scholarly journals Regulation of Intracellular Calcium by Carbon Monoxide in Human Bronchial Epithelial Cells

2017 ◽  
Vol 42 (6) ◽  
pp. 2377-2390 ◽  
Author(s):  
Rui-Gang Zhang ◽  
Chung-Yin Yip ◽  
Wing-Hung Ko
Keyword(s):  
Carbon Monoxide ◽  
Protein Kinase ◽  
Intracellular Calcium ◽  
Soluble Guanylyl Cyclase ◽  
Bronchial Epithelial Cell ◽  
Inhibitory Effect ◽  
Epithelial Cell Line ◽  
Protein Kinase Activity ◽  
Bronchial Epithelial ◽  
Dependent Protein

Background/Aims: Carbon monoxide (CO) is an important autocrine/paracrine messenger involved in a variety of physiological and pathological processes. This study aimed to investigate the regulatory role of CO released by CO-releasing molecule-2 (CORM-2) in a P2Y receptor-mediated calcium-signaling pathway in the human bronchial epithelial cell line, 16HBE14o-. Methods: Intracellular calcium ([Ca2+]i) was measured by fura-2 microspectrofluorimetry. D-myo-inositol-1-phosphate (IP1) levels and cGMP-dependent protein kinase activity (PKG) were also quantified. Results: The exogenous application of CORM-2 increased both intracellular Ca2+ and IP1, which are inhibited by U73122, a phospholipase C (PLC) inhibitor. In contrast, the P2Y2/P2Y4 receptor-mediated intracellular Ca2+ release and influx induced by UTP were inhibited in the presence of CORM-2. However, CORM-2 did not affect the store-operated Ca2+ entry (SOCE) induced by thapsigargin (Tg). Moreover, the inhibitory effect of CORM-2 on UTP-induced calcium increase could be attenuated by a soluble guanylyl cyclase (sGC) inhibitor, 1H-[1,2,4]oxadiazolo[4,3,-a]quinoxalin-1-one (ODQ), or a Protein Kinase G (PKG) inhibitor, KT5823, suggesting the involvement of sGC/PKG signaling in this process. Conclusion: CORM-2 serves a dual role in modulating [Ca2+]i in 16HBE14o- cells. Thus, CO released by CORM-2 may act as a regulator of calcium homeostasis in human airway epithelia. These findings help further elucidate the function of CO in many physiological and pathological conditions.

Retinoic acid inhibits interleukin-4-induced eotaxin production in a human bronchial epithelial cell line

2004 ◽  
Vol 286 (4) ◽  
pp. L777-L785 ◽  
Author(s):  
Kei Takamura ◽  
Yasuyuki Nasuhara ◽  
Motoko Kobayashi ◽  
Tomoko Betsuyaku ◽  
Yoko Tanino ◽  
...  
Keyword(s):  
Retinoic Acid ◽  
Epithelial Cell ◽  
Cell Line ◽  
Nuclear Translocation ◽  
Bronchial Epithelial Cell ◽  
Inhibitory Effect ◽  
Human Bronchial Epithelial Cell ◽  
Epithelial Cell Line ◽  
Transcriptional Level ◽  
Bronchial Epithelial

Retinoic acid (RA) is known to accelerate wound healing and induce cell differentiation. All- trans RA (ATRA) exerts its effect by binding retinoic acid receptors, which are members of the nuclear receptor family. We investigated whether RA can alter expression of eotaxin, a potent eosinophil chemoattractant that is regulated by the transcription factors signal transducer and activator of transcription 6 (STAT6) and NF-κB. We examined the effects of RA on eotaxin expression in a human bronchial epithelial cell line BEAS-2B. ATRA and its stereodimer 9- cis retinoic acid (9- cis RA) inhibited IL-4-induced release of eotaxin at 10-6M by 78.0 and 52.0%, respectively ( P < 0.05). ATRA and 9- cis RA also significantly inhibited IL-4-induced eotaxin mRNA expression at 10-6M by 52.3 and 53.5%, respectively ( P < 0.05). In contrast, neither ATRA nor 9- cis RA had any effects on TNF-α-induced eotaxin production. In transfection studies using eotaxin promoter luciferase plasmids, the inhibitory effect of ATRA on IL-4-induced eotaxin production was confirmed at the transcriptional level. Interestingly, ATRA had no effects on IL-4-induced tyrosine phosphorylation, nuclear translocation, or DNA binding activity of STAT6. Activating protein-1 was not involved in ATRA-mediated transrepression of eotaxin with IL-4 stimulation. The mechanism of the inhibitory effect of ATRA on IL-4-induced eotaxin production in human bronchial epithelial cells has not been elucidated but does not appear to be due to an effect on STAT6 activation. These findings raise the possibility that RA may reduce eosinophilic airway inflammation, one of the prominent pathological features of allergic diseases such as bronchial asthma.

Ca2+ and lipolysis in adipocytes from exercise-trained rats

1994 ◽  
Vol 77 (6) ◽  
pp. 2618-2624 ◽  
Author(s):  
T. Izawa ◽  
T. Komabayashi
Keyword(s):  
Protein Kinase ◽  
Adrenocorticotropic Hormone ◽  
Kinase Activity ◽  
Inhibitory Effect ◽  
Protein Kinase Activity ◽  
Dibutyryl Camp ◽  
Inhibitory Effects ◽  
Dependent Protein Kinase ◽  
Camp Dependent Protein Kinase ◽  
Dependent Protein

The effects of Ca2+ on lipolysis and protein kinase activity in adipocytes from exercise-trained rats were investigated. Chronic exercise significantly increased lipolytic responses to norepinephrine and dibutyryl adenosine 3′,5′-cyclic monophosphate (cAMP). The inhibitory effects of N-(6-aminohexyl)-5-chloro-1-naphthalene sulfonamide (W-7), a calumodulin inhibitor, on norepinephrine- and dibutyryl cAMP-stimulated lipolysis were significantly greater in trained than in sedentary rats. Training did not alter cAMP-dependent protein kinase activity. However, the inhibitory effect of W-7 on cAMP-dependent protein kinase activity was much greater in trained than in sedentary rats. The basal intracellular free Ca2+ concentration ([Ca2+]i) was significantly higher in trained than in sedentary rats. The rapid and transient increases in [Ca2+]i due to adrenocorticotropic hormone and phenylephrine from basal levels were significantly lower in trained than in sedentary rats. However, the higher basal [Ca2+]i level in trained rats led to increases in sustained [Ca2+]i levels after stimulation. We concluded that in trained rats the regulation of protein kinase activity by cAMP depends to a greater degree on Ca(2+)-calmodulin complex than it does in sedentary rats and that training alters adipocyte intracellular Ca2+ homeostasis, including [Ca2+]i responsiveness to hormones.

Interaction of acetylcholine and epinephrine on heart cyclic AMP-dependent protein kinase

1978 ◽  
Vol 234 (4) ◽  
pp. H432-H438
Author(s):  
S. L. Keely ◽  
T. M. Lincoln ◽  
J. D. Corbin
Keyword(s):  
Protein Kinase ◽  
Kinase Activity ◽  
Inhibitory Effect ◽  
Contractile Force ◽  
Protein Kinase Activity ◽  
Dependent Protein Kinase ◽  
Kinase Activation ◽  
Camp Dependent Protein Kinase ◽  
Cholinergic Agent ◽  
Dependent Protein

In the isolated perfused rat heart, epinephrine produced a rapid, concentration-dependent increase in cyclic adenosine 3',5'-monophosphate (cAMP), activation of cAMP-dependent protein kinase, activation of phosphorylase, and increase in contractile force. At epinephrine concentrations of 1 micron or less, acetylcholine antagonized all these beta-adrenergic effects and also increased cyclic guanosine 3',5'-monophosphate (cGMP) levels. When used alone, acetylcholine produced a rapid elevation of cGMP and markedly diminished contractile force but did not significantly lower basal cAMP levels or cAMP-dependent protein kinase activity. The data suggest that changes in cAMP-dependent protein kinase activity can explain the antagonism of epinephrine-induced activation of phosphorylase by acetylcholine, but cannot completely account for the inhibitory effect of the cholinergic agent on contractile force.

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