muromonab-cd3 has been researched along with chelerythrine* in 3 studies
3 other study(ies) available for muromonab-cd3 and chelerythrine
| Article | Year |
|---|---|
Activation of alpha-1 adrenergic receptors increases cytosolic calcium in neurones of the paraventricular nucleus of the hypothalamus.
Norepinephrine (NE) activates adrenergic receptors (ARs) in the hypothalamic paraventricular nucleus (PVN) to increase excitatory currents, depolarise neurones and, ultimately, augment neuro-sympathetic and endocrine output. Such cellular events are known to potentiate intracellular calcium ([Ca Topics: Adrenergic alpha-1 Receptor Agonists; Animals; Benzophenanthridines; Cadmium Chloride; Calcium; Clonidine; Cytosol; Estrenes; Macrocyclic Compounds; Male; Neurons; Norepinephrine; Oxazoles; Paraventricular Hypothalamic Nucleus; Phenylephrine; Prazosin; Pyrrolidinones; Rats; Receptors, Adrenergic, alpha-1; Thapsigargin | 2019 |
Prazosin-stimulated release of hepatic triacylglyceride lipase from primary cultured rat hepatocytes is involved in the regulation of cAMP-dependent protein kinase through activation of the Ca(2+)/calmodulin-dependent protein kinase-II.
Prazosin is an α1 adrenoceptor antagonist used in pharmacotherapy for the treatment of hypertension. Prazosin alters lipid metabolism in vivo, but the involved mechanism is not fully understood. In this study, we investigated the mechanism underlying the alteration of lipid metabolism. We show that the prazosin-stimulated release of hepatic triacylglyceride lipase (HTGL) from primary cultured rat hepatocytes involved Ca(2+)/calmodulin-dependent protein kinase II (CaMK-II) activation.. Primary cultured rat hepatocytes were incubated with prazosin and other agents. The hepatocytes were used in the CaMK-II and protein kinase A (PKA) activity assay. The supernatant was used in the HTGL activity assay and western blotting.. Prazosin-stimulated HTGL release was suppressed by the inositol triphosphate receptor inhibitor xestospongin C and by the calmodulin inhibitor trifluoperazine but not by the protein kinase C inhibitor chelerythrine chloride or a diacylglycerol kinase inhibitor (R59949). Furthermore, the calmodulin-dependent protein kinase II (CaMK-II) activity in prazosin-treated hepatocytes increased in a time- and dose-dependent manner. The cAMP-dependent PKA activity of prazosin-stimulated hepatocytes was suppressed by a phospholipase C (PLC) inhibitor (U-73122), trifluoperazine, and a CaMK-II inhibitor (KN-93).. These results suggested that prazosin-stimulated HTGL release from hepatocytes was caused by activation of PKA associated with stimulation of CaMK-II activity through a signal cascade from PLC. Topics: Animals; Benzophenanthridines; Benzylamines; Calcium-Calmodulin-Dependent Protein Kinase Type 2; Cyclic AMP-Dependent Protein Kinases; Dose-Response Relationship, Drug; Estrenes; Hepatocytes; Lipoprotein Lipase; Macrocyclic Compounds; Male; Oxazoles; Piperidines; Prazosin; Primary Cell Culture; Pyrrolidinones; Quinazolinones; Rats; Sulfonamides; Time Factors; Trifluoperazine | 2016 |
Two distinct signaling pathways for regulation of spontaneous local Ca2+ release by phospholipase C in airway smooth muscle cells.
Spontaneous local Ca(2+) release events have been observed in airway smooth muscle cells (SMCs), but the underlying mechanisms are largely unknown. Considering that each type of SMCs may use its own mechanisms to regulate local Ca(2+) release events, we sought to investigate the signaling pathway for spontaneous local Ca(2+) release events in freshly isolated mouse airway SMCs using a laser scanning confocal microscope. Application of ryanodine to block ryanodine receptors (RyRs) abolished spontaneous local Ca(2+) release events, indicating that these events are RyR-mediated Ca(2+) sparks. Inhibition of inositol 1,4,5-triphosphate receptors (IP(3)Rs) by 2-aminoethoxydiphenyl-borate (2-APB) or xestospongin-C significantly blocked the activity of Ca(2+) sparks. Under patch clamp conditions, dialysis of IP(3) to activate IP(3)Rs increased the activity of local Ca(2+) events in control cells but had no effect in ryanodine-pretreated cells. The RyR agonist caffeine augmented the frequency of Ca(2+) sparks in cells pretreated with and without 2-APB or xestospongin-C. The specific phospholipase C (PLC) blocker U73122 decreased the activity of Ca(2+) sparks and prevented xestospongin-C from producing the inhibitory effect. The protein kinase C (PKC) activator 1-oleoyl-2-acetyl-glycerol or phorbol-12-myristate-13-acetate inhibited Ca(2+) sparks, whereas the PKC inhibitor chelerythrine, PKCvarepsilon inhibitory peptide, or PKCvarepsilon gene knockout produced an opposite effect. Collectively, our data suggest that the basal activation of PLC regulates the activity of RyR-mediated, spontaneous Ca(2+) sparks in airway SMCs through two distinct signaling pathways: a positive IP(3)-IP(3)R pathway and a negative diacylglycerol-PKCvarepsilon pathway. Topics: Alkaloids; Animals; Benzophenanthridines; Boron Compounds; Caffeine; Calcium; Cells, Cultured; Diglycerides; Estrenes; Inositol 1,4,5-Trisphosphate; Inositol 1,4,5-Trisphosphate Receptors; Macrocyclic Compounds; Male; Mice; Myocytes, Smooth Muscle; Oxazoles; Pyrrolidinones; Respiratory System; Ryanodine; Ryanodine Receptor Calcium Release Channel; Sarcoplasmic Reticulum; Signal Transduction; Type C Phospholipases | 2007 |