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    Biochem Biophys Res Commun. 1995 Mar 8;208(1):89-95.

    Molecular cloning of the human volume-sensitive chloride conductance regulatory protein, pICln, from ocular ciliary epithelium.

    Anguita J, Chalfant ML, Civan MM, Coca-Prados M.

    Source

    Department of Ophthalmology, Yale University School of Medicine, New Haven, CT.

    Abstract

    Chloride channels in the ocular ciliary epithelium are believed to play a key role in aqueous humor formation. We isolated a cDNA clone from a lambda Uni-ZAP cDNA library of human nonpigmented ciliary epithelial (NPE) cells encoding the swelling-induced chloride channel/channel regulator pICln. The human clone contains an open reading frame of 237 amino acids (M(r) 26,293). The deduced human amino-acid sequence shows 90.2% and 92.7% identity with counterparts isolated from rat kidney and the canine kidney epithelial cell line MDCK. Human NPE cell lines exhibited significant levels of pICln transcripts. Complementary perforated-patch, whole-cell patch clamping demonstrated that swelling activates Cl- channels of the NPE cells, as suggested by ruptured-patch measurements. The results document the molecular isolation and identification of a human cDNA clone of a Cl- conductance regulator from ocular cells displaying volume-activated Cl-channels.

    PMID:
    7887970
    [PubMed - indexed for MEDLINE]

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