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  1. Article: Genomic evidence for dysregulated glutamine metabolism in the asthmatic airway epithelium.

    Bravo-Solarte, Daniela C / Stelzig, Kimberly E / Cuervo-Pardo, Lyda / Berdnikovs, Sergejs / Chiarella, Sergio E

    Clinical and translational allergy

    2022  Volume 12, Issue 7, Page(s) e12178

    Language English
    Publishing date 2022-07-05
    Publishing country England
    Document type Journal Article
    ZDB-ID 2630865-4
    ISSN 2045-7022
    ISSN 2045-7022
    DOI 10.1002/clt2.12178
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  2. Article ; Online: Passive siRNA transfection method for gene knockdown in air-liquid interface airway epithelial cell cultures.

    Bartman, Colleen M / Stelzig, Kimberly E / Linden, David R / Prakash, Y S / Chiarella, Sergio E

    American journal of physiology. Lung cellular and molecular physiology

    2021  Volume 321, Issue 1, Page(s) L280–L286

    Abstract: Differentiation of human bronchial epithelial cells (HBEs) in air-liquid interface (ALI) cultures recapitulates organotypic modeling of the in vivo environment. Although ALI cultures are invaluable for studying the respiratory epithelial barrier, loss-of- ...

    Abstract Differentiation of human bronchial epithelial cells (HBEs) in air-liquid interface (ALI) cultures recapitulates organotypic modeling of the in vivo environment. Although ALI cultures are invaluable for studying the respiratory epithelial barrier, loss-of-function studies are limited by potentially cytotoxic reagents in classical transfection methods, the length of the differentiation protocol, and the number of primary epithelial cell passages. Here, we present the efficacy and use of a simple method for small interfering RNA (siRNA) transfection of normal HBEs (NHBEs) in ALI cultures that does not require potentially cytotoxic transfection reagents and does not detrimentally alter the physiology or morphology of NHBEs during the differentiation process. This transfection protocol introduces a reproducible and efficient method for loss-of-function studies in HBE ALI cultures that can be leveraged for modeling the respiratory system and airway diseases.
    MeSH term(s) Cell Culture Techniques/methods ; Cell Differentiation ; Cells, Cultured ; Epithelial Cells/cytology ; Epithelial Cells/metabolism ; Gene Expression Regulation ; Gene Knockdown Techniques ; Humans ; RNA, Small Interfering/genetics ; Respiratory Mucosa/cytology ; Respiratory Mucosa/metabolism ; Transfection/methods
    Chemical Substances RNA, Small Interfering
    Language English
    Publishing date 2021-05-26
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 1013184-x
    ISSN 1522-1504 ; 1040-0605
    ISSN (online) 1522-1504
    ISSN 1040-0605
    DOI 10.1152/ajplung.00122.2021
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    In stock of ZB MED Cologne/Königswinter

    Uc I Zs.89: Show issues Location:
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  3. Article ; Online: Estrogen regulates the expression of SARS-CoV-2 receptor ACE2 in differentiated airway epithelial cells.

    Stelzig, Kimberly E / Canepa-Escaro, Fabrizio / Schiliro, Marta / Berdnikovs, Sergejs / Prakash, Y S / Chiarella, Sergio E

    American journal of physiology. Lung cellular and molecular physiology

    2020  Volume 318, Issue 6, Page(s) L1280–L1281

    Abstract: There is marked sexual dimorphism in the current coronavirus disease 2019 (COVID-19) pandemic. Here we report that estrogen can regulate the expression of angiotensin-converting enzyme 2 (ACE2), a key component for severe acute respiratory syndrome ... ...

    Abstract There is marked sexual dimorphism in the current coronavirus disease 2019 (COVID-19) pandemic. Here we report that estrogen can regulate the expression of angiotensin-converting enzyme 2 (ACE2), a key component for severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) cell entry, in differentiated airway epithelial cells. Further studies are required to elucidate the mechanisms by which sex steroids regulate SARS-CoV-2 infectivity.
    MeSH term(s) Angiotensin-Converting Enzyme 2 ; Betacoronavirus/drug effects ; COVID-19 ; Coronavirus Infections/drug therapy ; Coronavirus Infections/metabolism ; Epithelial Cells/drug effects ; Epithelial Cells/virology ; Estrogens/metabolism ; Estrogens/pharmacology ; Humans ; Pandemics ; Peptidyl-Dipeptidase A/metabolism ; Pneumonia, Viral/drug therapy ; Pneumonia, Viral/metabolism ; Respiratory System/drug effects ; Respiratory System/metabolism ; SARS-CoV-2
    Chemical Substances Estrogens ; Peptidyl-Dipeptidase A (EC 3.4.15.1) ; ACE2 protein, human (EC 3.4.17.23) ; Angiotensin-Converting Enzyme 2 (EC 3.4.17.23)
    Keywords covid19
    Language English
    Publishing date 2020-05-20
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 1013184-x
    ISSN 1522-1504 ; 1040-0605
    ISSN (online) 1522-1504
    ISSN 1040-0605
    DOI 10.1152/ajplung.00153.2020
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    In stock of ZB MED Cologne/Königswinter

    Uc I Zs.89: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
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  4. Article: Estrogen regulates the expression of SARS-CoV-2 receptor ACE2 in differentiated airway epithelial cells

    Stelzig, Kimberly E / Canepa-Escaro, Fabrizio / Schiliro, Marta / Berdnikovs, Sergejs / Prakash, Y S / Chiarella, Sergio E

    Am J Physiol Lung Cell Mol Physiol

    Abstract: There is marked sexual dimorphism in the current coronavirus disease 2019 (COVID-19) pandemic. Here we report that estrogen can regulate the expression of angiotensin-converting enzyme 2 (ACE2), a key component for severe acute respiratory syndrome ... ...

    Abstract There is marked sexual dimorphism in the current coronavirus disease 2019 (COVID-19) pandemic. Here we report that estrogen can regulate the expression of angiotensin-converting enzyme 2 (ACE2), a key component for severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) cell entry, in differentiated airway epithelial cells. Further studies are required to elucidate the mechanisms by which sex steroids regulate SARS-CoV-2 infectivity.
    Keywords covid19
    Publisher WHO
    Document type Article
    Note WHO #Covidence: #326936
    Database COVID19

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  5. Article ; Online: Autosomal Recessive Bestrophinopathy Is Not Associated With the Loss of Bestrophin-1 Anion Channel Function in a Patient With a Novel BEST1 Mutation.

    Johnson, Adiv A / Bachman, Lori A / Gilles, Benjamin J / Cross, Samuel D / Stelzig, Kimberly E / Resch, Zachary T / Marmorstein, Lihua Y / Pulido, Jose S / Marmorstein, Alan D

    Investigative ophthalmology & visual science

    2015  Volume 56, Issue 8, Page(s) 4619–4630

    Abstract: Purpose: Mutations in BEST1, encoding bestrophin-1 (Best1), cause autosomal recessive bestrophinopathy (ARB). Encoding bestrophin-1 is a pentameric anion channel localized to the basolateral plasma membrane of the RPE. Here, we characterize the effects ... ...

    Abstract Purpose: Mutations in BEST1, encoding bestrophin-1 (Best1), cause autosomal recessive bestrophinopathy (ARB). Encoding bestrophin-1 is a pentameric anion channel localized to the basolateral plasma membrane of the RPE. Here, we characterize the effects of the mutations R141H (CGC > CAC) and I366fsX18 (c.1098_1100+7del), identified in a patient in our practice, on Best1 trafficking, oligomerization, and channel activity.
    Methods: Currents of Cl- were assessed in transfected HEK293 cells using whole-cell patch clamp. Best1 localization was assessed by confocal microscopy in differentiated, human-induced pluripotent stem cell-derived RPE (iPSC-RPE) cells following expression of mutants via adenovirus-mediated gene transfer. Oligomerization was evaluated by coimmunoprecipitation in iPSC-RPE and MDCK cells.
    Results: Compared to Best1, Best1 I366fsX18 currents were increased while Best1 R141H Cl- currents were diminished. Coexpression of Best1 R141H with Best1 or Best1 I366fsX18 resulted in rescued channel activity. Overexpressed Best1, Best1 R141H, and Best1 I366fsX18 were all properly localized in iPSC-RPE cells; Best1 R141H and Best1 I366fsX18 coimmunoprecipitated with endogenous Best1 in iPSC-RPE cells and with each other in MDCK cells.
    Conclusions: The first 366 amino acids of Best1 are sufficient to mediate channel activity and homo-oligomerization. The combination of Best1 and Best1 R141H does not cause disease, while Best1 R141H together with Best1 I366fsX18 causes ARB. Since both combinations generate comparable Cl- currents, this indicates that ARB in this patient is not caused by a loss of channel activity. Moreover, Best1 I366fsX18 differs from Best1 in that it lacks most of the cytosolic C-terminal domain, suggesting that the loss of this region contributes significantly to the pathogenesis of ARB in this patient.
    MeSH term(s) Adolescent ; Bestrophins ; Blotting, Western ; Cell Membrane/metabolism ; Chloride Channels/biosynthesis ; Chloride Channels/genetics ; Chloride Channels/metabolism ; DNA/genetics ; DNA Mutational Analysis ; Eye Diseases, Hereditary/genetics ; Eye Diseases, Hereditary/metabolism ; Eye Diseases, Hereditary/pathology ; Eye Proteins/biosynthesis ; Eye Proteins/genetics ; Female ; Fluorescein Angiography ; Fundus Oculi ; Gene Expression Regulation ; Genes, Recessive ; HEK293 Cells/metabolism ; HEK293 Cells/ultrastructure ; Humans ; Microscopy, Confocal ; Microscopy, Electron ; Microscopy, Fluorescence ; Mutation ; Patch-Clamp Techniques ; Retinal Diseases/genetics ; Retinal Diseases/metabolism ; Retinal Diseases/pathology ; Retinal Pigment Epithelium/metabolism ; Retinal Pigment Epithelium/ultrastructure
    Chemical Substances BEST1 protein, human ; Bestrophins ; Chloride Channels ; Eye Proteins ; DNA (9007-49-2)
    Language English
    Publishing date 2015-07
    Publishing country United States
    Document type Case Reports ; Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 391794-0
    ISSN 1552-5783 ; 0146-0404
    ISSN (online) 1552-5783
    ISSN 0146-0404
    DOI 10.1167/iovs.15-16910
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