Antioxidative enzymes in human nasal mucosa after exposure to ozone. Possible role of GSTM1 deficiency

2003 ◽  
Vol 52 (2) ◽  
pp. 51-55 ◽  
Author(s):  
R. Otto-Knapp ◽  
K Jurgovsky ◽  
K. Schierhorn ◽  
G. Kunkel
2007 ◽  
Vol 292 (4) ◽  
pp. L879-L884 ◽  
Author(s):  
Jin Kook Kim ◽  
Sung-Shik Kim ◽  
Keung Won Rha ◽  
Chang-Hoon Kim ◽  
Jae Hoon Cho ◽  
...  

Surfactant proteins (SPs), designated SP-A, SP-B, SP-C, and SP-D, play an important role in surfactant metabolism and host defense mechanisms in the lung. This study investigates expression of the different SP types in human nasal mucosa and cultured normal human nasal epithelial (NHNE) cells and whether the expression of SP mRNA is influenced by the degree of mucociliary differentiation. RT-PCR was performed with mRNA from cultured NHNE cells and nasal mucosa. Immunohistochemical staining for SPs was performed on nasal mucosa specimens. Western blot analysis was performed on cell lysates from cultured NHNE cells. SP-A2, SP-B, and SP-D mRNAs were expressed in normal NHNE cells and human nasal mucosa. SPs were localized in ciliated cells of the surface epithelium and serous acini of the submucosal glands. SP-A, SP-B, and SP-D proteins were expressed in cultured NHNE cells. The degree of mucociliary differentiation influenced expression of the SP gene. We demonstrate that SP-A, SP-B, and SP-D are expressed in human nasal mucosa and cultured NHNE cells. Further study of the functional role of SPs in the upper airway is required.


2003 ◽  
Vol 31 (3) ◽  
pp. 326-331 ◽  
Author(s):  
David A. Groneberg ◽  
Werner Heppt ◽  
Annette Cryer ◽  
Anke Wussow ◽  
Christian Peiser ◽  
...  

Author(s):  
Thi Nga Nguyen ◽  
Hideaki Suzuki ◽  
Jun-ichi Ohkubo ◽  
Tetsuro Wakasugi ◽  
Takuro Kitamura

<b><i>Background:</i></b> The ciliary beat of the airway epithelium, including the sinonasal epithelium, has a significant role in frontline defense and is thought to be controlled by the level of intracellular Ca<sup>2+</sup>. Involvement of calmodulin and adenylate/guanylate cyclases in the regulation of ciliary beats has been reported, and here we investigated the interrelation between these components of the ciliary beat regulatory pathway. <b><i>Methods:</i></b> The inferior turbinates were collected from 29 patients with chronic hypertrophic rhinitis/rhinosinusitis during endoscopic sinonasal surgery. The turbinate mucosa was cut into thin strips, and mucociliary movement was observed under a phase-contrast light microscope equipped with a high-speed digital video camera. <b><i>Results:</i></b> The ciliary beat frequency (CBF) was significantly increased by stimulation with 100 μM CALP3 (calmodulin agonist), which was completely suppressed by adding 100 µM SQ22536 (adenylate cyclase inhibitor) and 10 µM ODQ (guanylate cyclase inhibitor) together and by adding 1 µM KT5720 (protein kinase A inhibitor) and 1 µM KT5823 (protein kinase G inhibitor) together. The CBF was significantly increased by stimulation with 10 µM forskolin (adenylate cyclase activator) and 10 µM BAY41-2272 (guanylate cyclase activator) and by stimulation with 100 µM 8-bromo-cAMP (cAMP analog) and 100 µM 8-bromo-cGMP (cGMP analog), which was not changed by adding 1 µM calmidazolium (calmodulin antagonist). <b><i>Conclusions:</i></b> These results confirmed that the regulatory pathway of ciliary beats in the human nasal mucosa involves calmodulin, adenylate/guanylate cyclases, and protein kinases A/G and indicate that adenylate/guanylate cyclases and protein kinases A/G act downstream of calmodulin, but not vice versa, and that these cyclases relay calmodulin signaling.


1992 ◽  
Vol 89 (5) ◽  
pp. 1032-1039 ◽  
Author(s):  
J BARANIUK ◽  
P SILVER ◽  
M KALINER ◽  
P BARNES

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