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  1. Book ; Thesis: Role of osmolality and aquaporins in the migration of IMCD-cells

    Rose, Ralph Christopher

    2019  

    Institution Westfälische Wilhelms-Universität Münster
    Author's details Ralph Christopher Rose aus Hamm
    Language English
    Size 58, IV Blätter, Diagramme
    Publishing place Münster
    Publishing country Germany
    Document type Book ; Thesis
    Thesis / German Habilitation thesis Dissertation, Westfälische Wilhelms-Universität Münster, 2019
    HBZ-ID HT020247270
    Database Catalogue ZB MED Medicine, Health

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    In stock of ZB MED Cologne/Königswinter

    Shelf markLoan statusLocation
    2020 E 431 order for loan Magazin

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  2. Article ; Online: Unexpected localization of AQP3 and AQP4 induced by migration of primary cultured IMCD cells.

    Rose, Ralph / Kemper, Björn / Schwab, Albrecht / Schlatter, Eberhard / Edemir, Bayram

    Scientific reports

    2021  Volume 11, Issue 1, Page(s) 11930

    Abstract: Aquaporin-2-4 (AQP) are expressed in the principal cells of the renal collecting duct (CD). Beside their role in water transport across membranes, several studies showed that AQPs can influence the migration of cells. It is unknown whether this also ... ...

    Abstract Aquaporin-2-4 (AQP) are expressed in the principal cells of the renal collecting duct (CD). Beside their role in water transport across membranes, several studies showed that AQPs can influence the migration of cells. It is unknown whether this also applies for renal CD cells. Another fact is that the expression of these AQPs is highly modulated by the external osmolality. Here we analyzed the localization of AQP2-4 in primary cultured renal inner medullary CD (IMCD) cells and how osmolality influences the migration behavior of these cells. The primary IMCD cells showed a collective migration behavior and there were no differences in the migration speed between cells cultivated either at 300 or 600 mosmol/kg. Acute increase from 300 to 600 mosmol/kg led to a marked reduction and vice versa an acute decrease from 600 to 300 mosmol/kg to a marked increase in migration speed. Interestingly, none of the analyzed AQPs were localized at the leading edge. While AQP3 disappeared within the first 2-3 rows of cells, AQP4 was enriched at the rear end. Further analysis indicated that migration induced lysosomal degradation of AQP3. This could be prevented by activation of the protein kinase A, inducing localization of AQP3 and AQP2 at the leading edge and increasing the migration speed.
    MeSH term(s) Animals ; Aquaporin 3/genetics ; Aquaporin 3/metabolism ; Aquaporin 4/genetics ; Aquaporin 4/metabolism ; Bucladesine/pharmacology ; Cell Movement/drug effects ; Cell Movement/physiology ; Cell Shape ; Cells, Cultured ; Kidney Medulla/cytology ; Kidney Tubules, Collecting/cytology ; Kidney Tubules, Collecting/drug effects ; Kidney Tubules, Collecting/metabolism ; Microscopy, Fluorescence/methods ; Osmolar Concentration ; Primary Cell Culture ; Rats ; Sodium-Hydrogen Exchanger 1/metabolism ; beta Catenin/metabolism
    Chemical Substances Aquaporin 4 ; Sodium-Hydrogen Exchanger 1 ; beta Catenin ; Aquaporin 3 (158801-98-0) ; Bucladesine (63X7MBT2LQ)
    Language English
    Publishing date 2021-06-07
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/s41598-021-91369-y
    Database MEDical Literature Analysis and Retrieval System OnLINE

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