scholarly journals THE LOCALIZATION OF SUCCINIC DEHYDROGENASE, CYTOCHROME OXIDASE AND ADENOSINE TRIPHOSPHATASE IN CILIATED RESPIRATORY EPITHELIUM

1965 ◽  
Vol 13 (8) ◽  
pp. 677-683 ◽  
Author(s):  
HERTHA R. CRESS ◽  
ALEXANDER SPOCK ◽  
DUNCAN C. HEATHERINGTON
Keyword(s):  
Cytochrome Oxidase ◽  
Adenosine Triphosphatase ◽  
Succinic Dehydrogenase ◽  
Respiratory Epithelium ◽  
Ciliary Activity ◽  
Basal Bodies ◽  
Tissue Cultures ◽  
Respiratory Epithelial Cells ◽  
Respiratory Epithelial

Succinic dehydrogenase and cytochrome oxidase activities were found to be scattered throughout the cytoplasm of ciliated and nonciliated respiratory epithelial cells while ATPase activity was restricted to cilia and areas under the cilia in the regions of the ciliary basal bodies. In order to elucidate the role of ATPase further, tissue cultures of rabbit tracheal epithelium with beating cilia were incubated in a medium perfused with cigarette smoke which resulted in cessation of ciliary motility. Epithelium with beating cilia was positive for ATPase while the epithelium with nonbeating cilia was negative or only weakly positive in a few small scattered areas. The presence of ATPase in beating cilia and its absence in nonbeating cilia agree with biochemical and physiological studies suggesting an association between ATP and ciliary activity.

Inhibition of alveolarization and altered pulmonary mechanics in mice expressing GATA-6

2003 ◽  
Vol 285 (6) ◽  
pp. L1246-L1254 ◽  
Author(s):  
Cong Liu ◽  
Machiko Ikegami ◽  
Mildred T. Stahlman ◽  
Chitta R. Dey ◽  
Jeffrey A. Whitsett
Keyword(s):  
Epithelial Cells ◽  
Surfactant Protein ◽  
Mouse Lung ◽  
Pulmonary Mechanics ◽  
Respiratory Epithelial Cells ◽  
Surfactant Protein C ◽  
Spatial Regulation ◽  
Respiratory Epithelial ◽  
Tissue Elastance

GATA-6, a member of a family of zinc finger transcription factors, is expressed in epithelial cells of the developing lung. To further assess the role of GATA-6 in lung morphogenesis, GATA-6 was expressed in respiratory epithelial cells of the developing mouse lung under control of the surfactant protein C promoter (hSP-CGATA-6 mice). Although GATA-6 did not alter lung morphology at embryonic day 18.5, defects in alveolar septation were observed early in the neonatal period, and air space enlargement persisted to adulthood. Airway resistance, airway elastance, tissue damping, and tissue elastance were significantly decreased, and lung volumes were significantly increased at 12 wk of age. Normal postnatal morphogenesis of the lung depends upon precise temporal-spatial regulation of GATA-6.

Murine Tracheal and Nasal Septal Epithelium for Air–Liquid Interface Cultures: A Comparative Study

2007 ◽  
Vol 21 (5) ◽  
pp. 533-537 ◽  
Author(s):  
Bradford A. Woodworth ◽  
Marcelo B. Antunes ◽  
Geeta Bhargave ◽  
James N. Palmer ◽  
Noam A. Cohen
Keyword(s):  
Epithelial Cells ◽  
Respiratory Epithelium ◽  
Liquid Interface ◽  
Respiratory Epithelial Cells ◽  
Cell Counts ◽  
Total Cell Population ◽  
Respiratory Epithelial ◽  
Air Liquid Interface ◽  
Ciliated Epithelial Cells

Background Air–liquid interface cultures using murine tracheal respiratory epithelium have revolutionized the in vitro study of airway diseases. However, these cultures often are impractical because of the small number of respiratory epithelial cells that can be isolated from the mouse trachea. The ability to study ciliary physiology in vitro is of utmost importance in the research of chronic rhinosinusitis (CRS). Our hypothesis is that the murine nasal septum is a better source of ciliated respiratory epithelium to develop respiratory epithelial air–liquid interface models. Methods Nasal septa and tracheas were harvested from 10 BALB/c mice. The nasal septa were harvested by using a simple and straightforward novel technique. Scanning electron microscopy was performed on all specimens. Cell counts of ciliated respiratory epithelial cells were performed at one standard magnification (1535×). Comparative analysis of proximal and distal trachea, midanterior and midposterior nasal septal epithelium, was performed. Results Independent cell counts revealed highly significant differences in the proportion of cell populations (p < 0.00001). Ciliated cell counts for the trachea (106.9 ± 28) were an average of 38.7% of the total cell population. Nasal septal ciliated epithelial cells (277.5 ± 16) comprised 90.1% of the total cell population. Conclusion To increase the yield of respiratory epithelial cells harvested from mice, we have found that the nasal septum is a far superior source when compared with the trachea. The greater surface area and increased concentration of ciliated epithelial cells has the potential to provide an eightfold increase in epithelial cells for the development of air–liquid interface cultures.

scholarly journals A Role of Epithelial Cells and Virulence Factors in Biofilm Formation by Streptococcus pyogenes In Vitro

2020 ◽  
Vol 88 (10) ◽  
Author(s):  
Feiruz Alamiri ◽  
Yashuan Chao ◽  
Maria Baumgarten ◽  
Kristian Riesbeck ◽  
Anders P. Hakansson
Keyword(s):  
Antibiotic Resistance ◽  
Epithelial Cells ◽  
Virulence Factors ◽  
Streptococcus Pyogenes ◽  
Biofilm Formation ◽  
Model Systems ◽  
Respiratory Epithelial Cells ◽  
Abiotic Surfaces ◽  
Respiratory Epithelial

ABSTRACT Biofilm formation by Streptococcus pyogenes (group A streptococcus [GAS]) in model systems mimicking the respiratory tract is poorly documented. Most studies have been conducted on abiotic surfaces, which poorly represent human tissues. We have previously shown that GAS forms mature and antibiotic-resistant biofilms on physiologically relevant epithelial cells. However, the roles of the substratum, extracellular matrix (ECM) components, and GAS virulence factors in biofilm formation and structure are unclear. In this study, biofilm formation was measured on respiratory epithelial cells and keratinocytes by determining biomass and antibiotic resistance, and biofilm morphology was visualized using scanning electron microscopy. All GAS isolates tested formed biofilms that had similar, albeit not identical, biomass and antibiotic resistance for both cell types. Interestingly, functionally mature biofilms formed more rapidly on keratinocytes but were structurally denser and coated with more ECM on respiratory epithelial cells. The ECM was crucial for biofilm integrity, as protein- and DNA-degrading enzymes induced bacterial release from biofilms. Abiotic surfaces supported biofilm formation, but these biofilms were structurally less dense and organized. No major role for M protein, capsule, or streptolysin O was observed in biofilm formation on epithelial cells, although some morphological differences were detected. NAD-glycohydrolase was required for optimal biofilm formation, whereas streptolysin S and cysteine protease SpeB impaired this process. Finally, no correlation was found between cell adherence or autoaggregation and GAS biofilm formation. Combined, these results provide a better understanding of the role of biofilm formation in GAS pathogenesis and can potentially provide novel targets for future treatments against GAS infections.

scholarly journals Role of Pht Proteins in Attachment of Streptococcus pneumoniae to Respiratory Epithelial Cells

2014 ◽  
Vol 82 (4) ◽  
pp. 1683-1691 ◽  
Author(s):  
Anna Kallio ◽  
Kirsi Sepponen ◽  
Philippe Hermand ◽  
Philippe Denoël ◽  
Fabrice Godfroid ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Bacterial Attachment ◽  
Surface Proteins ◽  
Lung Epithelial Cells ◽  
Host Cells ◽  
Respiratory Epithelial Cells ◽  
Relative Significance ◽  
Mucosal Surfaces ◽  
Respiratory Epithelial

ABSTRACTPneumococcal adherence to mucosal surfaces is a critical step in nasopharyngeal colonization, but so far few pneumococcal adhesins involved in the interaction with host cells have been identified. PhtA, PhtB, PhtD, and PhtE are conserved pneumococcal surface proteins that have proven promising as vaccine candidates. One suggested virulence function of Pht proteins is to mediate adherence at the respiratory mucosa. In this study, we assessed the role of Pht proteins in pneumococcal binding to respiratory epithelial cells. Pneumococci were incubated with human nasopharyngeal epithelial cells (Detroit-562) and lung epithelial cells (A549 and NCI-H292), and the proportion of bound bacteria was measured by plating viable counts. Strains R36A (unencapsulated), D39 (serotype 2), 43 (serotype 3), 4-CDC (serotype 4), and 2737 (serotype 19F) with one or more of the four homologous Pht proteins deleted were compared with their wild-type counterparts. Also, the effect of anti-PhtD antibodies on the adherence of strain 2737 to the respiratory epithelial cells was studied. Our results suggest that Pht proteins play a role in pneumococcal adhesion to the respiratory epithelium. We also found that antibody to PhtD is able to inhibit bacterial attachment to the cells, suggesting that antibodies against PhtD present at mucosal surfaces might protect from pneumococcal attachment and subsequent colonization. However, the relative significance of Pht proteins to the ability of pneumococci to bindin vitroto epithelial cells depends on the genetic background and the capsular serotype of the strain.

scholarly journals Differential Role of CbpA and PspA in Modulation of In Vitro CXC Chemokine Responses of Respiratory Epithelial Cells to Infection with Streptococcus pneumoniae

2006 ◽  
Vol 74 (12) ◽  
pp. 6739-6749 ◽  
Author(s):  
Rikki M. A. Graham ◽  
James C. Paton
Keyword(s):  
Streptococcus Pneumoniae ◽  
Epithelial Cells ◽  
Deletion Mutant ◽  
Protein A ◽  
A549 Cells ◽  
Respiratory Pathogens ◽  
Respiratory Epithelial Cells ◽  
Cxc Chemokine ◽  
Respiratory Epithelial

ABSTRACTRespiratory epithelial cells play an active part in the host response to respiratory pathogens, such asStreptococcus pneumoniae, by releasing chemokines responsible for neutrophil recruitment. In order to investigate the role of specific pneumococcal virulence factors in eliciting CXC chemokine responses, type II pneumocytes (A549) and nasopharyngeal cells (Detroit-562) were infected withS. pneumoniaeD39 or mutants lacking choline-binding protein A (CbpA), pneumococcal surface protein A (PspA), or specific domains thereof. In response to wild-type D39, both A549 and Detroit-562 cells showed a significant increase in CXC chemokine mRNA and interleukin-8 protein. This response was increased twofold when acbpAdeletion mutant (ΔCbpA) was used, suggesting that CbpA inhibits CXC chemokine induction. All three N-terminal domains of CbpA are required for this effect, as in-frame deletion of the respective region ofcbpAhad the same effect on the CXC chemokine response as deletion ofcbpAaltogether. Infection with apspAdeletion mutant (ΔPspA) led to a twofold decrease in the CXC chemokine response of A549 but not Detroit-562 cells, compared to infection with D39 at 2 h. Thus, PspA appears to have the ability to stimulate early CXC chemokine release from A549 cells. Deletion of the region ofpspAencoding the first N-terminal α-helical domain reduced the ability ofS. pneumoniaeto elicit a chemokine response to the same degree as deletion ofpspAaltogether. Thus, the N termini of CbpA and PspA exert differential effects on CXC chemokine induction in epithelial cells infected withS. pneumoniae.

Ciliary Activity in Differentiating and Reactivated Human Respiratory Epithelial Cells

1999 ◽  
Vol 109 (1) ◽  
pp. 103-107 ◽  
Author(s):  
Robert Hard ◽  
Stephen R. Besch ◽  
Deborah Tristram ◽  
Jin Han ◽  
Wesley Hicks
Keyword(s):  
Epithelial Cells ◽  
Ciliary Activity ◽  
Respiratory Epithelial Cells ◽  
Human Respiratory Epithelial Cells ◽  
Respiratory Epithelial

scholarly journals Role of Xanthine Oxidase Activation and Reduced Glutathione Depletion in Rhinovirus Induction of Inflammation in Respiratory Epithelial Cells

2008 ◽  
Vol 283 (42) ◽  
pp. 28595-28606 ◽  
Author(s):  
Alberto Papi ◽  
Marco Contoli ◽  
Pierluigi Gasparini ◽  
Laura Bristot ◽  
Michael R. Edwards ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Xanthine Oxidase ◽  
Reduced Glutathione ◽  
Glutathione Depletion ◽  
Respiratory Epithelial Cells ◽  
Respiratory Epithelial
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