Use of microgravity bioreactors for development of an in vitro rat salivary gland cell culture model

1993 ◽  
Vol 51 (3) ◽  
pp. 265-273 ◽  
Author(s):  
Marian L. Lewis ◽  
Debra M. Moriarity ◽  
P. Samuel Campbell
2004 ◽  
Vol 171 (4S) ◽  
pp. 295-295
Author(s):  
Fernando C. Delvecchio ◽  
Ricardo M. Brizuela ◽  
Karen J. Byer ◽  
W. Patrick Springhart ◽  
Saeed R. Khan ◽  
...  

Pathogens ◽  
2020 ◽  
Vol 10 (1) ◽  
pp. 9
Author(s):  
Donghoon Kang ◽  
Natalia V. Kirienko

Pseudomonas aeruginosa is a multidrug-resistant, opportunistic pathogen that utilizes a wide-range of virulence factors to cause acute, life-threatening infections in immunocompromised patients, especially those in intensive care units. It also causes debilitating chronic infections that shorten lives and worsen the quality of life for cystic fibrosis patients. One of the key virulence factors in P. aeruginosa is the siderophore pyoverdine, which provides the pathogen with iron during infection, regulates the production of secreted toxins, and disrupts host iron and mitochondrial homeostasis. These roles have been characterized in model organisms such as Caenorhabditis elegans and mice. However, an intermediary system, using cell culture to investigate the activity of this siderophore has been absent. In this report, we describe such a system, using murine macrophages treated with pyoverdine. We demonstrate that pyoverdine-rich filtrates from P. aeruginosa exhibit substantial cytotoxicity, and that the inhibition of pyoverdine production (genetic or chemical) is sufficient to mitigate virulence. Furthermore, consistent with previous observations made in C. elegans, pyoverdine translocates into cells and disrupts host mitochondrial homeostasis. Most importantly, we observe a strong correlation between pyoverdine production and virulence in P. aeruginosa clinical isolates, confirming pyoverdine’s value as a promising target for therapeutic intervention. This in vitro cell culture model will allow rapid validation of pyoverdine antivirulents in a simple but physiologically relevant manner.


2013 ◽  
Vol 45 (4) ◽  
pp. 325 ◽  
Author(s):  
Anurupa Maitra ◽  
Shahnaz Patel ◽  
VijayR Bhate ◽  
VilliS Toddywalla ◽  
MaithiliA Athavale

PLoS ONE ◽  
2012 ◽  
Vol 7 (4) ◽  
pp. e35008 ◽  
Author(s):  
Elhaseen Elamin ◽  
Daisy Jonkers ◽  
Kati Juuti-Uusitalo ◽  
Sven van IJzendoorn ◽  
Freddy Troost ◽  
...  

2019 ◽  
Vol 64 (2) ◽  
pp. 112-123 ◽  
Author(s):  
Teruo Miyazaki ◽  
Akira Honda ◽  
Tadashi Ikegami ◽  
Takashi Iida ◽  
Yasushi Matsuzaki

2011 ◽  
Vol 113 (6) ◽  
pp. 1468-1475 ◽  
Author(s):  
Jun Zhang ◽  
Yuanlin Dong ◽  
Zhipeng Xu ◽  
Yiying Zhang ◽  
Chuxiong Pan ◽  
...  

2019 ◽  
Vol 39 (2) ◽  
Author(s):  
Swarna Mathre ◽  
K. Balasankara Reddy ◽  
Visvanathan Ramya ◽  
Harini Krishnan ◽  
Avishek Ghosh ◽  
...  

Abstract Phosphatidylinositol 5 phosphate 4-kinase (PIP4K) are enzymes that catalyse the phosphorylation of phosphatidylinositol 5-phosphate (PI5P) to generate PI(4,5)P2. Mammalian genomes contain three genes, PIP4K2Α, 2B and 2C and murine knockouts for these suggested important physiological roles in vivo. The proteins encoded by PIP4K2A, 2B and 2C show widely varying specific activities in vitro; PIP4K2A is highly active and PIP4K2C 2000-times less active, and the relationship between this biochemical activity and in vivo function is unknown. By contrast, the Drosophila genome encodes a single PIP4K (dPIP4K) that shows high specific activity in vitro and loss of this enzyme results in reduced salivary gland cell size in vivo. We find that the kinase activity of dPIP4K is essential for normal salivary gland cell size in vivo. Despite their highly divergent specific activity, we find that all three mammalian PIP4K isoforms are able to enhance salivary gland cell size in the Drosophila PIP4K null mutant implying a lack of correlation between in vitro activity measurements and in vivo function. Further, the kinase activity of PIP4K2C, reported to be almost inactive in vitro, is required for in vivo function. Our findings suggest the existence of unidentified factors that regulate PIP4K enzyme activity in vivo.


2015 ◽  
Vol 53 (1) ◽  
pp. 66-72 ◽  
Author(s):  
Robert Duliński ◽  
◽  
Emilia Katarzyna Cielecka ◽  
Małgorzata Pierzchalska ◽  
Krzysztof Żyła ◽  
...  

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