Unexpected localization of AQP3 and AQP4 induced by migration of primary cultured IMCD cells
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...
Guardado en:
Autores principales: | , , , , |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2021
|
Materias: | |
Acceso en línea: | https://doaj.org/article/0a225194b1554530bb1d639f14dd5a8e |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
id |
oai:doaj.org-article:0a225194b1554530bb1d639f14dd5a8e |
---|---|
record_format |
dspace |
spelling |
oai:doaj.org-article:0a225194b1554530bb1d639f14dd5a8e2021-12-02T17:34:40ZUnexpected localization of AQP3 and AQP4 induced by migration of primary cultured IMCD cells10.1038/s41598-021-91369-y2045-2322https://doaj.org/article/0a225194b1554530bb1d639f14dd5a8e2021-06-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-91369-yhttps://doaj.org/toc/2045-2322Abstract 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.Ralph RoseBjörn KemperAlbrecht SchwabEberhard SchlatterBayram EdemirNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-12 (2021) |
institution |
DOAJ |
collection |
DOAJ |
language |
EN |
topic |
Medicine R Science Q |
spellingShingle |
Medicine R Science Q Ralph Rose Björn Kemper Albrecht Schwab Eberhard Schlatter Bayram Edemir Unexpected localization of AQP3 and AQP4 induced by migration of primary cultured IMCD cells |
description |
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. |
format |
article |
author |
Ralph Rose Björn Kemper Albrecht Schwab Eberhard Schlatter Bayram Edemir |
author_facet |
Ralph Rose Björn Kemper Albrecht Schwab Eberhard Schlatter Bayram Edemir |
author_sort |
Ralph Rose |
title |
Unexpected localization of AQP3 and AQP4 induced by migration of primary cultured IMCD cells |
title_short |
Unexpected localization of AQP3 and AQP4 induced by migration of primary cultured IMCD cells |
title_full |
Unexpected localization of AQP3 and AQP4 induced by migration of primary cultured IMCD cells |
title_fullStr |
Unexpected localization of AQP3 and AQP4 induced by migration of primary cultured IMCD cells |
title_full_unstemmed |
Unexpected localization of AQP3 and AQP4 induced by migration of primary cultured IMCD cells |
title_sort |
unexpected localization of aqp3 and aqp4 induced by migration of primary cultured imcd cells |
publisher |
Nature Portfolio |
publishDate |
2021 |
url |
https://doaj.org/article/0a225194b1554530bb1d639f14dd5a8e |
work_keys_str_mv |
AT ralphrose unexpectedlocalizationofaqp3andaqp4inducedbymigrationofprimaryculturedimcdcells AT bjornkemper unexpectedlocalizationofaqp3andaqp4inducedbymigrationofprimaryculturedimcdcells AT albrechtschwab unexpectedlocalizationofaqp3andaqp4inducedbymigrationofprimaryculturedimcdcells AT eberhardschlatter unexpectedlocalizationofaqp3andaqp4inducedbymigrationofprimaryculturedimcdcells AT bayramedemir unexpectedlocalizationofaqp3andaqp4inducedbymigrationofprimaryculturedimcdcells |
_version_ |
1718379921227644928 |