Evidence for involvement of TRPA1 in the detection of vibrations by hair bundle mechanoreceptors in sea anemones |
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Authors: | Janna L Mahoney Erin M Graugnard Patricia Mire Glen M Watson |
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Institution: | (1) Department of Biology, University of Louisiana at Lafayette, Lafayette, LA 70504-2451, USA; |
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Abstract: | A homolog of TRPA1 was identified in the genome of the anemone, Nematostella vectensis (nv-TRPA1a), and predicted to possess six ankyrin repeat domains at the N-terminus and an ion channel domain near the C-terminus.
Transmembrane segments of the ion channel domain are well conserved among several known TRPA1 polypeptides. Inhibitors of
TRPA1 including ruthenium red decrease vibration-dependent discharge of nematocysts in N. vectensis and Haliplanella luciae. Activators of TRPA1 including URB-597 and polygodial increase nematocyst discharge in the absence of vibrations. Co-immunoprecipitation
yields a band on SDS-PAGE gels at the predicted mass of the nv-TRPA1a polypeptide among other bands. Co-immunoprecipitation
performed in the presence of antigenic peptide decreases the yield of this and several other polypeptides. In untreated controls,
anti-nv-TRPA1a primarily labels the base of the hair bundle with some labeling also distributed along the length of stereocilia.
Tissue immunolabeled in the presence of the antigenic peptide exhibits reduced labeling. Activating chemoreceptors for N-acetylated
sugars induce immunolabel to distribute distally in stereocilia. In anemones, activating chemoreceptors for N-acetylated sugars
induce hair bundles to elongate among several other structural and functional changes. Taken together, these results are consistent
with the possibility that nv-TRPA1a participates in signal transduction of anemone hair bundles. |
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