A CLCA regulatory protein present in the chemosensory cilia of olfactory sensory neurons induces a Ca²⁺-activated Cl^- current when transfected into HEK293.

ABSTRACT:

Background

CLCA is a family of metalloproteases that regulate Ca²⁺-activated Cl^- fluxes in epithelial tissues. In HEK293 cells, CLCA1 promotes membrane expression of an endogenous Anoctamin 1 (ANO1, also termed TMEM16A)-dependent Ca²⁺-activated Cl^- current. Motif architecture similarity with CLCA2, 3 and 4 suggested that they have similar functions. We previously detected the isoform CLCA4L in rat olfactory sensory neurons, where Anoctamin 2 is the principal chemotransduction Ca²⁺-activated Cl^- channel. We explored the possibility that this protein plays a role in odor transduction.

Results

We cloned and expressed CLCA4L from rat olfactory epithelium in HEK293 cells. In the transfected HEK293 cells we measured

SUBMITTER: Mura CV 

PROVIDER: S-EPMC5553735 | biostudies-literature | 2017 Aug

REPOSITORIES: biostudies-literature