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

Autor: Yvonne Myal, Florent Lhotellerie, Clara Chivasso, Christine Delporte, Benoit Vanhollebeke, Veronika Nesverova, Kevin L. Schey, Stefania Moscato, François Chaumont, Muhammad Shahnawaz Soyfoo, Chiara Baldini, Karelle Leroy, Zhen Wang, Jason Perret, Susanna Törnroth-Horsefield, Bruna Rayane Teodoro Junqueira, Michael Järvå, Letizia Mattii, Egor Zindy, Valérie Delforge, Anne Blanchard, Kristie L. Rose, Fredrik Öberg, Maud Martin, Nargis Bolaky
Jazyk: francouzština
Rok vydání: 2021
Předmět:
musculoskeletal diseases
QH301-705.5
Knockout
aquaporin-5
Saliva secretion
Aquaporin
Chromosomal translocation
salivary gland
Acinar Cells
Article
Salivary Glands
Cell Line
03 medical and health sciences
Mice
0302 clinical medicine
stomatognathic system
parasitic diseases
medicine
Animals
Humans
prolactin-inducible protein
Biology (General)
030304 developmental biology
Mice
Knockout

0303 health sciences
Binding Sites
Salivary gland
Chemistry
Aquaporin-5
Prolactin-inducible protein
Sjögren’s syndrome
Aquaporin 5
Membrane Transport Proteins
Protein Binding
Sjogren's Syndrome
fungi
General Medicine
Apical membrane
Sciences bio-médicales et agricoles
In vitro
Cell biology
medicine.anatomical_structure
Prolactin-Inducible Protein
030220 oncology & carcinogenesis
Knockout mouse
lipids (amino acids
peptides
and proteins)
Zdroj: Cells, 10
Cells
Volume 10
Issue 8
Cells, Vol 10, Iss 2108, p 2108 (2021)
Popis: 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: OpenAIRE