Your browser doesn't support javascript.
loading
Charge and lipophilicity are required for effective block of the hair-cell mechano-electrical transducer channel by FM1-43 and its derivatives.
Derudas, Marco; O'Reilly, Molly; Kirkwood, Nerissa K; Kenyon, Emma J; Grimsey, Sybil; Kitcher, Siân R; Workman, Shawna; Bull, James C; Ward, Simon E; Kros, Corné J; Richardson, Guy P.
Afiliação
  • Derudas M; Sussex Neuroscience, School of Life Sciences, University of Sussex, Brighton, United Kingdom.
  • O'Reilly M; Sussex Drug Discovery Centre, School of Life Sciences, University of Sussex, Brighton, United Kingdom.
  • Kirkwood NK; Sussex Neuroscience, School of Life Sciences, University of Sussex, Brighton, United Kingdom.
  • Kenyon EJ; Department of Experimental Cardiology, Academic Medical Center, Amsterdam, Netherlands.
  • Grimsey S; Sussex Neuroscience, School of Life Sciences, University of Sussex, Brighton, United Kingdom.
  • Kitcher SR; School of Biosciences, University of Kent, Canterbury, United Kingdom.
  • Workman S; Sussex Neuroscience, School of Life Sciences, University of Sussex, Brighton, United Kingdom.
  • Bull JC; School of Medicine, Institute of Life Sciences, Swansea University, Swansea, United Kingdom.
  • Ward SE; Sussex Neuroscience, School of Life Sciences, University of Sussex, Brighton, United Kingdom.
  • Kros CJ; Sussex Neuroscience, School of Life Sciences, University of Sussex, Brighton, United Kingdom.
  • Richardson GP; Section on Neuronal Circuitry, National Institute on Deafness and Other Communication Disorders NIH, Bethesda, MD, United States.
Front Cell Dev Biol ; 11: 1247324, 2023.
Article em En | MEDLINE | ID: mdl-37900280
The styryl dye FM1-43 is widely used to study endocytosis but behaves as a permeant blocker of the mechano-electrical transducer (MET) channel in sensory hair cells, loading rapidly and specifically into the cytoplasm of hair cells in a MET channel-dependent manner. Patch clamp recordings of mouse outer hair cells (OHCs) were used to determine how a series of structural modifications of FM1-43 affect MET channel block. Fluorescence microscopy was used to assess how the modifications influence hair-cell loading in mouse cochlear cultures and zebrafish neuromasts. Cochlear cultures were also used to evaluate otoprotective potential of the modified FM1-43 derivatives. Structure-activity relationships reveal that the lipophilic tail and the cationic head group of FM1-43 are both required for MET channel block in mouse cochlear OHCs; neither moiety alone is sufficient. The extent of MET channel block is augmented by increasing the lipophilicity/bulkiness of the tail, by reducing the number of positive charges in the head group from two to one, or by increasing the distance between the two charged head groups. Loading assays with zebrafish neuromasts and mouse cochlear cultures are broadly in accordance with these observations but reveal a loss of hair-cell specific labelling with increasing lipophilicity. Although FM1-43 and many of its derivatives are generally cytotoxic when tested on cochlear cultures in the presence of an equimolar concentration of the ototoxic antibiotic gentamicin (5 µM), at a 10-fold lower concentration (0.5 µM), two of the derivatives protect OHCs from cell death caused by 48 h-exposure to 5 µM gentamicin.
Palavras-chave

Texto completo: 1 Base de dados: MEDLINE Idioma: En Revista: Front Cell Dev Biol Ano de publicação: 2023 Tipo de documento: Article País de afiliação: Reino Unido

Texto completo: 1 Base de dados: MEDLINE Idioma: En Revista: Front Cell Dev Biol Ano de publicação: 2023 Tipo de documento: Article País de afiliação: Reino Unido