomycin (500 nM). Thus, TJ-90 stimulates small increases in the intracellular cAMP concentration ([cAMP]) and [Ca] in airway ciliary cells of mice. These small increases in [cAMP] and [Ca] cause inducing a transient CBF increase or a sustained CBF increase in an airway ciliary cells, depending on the dominant signal, Ca-signal, or cAMP-signal.

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Ofloxacin CAS Number [824 White PTFE red silicone s Cryogenic Storage Boxes P Toxoplasma gondii MIC 3 r Anti AGO2 Human, Monoclon Anti AGO2 Mouse, Monoclon Anti AGO2 Human, Monoclon Anti AGO2 Mouse, Monoclon Human Ciliary Neurotrophi FAM cAMP PDE IV substrate TAMRA cAMP PDE IV substra Screw Cap Tubes & O-Ring

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The effect of magnolol on Ca homeostasis and its related physiology in human oral cancer cells.

Magnolol, a polyphenol compound from herbal medicines, was shown to alter physiology in various cell models. However, the effect of magnolol on Ca homeostasis and its related physiology in oral cancer cells is unclear. This study examined whether magnolol altered Ca signaling and cell viability in OC2 human oral cancer cells.

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Human breast invasive duc Frozen multiple human org Oral squamous cell cancer Oral cavity cancer test t Anti AGO2 Human, Monoclon Anti AGO2 Human, Monoclon Mouse Anti-Human CA19-9 ( Macrophage Colony Stimula Macrophage Colony Stimula Breast cancer membrane pr serologically defined col Cancer Apoptosis Phospho-

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Arginase II inhibition prevents interleukin-8 production through regulation of p38 MAPK phosphorylation activated by loss of mitochondrial membrane potential in nLDL-stimulated hAoSMCs.

Arginase inhibition exhibits beneficial effects in vascular endothelial and smooth muscle cells. In human aortic smooth muscle cells (hAoSMCs), native low-density lipoprotein (nLDL) induced the production of interleukin-8 (IL-8) that is involved in the pathogenesis of cardiovascular diseases. Therefore, we examined the effect of arginase inhibition on IL-8 production and the underlying mechanism. In hAoSMCs, reverse transcription-PCR, western blotting and immunocytochemistry with MitoTracker confirmed that arginase II was confined predominantly to mitochondria. The mitochondrial membrane potential (MMP) was assessed using tetramethylrhodamine ethyl ester. The MMP decreased upon nLDL stimulation but was restored upon arginase inhibition. MMP loss caused by nLDL was prevented by treatment with the intracellular Ca chelator BAPTA-AM. In mitochondrial Ca measurements using Rhod-2 AM, increased mitochondrial Ca levels by nLDL were inhibited upon preincubation with an arginase inhibitor. Among the polyamines, spermine, an arginase activity-dependent product, caused mitochondrial Ca movement. The nLDL-induced MMP change resulted in p38 mitogen-activated protein kinase (MAPK) phosphorylation and IL-8 production and was prevented by the arginase inhibitors BAPTA and ruthenium 360. In isolated AoSMCs from ApoE mice fed a high-cholesterol diet, arginase activity, p38 MAPK phosphorylation, spermine and mitochondrial Ca levels and keratinocyte-derived chemokine (KC) production were increased compared with wild-type (WT) mice. However, in AoSMCs isolated from arginase II-null mice, increases in MMP and decreases in mitochondrial Ca levels were noted compared with WT and were associated with p38 MAPK activation and IL-8 production. These data suggest that arginase activity regulates the change in MMP through Ca uptake that is essential for p38 MAPK phosphorylation and IL-8 production.

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Cell Meter™ JC 10 Mitoc Cell Meter™ JC 10 Mitoc Cell Meter™ Mitochondri Cell Cycle Control Phosph Cytoskeleton II Phospho-S GPCR Signaling to MAPK ER Insulin Glucose Phospho-S Jak Stat II Phospho-Speci MAPK Phospho-Specific Arr NF-kB II Phospho-Specific Nuclear Membrane Receptor Cytokine (Human) Antibody

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TNF-α induces expression of the circadian clock gene Bmal1 via dual calcium-dependent pathways in rheumatoid synovial cells.

Tumor necrosis factor (TNF)-α is responsible for expressions of several clock genes and affects joint symptoms of rheumatoid arthritis (RA) with diurnal fluctuation. We tried to determine the mechanism involved in over-expression of Bmal1, induced by TNF-α, in primary cultured rheumatoid synovial cells. Cells were incubated with intra-cellular Ca chelator BAPTA-AM, calcineurin inhibitor FK506 and p300/CBP (CREB binding protein) inhibitor C646, respectively, or transfected with p300 and CBP small interfering RNA (siRNA) before stimulation with TNF-α. Oscillation phase and amplitude of Bmal1, transcriptional activator Rorα, transcriptional repressor Rev-erbα, and histone acetyltransferases (p300 and Cbp) were evaluated by quantitative real-time PCR. As results, TNF-α did not influence the oscillation phase of Rev-erbα, while enhanced those of Rorα, resulting in over-expression of Bmal1. When Ca influx was inhibited by BAPTA-AM, TNF-α-mediated up-regulation of Rorα was cancelled, however, that of Bmal1 was still apparent. When we further explored another pathway between TNF-α and Bmal1, TNF-α suppressed the expression of Rev-erbα in the absence of Ca influx, as well as those of p300 and Cbp genes. Finally, actions of TNF-α, in increasing Bmal1/Rorα and decreasing Rev-erbα, were cancelled by C646 treatment or silencing of both p300 and Cbp. In conclusion, we determined a novel role of TNF-α in inducing Bmal1 via dual calcium dependent pathways; Rorα was up-regulated in the presence of Ca influx and Rev-erbα was down-regulated in the absence of that. Results proposed that inhibition of p300/CBP could be new therapeutic targets for RA.

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BAPTA-AM dramatically improves maturation and development of bovine oocytes from grade-3 cumulus-oocyte complexes.

Intracellular free calcium ([Ca ] ) is essential for oocyte maturation and early embryonic development. Here, we investigated the role of [Ca ] in oocytes from cumulus-oocyte complexes (COCs) with respect to maturation and early embryonic development, using the calcium-buffering agent BAPTA-AM (1,2-bis[2-aminophenoxy]ethane-N,N,N',N'-tetraacetic acid tetrakis [acetoxymethyl ester]). COCs were graded based on compactness of the cumulus mass and appearance of the cytoplasm, with Grade 1 indicating higher quality and developmental potential than Grade 3. Results showed that: (i) [Ca ] in metaphase-II (MII) oocytes from Grade-3 COCs was significantly higher than those from Grade-1 COCs, and was significantly reduced by BAPTA-AM; (ii) nuclear maturation of oocytes from Grade-3 COCs treated with BAPTA-AM was enhanced compared to untreated COCs; (iii) protein abundance of Cyclin B and oocyte-specific Histone 1 (H1FOO) was improved in MII oocytes from Grade-3 COCs treated with BAPTA-AM; (iv) Ca transients were triggered in each group upon fertilization, and the amplitude of [Ca ] oscillations increased in the Grade-3 group upon treatment with BAPTA-AM, with the magnitude approaching that of the Grade-1 group; and (v) cleavage rates and blastocyst-formation rates were improved in the Grade-3 group treated with BAPTA-AM compared to untreated controls following in vitro fertilization and parthenogenetic activation. Therefore, BAPTA-AM dramatically improved oocyte maturation, oocyte quality, and embryonic development of oocytes from Grade-3 COCs.

2879 related Products with: BAPTA-AM dramatically improves maturation and development of bovine oocytes from grade-3 cumulus-oocyte complexes.

DNA (cytosine 5) methyltr ELBI ELISA grade bovine t ELBI ELISA grade bovine t ELISA grade bovine type I T-cell proliferation grad TCBI T cell proliferation TCBI T cell proliferation IMBI Immunization grade b Immunization grade bovine Immunization grade bovine Immunization grade bovine Immunization grade bovine

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Diosgenin, an Activator of 1,25D3-MARRS Receptor/ERp57, Attenuates the Effects of TNF-α by Causing ADAM10-Dependent Ectodomain Shedding of TNF Receptor 1.

We investigated how diosgenin, a steroidal sapogenin, has anti-tumor necrosis factor-α (TNF-α) effects in human aortic endothelial cells (HAECs).

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Calcimycin mediates mycobacterial killing by inducing intracellular calcium-regulated autophagy in a P2RX7 dependent manner.

Phenotypic screening led to the identification of calcimycin as a potent inhibitor of Mycobacterium bovis BCG (M. bovis BCG) growth in vitro and in THP-1 cells. In the present study, we aim to decipher the mechanism of antimycobacterial activity of calcimycin. We noticed that treatment with calcimycin led to up-regulation of different autophagy markers like Beclin-1, autophagy-related gene (Atg) 7, Atg 3 and enhanced microtubule-associated protein 1A/1B-light chain 3-I (LC3-I) to LC3-II conversion in macrophages. This calcimycin-mediated killing of intracellular M. smegmatis and M. bovis BCG was abrogated in the presence of 3-methyladenine (3-MA). We also demonstrate that calcimycin binding with purinergic receptor P2X7 (P2RX7) led to increase in intracellular calcium level that regulates the extracellular release of ATP. ATP was able to regulate calcimycin-induced autophagy through P2RX7 in an autocrine fashion. Blocking of either P2RX7 expression by 1-[N,O-bis(5-Isoquinolinesulfonyl)-N-methyl-l-tyrosyl]-4-phenylpiperazine (KN-62) or reducing intracellular calcium levels by 1,2-Bis(2-aminophenoxy)ethane-N,N,N',N'-tetraacetic acid tetra (acetoxy-methyl) ester (BAPTA-AM) abrogated the antimycobacterial activity of calcimycin. Taken together, these results showed that calcimycin exerts its antimycobacterial effect by regulating intracellular calcium-dependent ATP release that induces autophagy in a P2RX7 dependent manner.

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Effect of Methoxsalen on Ca²⁺ Homeostasis and Viability in Human Osteosarcoma Cells.

Methoxsalen is a natural compound found in many seed plants. The effect of methoxsalen on Ca²⁺- related physiology in human osteosarcoma is unclear. This study investigated the effect of methoxsalen on cytosolic free Ca²⁺ concentrations ([Ca²⁺]i) in MG63 human osteosarcoma cells. Methoxsalen induced [Ca²⁺]i rises concentration-dependently. Methoxsalen-induced Ca²⁺ entry was confirmed by Mn²⁺-induced quench of fura-2 fluorescence. This Ca²⁺ entry was suppressed by nifedipine, econazole, and SKF96365. In Ca²⁺-free medium, incubation with the endoplasmic reticulum Ca²⁺ pump inhibitor 2,5-di-tert-butylhydroquinone (BHQ) inhibited methoxsalen-evoked [Ca²⁺]i rises by 96%. In contrast, incubation with methoxsalen abolished BHQ-evoked [Ca²⁺]i rises. Inhibition of phospholipase C (PLC) with U73122 abolished methoxsalen-induced [Ca²⁺]i rises. Methoxsalen was cytotoxic at 300-700 μM in a concentration-dependent fashion. Chelating cytosolic Ca²⁺ with 1,2-bis(2-aminophenoxy)ethane-N,N,N’,N’-tetraacetic acid/acetoxymethyl ester (BAPTA/AM) did not prevent methoxsalen-induced cytotoxicity. Collectively, our data suggest that in MG63 cells, methoxsalen induced [Ca²⁺]i rises by evoking PLC-dependent Ca²⁺ release from the endoplasmic reticulum, and Ca²⁺ entry via store-operated Ca²⁺ entry. Methoxsalen also induced Ca²⁺- disassociated cell death.

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Effect of Protriptyline on [Ca²⁺]i and Viability in MDCK Renal Tubular Cells.

Protriptyline has been used as an antidepressant. Clinically it has been prescribed in the auxiliary treatment of cancer patients. However, its effect on Ca²⁺ signaling and related physiology is unknown in renal cells. This study examined the effect of protriptyline on cytosolic free Ca²⁺ concentrations ([Ca²⁺]i) and viability in Madin-Darby canine kidney (MDCK) tubular cells. Protriptyline induced [Ca²⁺]i rises concentration-dependently. The response was reduced by 20% by removing extracellular Ca²⁺. Protriptyline-induced Ca²⁺ entry was not altered by protein kinase C (PKC) activity but was inhibited by 20% by three modulators of store-operated Ca²⁺ channels: nifedipine, econazole and SKF96365. In Ca²⁺-free medium, treatment with the endoplasmic reticulum Ca²⁺ pump inhibitor 2,5- di-tert-butylhydroquinone (BHQ) or thapsigargin partially inhibited protriptyline-evoked [Ca²⁺]i rises. Conversely, treatment with protriptyline inhibited partially BHQ or thapsigargin-evoked [Ca²⁺]i rises. Inhibition of phospholipase C (PLC) with U73122 did not change protriptyline-induced [Ca²⁺]i rises. Protriptyline at 5-200 μM decreased cell viability, which was not reversed by pretreatment with the Ca²⁺ chelator 1,2-bis(2-aminophenoxy)ethane-N,N,N’,N’-tetraacetic acid-acetoxymethyl ester (BAPTA/ AM). Together, in MDCK cells, protriptyline induced [Ca²⁺]i rises by evoking PLC-independent Ca²⁺ release from the endoplasmic reticulum and other unknown stores, and Ca²⁺ entry via PKCinsensitive store-operated Ca²⁺ entry. Protriptyline also caused Ca²⁺-independent cell death.

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Caffeine Suppresses the Activation of Hepatic Stellate Cells cAMP-Independently by Antagonizing Adenosine Receptors.

During liver injury, hepatic stellate cells (HSCs) are activated by various cytokines and transdifferentiated into myofibroblast-like activated HSCs, which produce collagen, a major source of liver fibrosis. Therefore, the suppression of HSC activation is regarded as a therapeutic target for liver fibrosis. Several epidemiological reports have revealed that caffeine intake decreases the risk of liver disease. In this study, therefore, we investigated the effect of caffeine on the activation of primary HSCs isolated from mice. Caffeine suppressed the activation of HSC in a concentration-dependent manner. BAPTA-AM, an intracellular Ca chelator, had no effect on the caffeine-induced suppression of HSC activation. None of the isoform-selective inhibitors of phosphodiesterase1 to 5 affected changes in the morphology of HSC during activation, whereas CGS-15943, an adenosine receptor antagonist, inhibited them. Caffeine had no effect on intracellular cAMP level or on the phosphorylation of extracellular signal-regulated kinase (ERK)1/2. In contrast, caffeine significantly decreased the phosphorylation of Akt1. These results suggest that caffeine inhibits HSC activation by antagonizing adenosine receptors, leading to Akt1 signaling activation.

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