Protein differences in cilia of mechanoreceptor hair and gill cells of the scallop Mizuhopecten yessoensis |
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| Institution: | 2. Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138, USA;1. Sorbonne Université, Institut National de la Santé et de la Recherche Médicale, Childhood Genetic Disorders, Département de Génétique Médicale, Hôpital Armand-Trousseau, Assistance Publique-Hôpitaux de Paris, Paris 75012, France;2. Université Côte d’Azur, CNRS, IPMC, Sophia-Antipolis, 06560, France;3. Genetics and Genomic Medicine, University College London, UCL Great Ormond Street Institute of Child Health, London WC1N 1EH, UK;4. NIHR Biomedical Research Centre at Great Ormond Street Hospital, London, UK;1. State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, National Centre for Magnetic Resonance in Wuhan, Innovation Academy of Precision Measurement Science and Technology, CAS, Wuhan 430071, China;2. University of Chinese Academy of Sciences, Beijing 100049, China;3. Department of Joint Surgery, Center for Orthopaedic Surgery, The Third Affiliated Hospital of Southern Medical University, Guangzhou, 510515, China;4. Golden Health (Guangdong) Biotechnology Co., Ltd, Foshan 528225, China;5. School of Biomedical and Pharmaceutical Sciences, Guangdong University of Technology, Guangzhou 510006, China;6. Engineering Research Academy of High Value Utilization of Green Plants, Meizhou 514021, China;1. The Ritchie Centre, Hudson Institute of Medical Research and Department of Paediatrics, Monash University, Melbourne, Australia;2. Melbourne Children''s Sleep Centre, Monash Children''s Hospital, Melbourne, Victoria, Australia |
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| Abstract: | - 1.1. In search for mechanosensory molecules the composition of the ciliary proteins of mechanoreceptor hair cells of the abdominal organ and less mechanosensitive gill cells were compared electrophoretically.
- 2.2. The hair cells and gill cilia were very similar in their polypeptide sets but differed by contents of three axonemal polypeptides with molecular weights of 125, 149 and 300 kilodaltons (kDa) and one membrane polypeptide of 159 kDa.
- 3.3. The membrane polypeptide with a molecular weight of 159 kDa represented approximately 3% of the total ciliary protein of hair cells. There was only a trace of this polypeptide in gill cilia and their membrane fraction.
- 4.4. A peculiarity of ciliary membranes of the hair cells was a high content of the 159 kDa-polypeptide, which constituted more than 20% of the total protein of membrane fraction.
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