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Hear Res. 2015 Sep;327:245-56. doi: 10.1016/j.heares.2015.07.005. Epub 2015 Jul 14.

Proteomic identification of hair cell repair proteins in the model sea anemone Nematostella vectensis.

Author information

1
Department of Biology, University of Louisiana Lafayette, USA.
2
Department of Biology, University of Louisiana Lafayette, USA. Electronic address: gmw5722@louisiana.edu.

Abstract

Sea anemones have an extraordinary capability to repair damaged hair bundles, even after severe trauma. A group of secreted proteins, named repair proteins (RPs), found in mucus covering sea anemones significantly assists the repair of damaged hair bundle mechanoreceptors both in the sea anemone Haliplanella luciae and the blind cavefish Astyanax hubbsi. The polypeptide constituents of RPs must be identified in order to gain insight into the molecular mechanisms by which repair of hair bundles is accomplished. In this study, several polypeptides of RPs were isolated from mucus using blue native PAGE and then sequenced using LC-MS/MS. Thirty-seven known polypeptides were identified, including Hsp70s, as well as many polypeptide subunits of the 20S proteasome. Other identified polypeptides included those involved in cellular stress responses, protein folding, and protein degradation. Specific inhibitors of Hsp70s and the 20S proteasome were employed in experiments to test their involvement in hair bundle repair. The results of those experiments suggested that repair requires biologically active Hsp70s and 20S proteasomes. A model is proposed that considers the function of extracellular Hsp70s and 20S proteasomes in the repair of damaged hair cells.

KEYWORDS:

20S proteasome; Hair bundle; Hsp70s; Repair proteins

PMID:
26183436
DOI:
10.1016/j.heares.2015.07.005
[Indexed for MEDLINE]

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