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Start Over Author "Egor Zindy" Journal international journal of molecular sciences
2 results on '"Egor Zindy"'

1. Ezrin Is a Novel Protein Partner of Aquaporin-5 in Human Salivary Glands and Shows Altered Expression and Cellular Localization in Sjögren’s Syndrome

Author

Clara Chivasso, Carl Johan Hagströmer, Kristie L. Rose, Florent Lhotellerie, Lionel Leblanc, Zhen Wang, Stefania Moscato, Clément Chevalier, Egor Zindy, Maud Martin, Benoit Vanhollebeke, Françoise Gregoire, Nargis Bolaky, Jason Perret, Chiara Baldini, Muhammad Shahnawaz Soyfoo, Letizia Mattii, Kevin L. Schey, Susanna Törnroth-Horsefield, and Christine Delporte

Subjects
Sjögren’s syndrome, aquaporin-5, ezrin, salivary glands, protein–protein interaction, Biology (General), QH301-705.5, Chemistry, QD1-999
Abstract

Sjögren’s syndrome (SS) is an exocrinopathy characterized by the hypofunction of salivary glands (SGs). Aquaporin-5 (AQP5); a water channel involved in saliva formation; is aberrantly distributed in SS SG acini and contributes to glandular dysfunction. We aimed to investigate the role of ezrin in AQP5 mislocalization in SS SGs. The AQP5–ezrin interaction was assessed by immunoprecipitation and proteome analysis and by proximity ligation assay in immortalized human SG cells. We demonstrated, for the first time, an interaction between ezrin and AQP5. A model of the complex was derived by computer modeling and in silico docking; suggesting that AQP5 interacts with the ezrin FERM-domain via its C-terminus. The interaction was also investigated in human minor salivary gland (hMSG) acini from SS patients (SICCA-SS); showing that AQP5–ezrin complexes were absent or mislocalized to the basolateral side of SG acini rather than the apical region compared to controls (SICCA-NS). Furthermore, in SICCA-SS hMSG acinar cells, ezrin immunoreactivity was decreased at the acinar apical region and higher at basal or lateral regions, accounting for altered AQP5–ezrin co-localization. Our data reveal that AQP5–ezrin interactions in human SGs could be involved in the regulation of AQP5 trafficking and may contribute to AQP5-altered localization in SS patients

Published
2021
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2. Ezrin Is a Novel Protein Partner of Aquaporin-5 in Human Salivary Glands and Shows Altered Expression and Cellular Localization in Sjögren’s Syndrome

Author

Jason Perret, Clément Chevalier, Muhammad Shahnawaz Soyfoo, Christine Delporte, Florent Lhotellerie, Egor Zindy, Kristie L. Rose, Letizia Mattii, Kevin L. Schey, Zhen Wang, Stefania Moscato, Lionel Leblanc, Nargis Bolaky, Chiara Baldini, Carl Johan Hagströmer, Françoise Grégoire, Clara Chivasso, Susanna Törnroth-Horsefield, Benoit Vanhollebeke, and Maud Martin

Subjects
Models, Molecular, Saliva, salivary glands, aquaporin-5, Informatique appliquée logiciel, Proximity ligation assay, Ezrin, environment and public health, Physico-chimie générale, 0302 clinical medicine, Models, Protein Interaction Mapping, Protein Interaction Maps, Biology (General), Spectroscopy, Cellular localization, 0303 health sciences, Salivary gland, Chemistry, General Medicine, Sciences bio-médicales et agricoles, 3. Good health, Computer Science Applications, Cell biology, Protein–protein interaction, Protein Transport, medicine.anatomical_structure, Sjogren's Syndrome, 030220 oncology & carcinogenesis, Proteome, Protein Binding, Immunoprecipitation, QH301-705.5, Aquaporin, macromolecular substances, Salivary glands, Chimie inorganique, Catalysis, Article, Inorganic Chemistry, 03 medical and health sciences, Structure-Activity Relationship, Aquaporin-5, Sjögren’s syndrome, Amino Acid Sequence, Aquaporin 5, Carrier Proteins, Cytoskeletal Proteins, Humans, Salivary Glands, Gene Expression Regulation, stomatognathic system, medicine, Spectroscopie [état condense], Physical and Theoretical Chemistry, Molecular Biology, QD1-999, 030304 developmental biology, Organic Chemistry, Biologie moléculaire, Molecular, Chimie théorique, ezrin, Chimie organique, Spectroscopie [électromagnétisme, optique, acoustique], protein–protein interaction, Catalyses hétérogène et homogène
Abstract

Sjögren’s syndrome (SS) is an exocrinopathy characterized by the hypofunction of salivary glands (SGs). Aquaporin-5 (AQP5), a water channel involved in saliva formation, is aberrantly distributed in SS SG acini and contributes to glandular dysfunction. We aimed to investigate the role of ezrin in AQP5 mislocalization in SS SGs. The AQP5–ezrin interaction was assessed by immunoprecipitation and proteome analysis and by proximity ligation assay in immortalized human SG cells. We demonstrated, for the first time, an interaction between ezrin and AQP5. A model of the complex was derived by computer modeling and in silico docking, suggesting that AQP5 interacts with the ezrin FERM-domain via its C-terminus. The interaction was also investigated in human minor salivary gland (hMSG) acini from SS patients (SICCA-SS), showing that AQP5–ezrin complexes were absent or mislocalized to the basolateral side of SG acini rather than the apical region compared to controls (SICCA-NS). Furthermore, in SICCA-SS hMSG acinar cells, ezrin immunoreactivity was decreased at the acinar apical region and higher at basal or lateral regions, accounting for altered AQP5–ezrin co-localization. Our data reveal that AQP5–ezrin interactions in human SGs could be involved in the regulation of AQP5 trafficking and may contribute to AQP5-altered localization in SS patients

Published
2021

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