Novel Fusion Protein Constructs Targeting DNA Repair Enzymes To Mitochondria Protect Against Pseudomonas Aeruginosa-Induced Acute Lung Injury In Intact Rats

2011 ◽  
Author(s):  
Joshua Chouteau ◽  
Olena Gorodnya ◽  
Mykhaylo Ruchko ◽  
Boniface Obiako ◽  
Glenn Wilson ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Dna Repair ◽  
Acute Lung Injury ◽  
Lung Injury ◽  
Fusion Protein ◽  
Dna Repair Enzymes ◽  
Repair Enzymes ◽  
Intact Rats ◽  
Protein Constructs

scholarly journals Mitochondrial DNA repair enzymes attenuate ventilator induced lung injury

2011 ◽  
Vol 25 (S1) ◽  
Author(s):  
Masahiro Hashizume ◽  
Marc Mouner ◽  
Mark Gillespie ◽  
Joshua Chouteau ◽  
James C. Parker
Keyword(s):  
Dna Repair ◽  
Mitochondrial Dna ◽  
Lung Injury ◽  
Dna Repair Enzymes ◽  
Repair Enzymes ◽  
Ventilator Induced Lung Injury ◽  
Mitochondrial Dna Repair

scholarly journals DASH-type cryptochromes – solved and open questions

2020 ◽  
Vol 401 (12) ◽  
pp. 1487-1493
Author(s):  
Stephan Kiontke ◽  
Tanja Göbel ◽  
Annika Brych ◽  
Alfred Batschauer
Keyword(s):  
Dna Repair ◽  
Circadian Clock ◽  
Blue Light ◽  
Dna Repair Enzymes ◽  
Repair Enzymes ◽  
Open Questions ◽  
Essential Components ◽  
Repair Activity ◽  
Almost All ◽  
Uv Lesions

AbstractDrosophila, Arabidopsis, Synechocystis, human (DASH)-type cryptochromes (cry-DASHs) form one subclade of the cryptochrome/photolyase family (CPF). CPF members are flavoproteins that act as DNA-repair enzymes (DNA-photolyases), or as ultraviolet(UV)-A/blue light photoreceptors (cryptochromes). In mammals, cryptochromes are essential components of the circadian clock feed-back loop. Cry-DASHs are present in almost all major taxa and were initially considered as photoreceptors. Later studies demonstrated DNA-repair activity that was, however, restricted to UV-lesions in single-stranded DNA. Very recent studies, particularly on microbial organisms, substantiated photoreceptor functions of cry-DASHs suggesting that they could be transitions between photolyases and cryptochromes.

PcrV antibody protects multi-drug resistant Pseudomonas aeruginosa induced acute lung injury

2014 ◽  
Vol 193 ◽  
pp. 21-28 ◽  
Author(s):  
Qin Wang ◽  
Huayin Li ◽  
Jian Zhou ◽  
Ming Zhong ◽  
Duming Zhu ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Acute Lung Injury ◽  
Lung Injury ◽  
Drug Resistant

scholarly journals Effects of Antibiotic Therapy on Pseudomonas aeruginosa-Induced Lung Injury in a Rat Model

1999 ◽  
Vol 43 (10) ◽  
pp. 2389-2394 ◽  
Author(s):  
Erika J. Ernst ◽  
Satoru Hashimoto ◽  
Joseph Guglielmo ◽  
Teiji Sawa ◽  
Jean-Francois Pittet ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Acute Lung Injury ◽  
Lung Injury ◽  
Rat Model ◽  
In Vivo Model ◽  
Antibiotic Administration ◽  
Lung Water ◽  
Alveolar Epithelial ◽  
The Right

ABSTRACT The effect of antibiotics on the acute lung injury induced by virulent Pseudomonas aeruginosa PA103 was quantitatively analyzed in a rat model. Lung injury was induced by the instillation of PA103 directly into the right lower lobes of the lungs of anesthetized rats. The alveolar epithelial injury, extravascular lung water, and total plasma equivalents were measured as separate, independent parameters of acute lung injury. Four hours after the instillation of PA103, all the parameters were increased linearly depending on the dose of P. aeruginosa. Next, we examined the effects of intravenously administered antibiotics on the parameters of acute lung injury in d-galactosamine-sensitized rats. One hour after the rats received 107 CFU of PA103, an intravenous bolus injection of aztreonam (60 mg/kg) or imipenem-cilastatin (30 mg/kg) was administered. Despite an MIC indicating resistance, imipenem-cilastatin improved all the measurements of lung injury; in contrast, aztreonam, which had an MIC indicating sensitivity, did not improve any of the lung injury parameters. The antibiotics did not generate different quantities of plasma endotoxin; therefore, endotoxin did not appear to explain the differences in lung injury. This in vivo model is useful to quantitatively compare the efficacies of parenteral antibiotic administration on Pseudomonas airspace infections.

DNA Repair Enzymes in Mammalian Cells

1977 ◽  
pp. 263-322 ◽  
Author(s):  
Errol C. Friedberg ◽  
Kern H. Cook ◽  
James Duncan ◽  
Kristien Mortelmans
Keyword(s):  
Dna Repair ◽  
Mammalian Cells ◽  
Dna Repair Enzymes ◽  
Repair Enzymes

scholarly journals DNA damage shifts circadian clock time via Hausp-dependent Cry1 stabilization

eLife ◽  
2015 ◽  
Vol 4 ◽  
Author(s):  
Stephanie J Papp ◽  
Anne-Laure Huber ◽  
Sabine D Jordan ◽  
Anna Kriebs ◽  
Madelena Nguyen ◽  
...  
Keyword(s):  
Dna Damage ◽  
Dna Repair ◽  
Circadian Clock ◽  
Transcriptional Response ◽  
Genotoxic Stress ◽  
Genomic Integrity ◽  
Clock Time ◽  
Dna Repair Enzymes ◽  
Repair Enzymes ◽  
Specific Protease

The circadian transcriptional repressors cryptochrome 1 (Cry1) and 2 (Cry2) evolved from photolyases, bacterial light-activated DNA repair enzymes. In this study, we report that while they have lost DNA repair activity, Cry1/2 adapted to protect genomic integrity by responding to DNA damage through posttranslational modification and coordinating the downstream transcriptional response. We demonstrate that genotoxic stress stimulates Cry1 phosphorylation and its deubiquitination by Herpes virus associated ubiquitin-specific protease (Hausp, a.k.a Usp7), stabilizing Cry1 and shifting circadian clock time. DNA damage also increases Cry2 interaction with Fbxl3, destabilizing Cry2. Thus, genotoxic stress increases the Cry1/Cry2 ratio, suggesting distinct functions for Cry1 and Cry2 following DNA damage. Indeed, the transcriptional response to genotoxic stress is enhanced in Cry1−/− and blunted in Cry2−/− cells. Furthermore, Cry2−/− cells accumulate damaged DNA. These results suggest that Cry1 and Cry2, which evolved from DNA repair enzymes, protect genomic integrity via coordinated transcriptional regulation.

scholarly journals Structural and cellular analyses of cancer-associated mutations in DNA repair enzymes

2019 ◽  
Vol 75 (a1) ◽  
pp. a327-a327
Author(s):  
Brian E. Eckenroth ◽  
Ash Prakash ◽  
Brittany L. Carroll ◽  
Joann B. Sweasy ◽  
Sylvie Doublié
Keyword(s):  
Dna Repair ◽  
Dna Repair Enzymes ◽  
Repair Enzymes
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