Unraveling Human AQP5-PIP Molecular Interaction and Effect on AQP5 Salivary Glands Localization in SS Patients
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 hypofunc...
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Published in | Cells (Basel, Switzerland) Vol. 10; no. 8; p. 2108 |
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Main Authors | , , , , , , , , , , , , , , , , , , , , , , , , |
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Abstract | 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. |
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AbstractList | 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. |
Author | Martin, Maud Zindy, Egor Baldini, Chiara Junqueira, Bruna Moscato, Stefania Törnroth-Horsefield, Susanna Wang, Zhen Vanhollebeke, Benoit Chivasso, Clara Delforge, Valérie Järvå, Michael Delporte, Christine Nesverova, Veronika Lhotellerie, Florent Rose, Kristie L Soyfoo, Muhammad Shahnawaz Perret, Jason Blanchard, Anne Bolaky, Nargis Chaumont, François Öberg, Fredrik Kryh Leroy, Karelle Schey, Kevin L Myal, Yvonne Mattii, Letizia |
AuthorAffiliation | 1 Laboratory of Pathophysiological and Nutritional Biochemistry, Université Libre de Bruxelles, 1070 Brussels, Belgium; clara.chivasso@ulb.be (C.C.); Florent.Lhotellerie@ulb.be (F.L.); Valerie.Delforge@ulb.be (V.D.); Nargis.Bolaky@ulb.ac.be (N.B.); Jason.Perret@ulb.be (J.P.) 4 Department of Pathology, University of Manitoba, Winnipeg, MB R3E 0T5, Canada; aaablanch@gmail.com (A.B.); Yvonne.Myal@umanitoba.ca (Y.M.) 2 Division of Biochemistry and Structural Biology, Lund University, 221 00 Lund, Sweden; verca.nesver@gmail.com (V.N.); susanna.horsefield@biochemistry.lu.se (S.T.-H.) 8 Louvain Institute of Biomolecular Science and Technology, UCLouvain, 1348 Louvain-la Neuve, Belgium; bruna.teodoro@uclouvain.be (B.J.); francois.chaumont@uclouvain.be (F.C.) 10 Department of Rheumatology, Erasme Hospital, Université Libre de Bruxelles, 1070 Brussels, Belgium; muhammad.shah.soyfoo@ulb.be 5 Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN 37240, USA; kristie.rose@Va |
AuthorAffiliation_xml | – name: 10 Department of Rheumatology, Erasme Hospital, Université Libre de Bruxelles, 1070 Brussels, Belgium; muhammad.shah.soyfoo@ulb.be – name: 2 Division of Biochemistry and Structural Biology, Lund University, 221 00 Lund, Sweden; verca.nesver@gmail.com (V.N.); susanna.horsefield@biochemistry.lu.se (S.T.-H.) – name: 1 Laboratory of Pathophysiological and Nutritional Biochemistry, Université Libre de Bruxelles, 1070 Brussels, Belgium; clara.chivasso@ulb.be (C.C.); Florent.Lhotellerie@ulb.be (F.L.); Valerie.Delforge@ulb.be (V.D.); Nargis.Bolaky@ulb.ac.be (N.B.); Jason.Perret@ulb.be (J.P.) – name: 4 Department of Pathology, University of Manitoba, Winnipeg, MB R3E 0T5, Canada; aaablanch@gmail.com (A.B.); Yvonne.Myal@umanitoba.ca (Y.M.) – name: 12 Research Institute for Oncology and Hematology (RIOH), CancerCare Manitoba, Winnipeg, MB R3E 0V9, Canada – name: 7 Multimodal Image Processing, Center for Microscopy and Molecular Imaging (CMMI), 6041 Gosselies, Belgium; egor.zindy@ulb.be – name: 5 Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN 37240, USA; kristie.rose@Vanderbilt.Edu (K.L.R.); zhen.wang@Vanderbilt.Edu (Z.W.); k.schey@Vanderbilt.Edu (K.L.S.) – name: 9 Laboratory of Histology, Neuroanatomy and Neuropathology, UNI (ULB Neuroscience Institute), Faculty of Medicine, Université Libre de Bruxelles, 1070 Brussels, Belgium; kleroy@ulb.be – name: 6 Laboratory of Neurovascular Signaling, Université Libre de Bruxelles, 6041 Gosselies, Belgium; maud.martin@ulb.be (M.M.); Benoit.Vanhollebeke@ulb.be (B.V.) – name: 11 Department of Clinical and Experimental Medicine, University of Pisa, 56126 Pisa, Italy; stefania.moscato@unipi.it (S.M.); chiara.baldini74@gmail.com (C.B.); letizia.mattii@med.unipi.it (L.M.) – name: 3 Department of Chemistry and Molecular Biology, University of Gothenburg, 907 36 Umeå, Sweden; michael.jarva@umu.se (M.J.); fredrik.kryh.oberg@gmail.com (F.K.Ö.) – name: 8 Louvain Institute of Biomolecular Science and Technology, UCLouvain, 1348 Louvain-la Neuve, Belgium; bruna.teodoro@uclouvain.be (B.J.); francois.chaumont@uclouvain.be (F.C.) |
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SubjectTerms | Acinar cells Aquaporin 5 Aquaporins Basic Medicine Breast cancer C-Terminus Cell and Molecular Biology Cell culture Cell- och molekylärbiologi Clinical Medicine Cloning Exocrine glands Glycoproteins Klinisk medicin Lacrimal gland and Nasolacrimal duct Localization Medical and Health Sciences Medicin och hälsovetenskap Medicinska och farmaceutiska grundvetenskaper Membranes Permeability Plasmids Prolactin Prolactin-inducible protein Protein interaction Proteins Reumatologi och inflammation Rheumatology and Autoimmunity RNA polymerase Saliva Salivary gland Sjogren's syndrome Sjögren’s syndrome |
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Title | Unraveling Human AQP5-PIP Molecular Interaction and Effect on AQP5 Salivary Glands Localization in SS Patients |
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