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Tytuł:
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Channel functions of claudins in the organization of biological systems.
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Autorzy:
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Meoli L; Institute of Clinical Physiology/Nutritional Medicine, Medical Department, Division of Gastroenterology, Infectiology, Rheumatology, Charité - Universitätsmedizin Berlin, 12203 Berlin, Germany.
Günzel D; Institute of Clinical Physiology/Nutritional Medicine, Medical Department, Division of Gastroenterology, Infectiology, Rheumatology, Charité - Universitätsmedizin Berlin, 12203 Berlin, Germany. Electronic address: .
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Źródło:
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Biochimica et biophysica acta. Biomembranes [Biochim Biophys Acta Biomembr] 2020 Sep 01; Vol. 1862 (9), pp. 183344. Date of Electronic Publication: 2020 May 20.
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Typ publikacji:
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Journal Article; Research Support, Non-U.S. Gov't; Review
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Język:
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English
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Imprint Name(s):
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Original Publication: Amsterdam : Elsevier
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MeSH Terms:
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Claudins/*genetics
Tight Junction Proteins/*genetics
Tight Junctions/*genetics
Animals ; Claudins/chemistry ; Mutation/genetics ; Permeability ; Protein Isoforms/genetics ; Tight Junction Proteins/chemistry ; Tight Junctions/chemistry ; Vertebrates/genetics
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Contributed Indexing:
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Keywords: Claudin; Epithelial transport physiology; Ion homeostasis; Paracellular channel; Tight junction
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Substance Nomenclature:
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0 (Claudins)
0 (Protein Isoforms)
0 (Tight Junction Proteins)
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Entry Date(s):
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Date Created: 20200523 Date Completed: 20201204 Latest Revision: 20201214
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Update Code:
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20240105
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DOI:
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10.1016/j.bbamem.2020.183344
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PMID:
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32442419
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Claudins are tight junction proteins mostly appreciated in their function of paracellular barrier-formation. Compared to a virtual absence of any tight junctions, their paracellular sealing role certainly stands out. Yet, it was recognized immediately after the discovery of the first claudins, that some members of the claudin protein family were able to convey size and charge selectivity to the paracellular pathway. Thus, paracellular permeability can be fine-tuned according to the physiological needs of a tissue by inserting these channel-forming claudins into tight junction strands. Precise permeability adjustment is further suggested by the presence of numerous isoforms of channel-forming claudins (claudin-10b-, -15-, -16-like isoforms) in various vertebrate taxa. Moreover, their expression and localization are controlled by multiple transcriptional and posttranslational mechanisms. Consequently, mutation or dysregulation of channel-forming claudins can cause severe diseases. The present review therefore aims at providing an up-to-date report of the current research on these aspects of channel-forming claudins and their possible implications on future developments.
Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
(Copyright © 2020 Elsevier B.V. All rights reserved.)
