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Expression of p11 and heteromeric TASK channels in mouse adrenal cortical cells and H295R cells.
Matsuoka, Hidetada; Harada, Keita; Sugawara, Akira; Kim, Donghee; Inoue, Masumi.
Afiliación
  • Matsuoka H; Department of Cell and Systems Physiology, University of Occupational and Environmental Health School of Medicine, Kitakyushu 807-8555, Japan.
  • Harada K; Department of Cell and Systems Physiology, University of Occupational and Environmental Health School of Medicine, Kitakyushu 807-8555, Japan.
  • Sugawara A; Department of Molecular Endocrinology, Tohoku University Graduate School of Medical Science, Sendai 980-8575, Japan.
  • Kim D; Department of Physiology and Biophysics, Chicago Medical School, Rosalind Franklin University of Medicine and Science, North Chicago, IL 60064-3095, USA.
  • Inoue M; Department of Cell and Systems Physiology, University of Occupational and Environmental Health School of Medicine, Kitakyushu 807-8555, Japan. Electronic address: minoue@med.uoeh-u.ac.jp.
Acta Histochem ; 124(5): 151898, 2022 Jul.
Article en En | MEDLINE | ID: mdl-35526370
TWIK-related acid-sensitive K+ (TASK) channels are thought to contribute to the resting membrane potential in adrenal cortical (AC) cells. However, the molecular identity of TASK channels in AC cells have not yet been elucidated. Thus, immunocytochemical and molecular biological approaches were employed to investigate the expression and intracellular distribution of TASK1 and TASK3 in mouse AC cells and H295R cells derived from human adrenocortical carcinoma. Immunocytochemical study revealed that immunoreactive materials were mainly located in the cytoplasm for TASK1 and at the cell periphery for TASK3 in mouse AC cells. A similar pattern of localization was observed when GFP-TASK1 and GFP-TASK3 were exogenously expressed in H295R cells. In addition, p11 that is known to suppress the endoplasmic reticulum exit of TASK1 was localized in the cytoplasm in mouse AC and H295R cells, but not in adrenal medullary cells. Proximity ligation assay (PLA) suggested formation of heteromeric TASK1-3 channels that were found predominantly in the cytoplasm and weakly at the cell periphery. A similar distribution was observed following exogenous expression of tandem TASK1-3 channels in H295R cells. When stimulated by angiotensin II, however, tandem TASK1-3 channels were present mainly in the cytoplasm in all H295R cells. In contrast to that in H295R cells, tandem channels were exclusively located at the cell periphery in all non-stimulated and exclusively in the cytoplasm in stimulated PC12 cells, respectively. From these results, we conclude that TASK1 proteins are present mainly in the cytoplasm and minimally at the cell periphery as a heteromeric channel with TASK3, whereas the majority of TASK3 is at the cell periphery as homomeric and heteromeric channels.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Canales de Potasio de Dominio Poro en Tándem / Células Endocrinas / Proteínas del Tejido Nervioso Límite: Animals / Humans Idioma: En Revista: Acta Histochem Año: 2022 Tipo del documento: Article País de afiliación: Japón Pais de publicación: Alemania
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Canales de Potasio de Dominio Poro en Tándem / Células Endocrinas / Proteínas del Tejido Nervioso Límite: Animals / Humans Idioma: En Revista: Acta Histochem Año: 2022 Tipo del documento: Article País de afiliación: Japón Pais de publicación: Alemania