Unraveling Human AQP5-PIP Molecular Interaction and Effect on AQP5 Salivary Glands Localization in SS Patients.

Autor: Chivasso C; Laboratory of Pathophysiological and Nutritional Biochemistry, Université Libre de Bruxelles, 1070 Brussels, Belgium., Nesverova V; Division of Biochemistry and Structural Biology, Lund University, 221 00 Lund, Sweden., Järvå M; Department of Chemistry and Molecular Biology, University of Gothenburg, 907 36 Umeå, Sweden., Blanchard A; Department of Pathology, University of Manitoba, Winnipeg, MB R3E 0T5, Canada., Rose KL; Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN 37240, USA., Öberg FK; Department of Chemistry and Molecular Biology, University of Gothenburg, 907 36 Umeå, Sweden., Wang Z; Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN 37240, USA., Martin M; Laboratory of Neurovascular Signaling, Université Libre de Bruxelles, 6041 Gosselies, Belgium., Lhotellerie F; Laboratory of Pathophysiological and Nutritional Biochemistry, Université Libre de Bruxelles, 1070 Brussels, Belgium., Zindy E; Multimodal Image Processing, Center for Microscopy and Molecular Imaging (CMMI), 6041 Gosselies, Belgium., Junqueira B; Louvain Institute of Biomolecular Science and Technology, UCLouvain, 1348 Louvain-la Neuve, Belgium., Leroy K; Laboratory of Histology, Neuroanatomy and Neuropathology, UNI (ULB Neuroscience Institute), Faculty of Medicine, Université Libre de Bruxelles, 1070 Brussels, Belgium., Vanhollebeke B; Laboratory of Neurovascular Signaling, Université Libre de Bruxelles, 6041 Gosselies, Belgium., Delforge V; Laboratory of Pathophysiological and Nutritional Biochemistry, Université Libre de Bruxelles, 1070 Brussels, Belgium., Bolaky N; Laboratory of Pathophysiological and Nutritional Biochemistry, Université Libre de Bruxelles, 1070 Brussels, Belgium., Perret J; Laboratory of Pathophysiological and Nutritional Biochemistry, Université Libre de Bruxelles, 1070 Brussels, Belgium., Soyfoo MS; Department of Rheumatology, Erasme Hospital, Université Libre de Bruxelles, 1070 Brussels, Belgium., Moscato S; Department of Clinical and Experimental Medicine, University of Pisa, 56126 Pisa, Italy., Baldini C; Department of Clinical and Experimental Medicine, University of Pisa, 56126 Pisa, Italy., Chaumont F; Louvain Institute of Biomolecular Science and Technology, UCLouvain, 1348 Louvain-la Neuve, Belgium., Mattii L; Department of Clinical and Experimental Medicine, University of Pisa, 56126 Pisa, Italy., Schey KL; Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN 37240, USA., Myal Y; Department of Pathology, University of Manitoba, Winnipeg, MB R3E 0T5, Canada.; Research Institute for Oncology and Hematology (RIOH), CancerCare Manitoba, Winnipeg, MB R3E 0V9, Canada., Törnroth-Horsefield S; Division of Biochemistry and Structural Biology, Lund University, 221 00 Lund, Sweden., Delporte C; Laboratory of Pathophysiological and Nutritional Biochemistry, Université Libre de Bruxelles, 1070 Brussels, Belgium.
Jazyk: angličtina
Zdroj: Cells [Cells] 2021 Aug 17; Vol. 10 (8). Date of Electronic Publication: 2021 Aug 17.
DOI: 10.3390/cells10082108
Abstrakt: Saliva secretion requires effective translocation of aquaporin 5 (AQP5) water channel to the salivary glands (SGs) acinar apical membrane. Patients with Sjögren's syndrome (SS) display abnormal AQP5 localization within acinar cells from SGs that correlate with sicca manifestation and glands hypofunction. Several proteins such as Prolactin-inducible protein (PIP) may regulate AQP5 trafficking as observed in lacrimal glands from mice. However, the role of the AQP5-PIP complex remains poorly understood. In the present study, we show that PIP interacts with AQP5 in vitro and in mice as well as in human SGs and that PIP misexpression correlates with an altered AQP5 distribution at the acinar apical membrane in PIP knockout mice and SS hMSG. Furthermore, our data show that the protein-protein interaction involves the AQP5 C-terminus and the N-terminal of PIP (one molecule of PIP per AQP5 tetramer). In conclusion, our findings highlight for the first time the role of PIP as a protein controlling AQP5 localization in human salivary glands but extend beyond due to the PIP-AQP5 interaction described in lung and breast cancers.
Databáze: MEDLINE
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