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Article ; Online: Inhaled delivery of a lipid nanoparticle encapsulated messenger RNA encoding a ciliary protein for the treatment of primary ciliary dyskinesia.

Woo, Caroline J / Allawzi, Ayed / Clark, Nicholas / Kaushal, Neha / Efthymiou, Tim / Thamsen, Maike / Nguyen, Jane / Wooster, Richard / Sullivan, James C

Pulmonary pharmacology & therapeutics

2022 Volume 75, Page(s) 102134

Abstract: Primary ciliary dyskinesia (PCD) is a respiratory disease caused by dysfunction of the cilia with currently no approved treatments. This predominantly autosomal recessive disease is caused by mutations in any one of over 50 genes involved in cilia ... ...

Abstract	Primary ciliary dyskinesia (PCD) is a respiratory disease caused by dysfunction of the cilia with currently no approved treatments. This predominantly autosomal recessive disease is caused by mutations in any one of over 50 genes involved in cilia function; DNAI1 is one of the more frequently mutated genes, accounting for approximately 5-10% of diagnosed PCD cases. A codon-optimized mRNA encoding DNAI1 and encapsulated in a lipid nanoparticle (LNP) was administered to mice via aerosolized inhalation resulting in the expression human DNAI1 in the multiciliated cells of the pseudostratified columnar epithelia. The spatial localization of DNAI1 expression in the bronchioles indicate that delivery of the DNAI1 mRNA transpires the lower airways. In a PCD disease model, exposure to the LNP-encapsulated DNAI1 mRNA resulted in increased ciliary beat frequency using high speed videomicroscopy showing the potential for an mRNA therapeutic to correct cilia function in patients with PCD due to DNAI1 mutations.
MeSH term(s)	Animals ; Axonemal Dyneins/genetics ; Cilia ; Humans ; Kartagener Syndrome/diagnosis ; Kartagener Syndrome/drug therapy ; Kartagener Syndrome/genetics ; Liposomes ; Mice ; Mutation ; Nanoparticles ; RNA, Messenger
Chemical Substances	Lipid Nanoparticles ; Liposomes ; RNA, Messenger ; Axonemal Dyneins (EC 3.6.4.2)
Language	English
Publishing date	2022-05-22
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1399707-5
ISSN	1522-9629 ; 1094-5539
ISSN (online)	1522-9629
ISSN	1094-5539
DOI	10.1016/j.pupt.2022.102134
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Article ; Online: IRE1α drives lung epithelial progenitor dysfunction to establish a niche for pulmonary fibrosis.

Auyeung, Vincent C / Downey, Michael S / Thamsen, Maike / Wenger, Talia A / Backes, Bradley J / Sheppard, Dean / Papa, Feroz R

American journal of physiology. Lung cellular and molecular physiology

2022 Volume 322, Issue 4, Page(s) L564–L580

Abstract: After lung injury, damage-associated transient progenitors (DATPs) emerge, representing a transitional state between injured epithelial cells and newly regenerated alveoli. DATPs express profibrotic genes, suggesting that they might promote idiopathic ... ...

Abstract	After lung injury, damage-associated transient progenitors (DATPs) emerge, representing a transitional state between injured epithelial cells and newly regenerated alveoli. DATPs express profibrotic genes, suggesting that they might promote idiopathic pulmonary fibrosis (IPF). However, the molecular pathways that induce and/or maintain DATPs are incompletely understood. Here we show that the bifunctional kinase/RNase-IRE1α-a central mediator of the unfolded protein response (UPR) to endoplasmic reticulum (ER) stress is a critical promoter of DATP abundance and function. Administration of a nanomolar-potent, monoselective kinase inhibitor of IRE1α (KIRA8)-or conditional epithelial IRE1α gene knockout-both reduce DATP cell number and fibrosis in the bleomycin model, indicating that IRE1α cell-autonomously promotes transition into the DATP state. IRE1α enhances the profibrotic phenotype of DATPs since KIRA8 decreases expression of integrin αvβ6, a key activator of transforming growth factor β (TGF-β) in pulmonary fibrosis, corresponding to decreased TGF-β-induced gene expression in the epithelium and decreased collagen accumulation around DATPs. Furthermore, IRE1α regulates DNA damage response (DDR) signaling, previously shown to promote the DATP phenotype, as IRE1α loss-of-function decreases H2AX phosphorylation,
MeSH term(s)	Apoptosis/physiology ; Endoplasmic Reticulum Stress/physiology ; Endoribonucleases/metabolism ; Humans ; Idiopathic Pulmonary Fibrosis/metabolism ; Lung/metabolism ; Protein Serine-Threonine Kinases/genetics
Chemical Substances	Protein Serine-Threonine Kinases (EC 2.7.11.1) ; Endoribonucleases (EC 3.1.-)
Language	English
Publishing date	2022-02-16
Publishing country	United States
Document type	Journal Article
ZDB-ID	1013184-x
ISSN	1522-1504 ; 1040-0605
ISSN (online)	1522-1504
ISSN	1040-0605
DOI	10.1152/ajplung.00408.2021
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Zs.A 2749: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)

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Book ; Online ; Thesis: The role of oxidative stress in C. elegans aging

Thamsen, Maike [Verfasser]

2011

Author's details	Maike Thamsen
Keywords	Naturwissenschaften ; Science
Subject code	sg500
Language	English
Document type	Book ; Online ; Thesis
Database	Digital theses on the web

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Article ; Online: The redoxome: Proteomic analysis of cellular redox networks.

Thamsen, Maike / Jakob, Ursula

Current opinion in chemical biology

2010 Volume 15, Issue 1, Page(s) 113–119

Abstract: Redox-regulated proteins play fundamentally important roles not only during the defense of organisms against oxidative stress conditions but also as targets of cellular signaling events. This realization has spurred the development of proteomic ... ...

Abstract	Redox-regulated proteins play fundamentally important roles not only during the defense of organisms against oxidative stress conditions but also as targets of cellular signaling events. This realization has spurred the development of proteomic techniques geared towards characterizing the redoxome; proteins with highly reactive cysteine residues, whose thiol oxidation state controls the function of the proteins, and by extension, the pathways they are part of. We will here summarize the most recent advances made in the field of redox proteomic analysis, aimed to elucidate the cellular redox networks that appear to control prokaryotic and eukaryotic organisms.
MeSH term(s)	Biotin/chemistry ; Homeostasis ; Humans ; Oxidation-Reduction ; Proteome/chemistry ; Proteomics/methods ; Sulfenic Acids/chemistry
Chemical Substances	Proteome ; Sulfenic Acids ; Biotin (6SO6U10H04)
Language	English
Publishing date	2010-12-02
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	1439176-4
ISSN	1879-0402 ; 1367-5931
ISSN (online)	1879-0402
ISSN	1367-5931
DOI	10.1016/j.cbpa.2010.11.013
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Article: The redoxome Proteomic analysis of cellular redox networks

Thamsen, Maike / Jakob, Ursula

Current Opinion in Chemical Biology. 2011 Feb., v. 15, no. 1

2011

Abstract	Redox-regulated proteins play fundamentally important roles not only during the defense of organisms against oxidative stress conditions but also as targets of cellular signaling events. This realization has spurred the development of proteomic techniques geared towards characterizing the redoxome; proteins with highly reactive cysteine residues, whose thiol oxidation state controls the function of the proteins, and by extension, the pathways they are part of. We will here summarize the most recent advances made in the field of redox proteomic analysis, aimed to elucidate the cellular redox networks that appear to control prokaryotic and eukaryotic organisms.
Keywords	cysteine ; oxidation ; oxidative stress ; proteins ; proteomics ; thiols
Language	English
Dates of publication	2011-02
Size	p. 113-119.
Publishing place	Elsevier Ltd
Document type	Article
ZDB-ID	1439176-4
ISSN	1879-0402 ; 1367-5931
ISSN (online)	1879-0402
ISSN	1367-5931
DOI	10.1016/j.cbpa.2010.11.013
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Drug-induced skin toxicity: gaps in preclinical testing cascade as opportunities for complex in vitro models and assays.

Hardwick, Rhiannon N / Betts, Catherine J / Whritenour, Jessica / Sura, Radhakrishna / Thamsen, Maike / Kaufman, Elad H / Fabre, Kristin

Lab on a chip

2019 Volume 20, Issue 2, Page(s) 199–214

Abstract: Skin is the largest organ of the body and serves as the principle barrier to the environment. Composed of multiple cell types arranged in stratified layers with highly specialized appendages, it serves sensory and immune surveillance roles in addition to ...

Abstract	Skin is the largest organ of the body and serves as the principle barrier to the environment. Composed of multiple cell types arranged in stratified layers with highly specialized appendages, it serves sensory and immune surveillance roles in addition to its primary mechanical function. Several complex in vitro models of skin (i.e. microphysiological systems (MPS) including but not limited to 3D tissues, organ-on-a-chip, organoids), have been developed and assays validated for regulatory purposes. As such, skin is arguably the most advanced organ with respect to model development and adoption across industries including chemical, cosmetic, and to a somewhat lesser extent, pharmaceutical. Early adoption of complex skin models and associated assays for assessment of irritation and corrosion spurred research into other areas such as sensitization, absorption, phototoxicity, and genotoxicity. Despite such considerable advancements, opportunities remain for immune capabilities, inclusion of appendages such as hair follicles, fluidics, and innervation, among others. Herein, we provide an overview of current complex skin model capabilities and limitations within the drug development scheme, and recommendations for future model development and assay qualification and/or validation with the intent to facilitate wider adoption of use within the pharmaceutical industry.
MeSH term(s)	Animals ; Drug Development ; Drug Industry ; Humans ; Lab-On-A-Chip Devices ; Models, Biological ; Pharmaceutical Preparations/chemistry ; Skin/drug effects
Chemical Substances	Pharmaceutical Preparations
Language	English
Publishing date	2019-10-10
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	2056646-3
ISSN	1473-0189 ; 1473-0197
ISSN (online)	1473-0189
ISSN	1473-0197
DOI	10.1039/c9lc00519f
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Article ; Online: Is overoxidation of peroxiredoxin physiologically significant?

Thamsen, Maike / Kumsta, Caroline / Li, Fei / Jakob, Ursula

Antioxidants & redox signaling

2010 Volume 14, Issue 4, Page(s) 725–730

Abstract: Eukaryotic peroxiredoxins are highly susceptible to sulfinic acid formation. This overoxidation, which is thought to convert peroxiredoxins into chaperones, can be reversed by sulfiredoxins. Several organisms, including Caenorhabditis elegans, lack ... ...

Abstract	Eukaryotic peroxiredoxins are highly susceptible to sulfinic acid formation. This overoxidation, which is thought to convert peroxiredoxins into chaperones, can be reversed by sulfiredoxins. Several organisms, including Caenorhabditis elegans, lack sulfiredoxins but encode sestrins, proteins proposed to be functionally equivalent. We induced peroxiredoxin overoxidation in C. elegans with a short peroxide pulse. We found that reduction of overoxidized peroxiredoxin 2 (PRDX-2) was extremely slow and sestrin-independent, strongly implying that worms lack an efficient repair system. Analysis of PRDX-2's overoxidation status during C. elegans lifespan revealed no accumulation of overoxidized PRDX-2 at any point, questioning whether PRDX-2 overoxidation in worms is physiologically relevant.
MeSH term(s)	Animals ; Caenorhabditis elegans/drug effects ; Caenorhabditis elegans/metabolism ; Caenorhabditis elegans Proteins/metabolism ; Humans ; Oxidation-Reduction/drug effects ; Peroxides/pharmacology ; Peroxiredoxins/metabolism
Chemical Substances	Caenorhabditis elegans Proteins ; Peroxides ; PRDX-2 protein, C elegans (EC 1.11.1.15) ; Peroxiredoxins (EC 1.11.1.15)
Language	English
Publishing date	2010-12-17
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1483836-9
ISSN	1557-7716 ; 1523-0864
ISSN (online)	1557-7716
ISSN	1523-0864
DOI	10.1089/ars.2010.3717
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Article ; Online: Effects of oxidative stress on behavior, physiology, and the redox thiol proteome of Caenorhabditis elegans.

Kumsta, Caroline / Thamsen, Maike / Jakob, Ursula

Antioxidants & redox signaling

2010 Volume 14, Issue 6, Page(s) 1023–1037

Abstract: Accumulation of reactive oxygen species has been implicated in various diseases and aging. However, the precise physiological effects of accumulating oxidants are still largely undefined. Here, we applied a short-term peroxide stress treatment to young ... ...

Abstract	Accumulation of reactive oxygen species has been implicated in various diseases and aging. However, the precise physiological effects of accumulating oxidants are still largely undefined. Here, we applied a short-term peroxide stress treatment to young Caenorhabditis elegans and measured behavioral, physiological, and cellular consequences. We discovered that exposure to peroxide stress causes a number of immediate changes, including loss in mobility, decreased growth rate, and decreased cellular adenosine triphosphate levels. Many of these alterations, which are highly reminiscent of changes in aging animals, are reversible, suggesting the presence of effective antioxidant systems in young C. elegans. One of these antioxidant systems involves the highly abundant protein peroxiredoxin 2 (PRDX-2), whose gene deletion causes phenotypes symptomatic of chronic peroxide stress and shortens lifespan. Applying the quantitative redox proteomic technique OxICAT to oxidatively stressed wild-type and prdx-2 deletion worms, we identified oxidation-sensitive cysteines in 40 different proteins, including proteins involved in mobility and feeding (e.g., MYO-2 and LET-75), protein translation and homeostasis (e.g., elongation factor 1 [EFT-1] and heat shock protein 1), and adenosine triphosphate regeneration (e.g., nucleoside diphosphate kinase). The oxidative modification of some of these redox-sensitive cysteines may contribute to the physiological and behavioral changes observed in oxidatively stressed animals.
MeSH term(s)	Animals ; Caenorhabditis elegans/drug effects ; Caenorhabditis elegans/metabolism ; Caenorhabditis elegans Proteins/genetics ; Caenorhabditis elegans Proteins/metabolism ; Oxidation-Reduction/drug effects ; Oxidative Stress/drug effects ; Oxidative Stress/genetics ; Peroxides/pharmacology ; Proteome
Chemical Substances	Caenorhabditis elegans Proteins ; Peroxides ; Proteome
Language	English
Publishing date	2010-10-28
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1483836-9
ISSN	1557-7716 ; 1523-0864
ISSN (online)	1557-7716
ISSN	1523-0864
DOI	10.1089/ars.2010.3203
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Article ; Online: Small molecule inhibition of IRE1α kinase/RNase has anti-fibrotic effects in the lung.

Thamsen, Maike / Ghosh, Rajarshi / Auyeung, Vincent C / Brumwell, Alexis / Chapman, Harold A / Backes, Bradley J / Perara, Gayani / Maly, Dustin J / Sheppard, Dean / Papa, Feroz R

PloS one

2019 Volume 14, Issue 1, Page(s) e0209824

Abstract: Endoplasmic reticulum stress (ER stress) has been implicated in the pathogenesis of idiopathic pulmonary fibrosis (IPF), a disease of progressive fibrosis and respiratory failure. ER stress activates a signaling pathway called the unfolded protein ... ...

Abstract	Endoplasmic reticulum stress (ER stress) has been implicated in the pathogenesis of idiopathic pulmonary fibrosis (IPF), a disease of progressive fibrosis and respiratory failure. ER stress activates a signaling pathway called the unfolded protein response (UPR) that either restores homeostasis or promotes apoptosis. The bifunctional kinase/RNase IRE1α is a UPR sensor/effector that promotes apoptosis if ER stress remains high and irremediable (i.e., a "terminal" UPR). Using multiple small molecule inhibitors against IRE1α, we show that ER stress-induced apoptosis of murine alveolar epithelial cells can be mitigated in vitro. In vivo, we show that bleomycin exposure to murine lungs causes early ER stress to activate IRE1α and the terminal UPR prior to development of pulmonary fibrosis. Small-molecule IRE1α kinase-inhibiting RNase attenuators (KIRAs) that we developed were used to evaluate the contribution of IRE1α activation to bleomycin-induced pulmonary fibrosis. One such KIRA-KIRA7-provided systemically to mice at the time of bleomycin exposure decreases terminal UPR signaling and prevents lung fibrosis. Administration of KIRA7 14 days after bleomycin exposure even promoted the reversal of established fibrosis. Finally, we show that KIRA8, a nanomolar-potent, monoselective KIRA compound derived from a completely different scaffold than KIRA7, likewise promoted reversal of established fibrosis. These results demonstrate that IRE1α may be a promising target in pulmonary fibrosis and that kinase inhibitors of IRE1α may eventually be developed into efficacious anti-fibrotic drugs.
MeSH term(s)	Alveolar Epithelial Cells/drug effects ; Alveolar Epithelial Cells/metabolism ; Alveolar Epithelial Cells/pathology ; Animals ; Apoptosis/drug effects ; Cell Line ; Endoplasmic Reticulum Stress/drug effects ; Endoribonucleases/antagonists & inhibitors ; Fibrosis/drug therapy ; Fibrosis/metabolism ; Fibrosis/pathology ; Lung/drug effects ; Lung/metabolism ; Lung/pathology ; Mice ; Protein Kinase Inhibitors/pharmacology ; Protein Kinase Inhibitors/therapeutic use ; Protein-Serine-Threonine Kinases/antagonists & inhibitors ; Unfolded Protein Response/drug effects
Chemical Substances	Protein Kinase Inhibitors ; Ern1 protein, mouse (EC 2.7.11.1) ; Protein-Serine-Threonine Kinases (EC 2.7.11.1) ; Endoribonucleases (EC 3.1.-)
Language	English
Publishing date	2019-01-09
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0209824
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Small molecule inhibition of IRE1α kinase/RNase has anti-fibrotic effects in the lung.

Maike Thamsen / Rajarshi Ghosh / Vincent C Auyeung / Alexis Brumwell / Harold A Chapman / Bradley J Backes / Gayani Perara / Dustin J Maly / Dean Sheppard / Feroz R Papa

PLoS ONE, Vol 14, Iss 1, p e

2019 Volume 0209824

Abstract	Endoplasmic reticulum stress (ER stress) has been implicated in the pathogenesis of idiopathic pulmonary fibrosis (IPF), a disease of progressive fibrosis and respiratory failure. ER stress activates a signaling pathway called the unfolded protein response (UPR) that either restores homeostasis or promotes apoptosis. The bifunctional kinase/RNase IRE1α is a UPR sensor/effector that promotes apoptosis if ER stress remains high and irremediable (i.e., a "terminal" UPR). Using multiple small molecule inhibitors against IRE1α, we show that ER stress-induced apoptosis of murine alveolar epithelial cells can be mitigated in vitro. In vivo, we show that bleomycin exposure to murine lungs causes early ER stress to activate IRE1α and the terminal UPR prior to development of pulmonary fibrosis. Small-molecule IRE1α kinase-inhibiting RNase attenuators (KIRAs) that we developed were used to evaluate the contribution of IRE1α activation to bleomycin-induced pulmonary fibrosis. One such KIRA-KIRA7-provided systemically to mice at the time of bleomycin exposure decreases terminal UPR signaling and prevents lung fibrosis. Administration of KIRA7 14 days after bleomycin exposure even promoted the reversal of established fibrosis. Finally, we show that KIRA8, a nanomolar-potent, monoselective KIRA compound derived from a completely different scaffold than KIRA7, likewise promoted reversal of established fibrosis. These results demonstrate that IRE1α may be a promising target in pulmonary fibrosis and that kinase inhibitors of IRE1α may eventually be developed into efficacious anti-fibrotic drugs.
Keywords	Medicine ; R ; Science ; Q
Subject code	610
Language	English
Publishing date	2019-01-01T00:00:00Z
Publisher	Public Library of Science (PLoS)
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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