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J Biol Chem, Vol. 275, Issue 15, 11164-11173, April 14, 2000
From the We previously reported a 120-kDa phosphoprotein
that translocated from cytosol to the apical membrane of gastric
parietal cells in association with stimulation of HCl secretion. To
determine the molecular identity of the protein, we performed molecular cloning and expression of the protein. Immunoblot analysis showed that
this protein was highly enriched in tissues that secrete water, such as
parietal cell, choroid plexus, salivary duct, lacrimal gland, kidney,
airway epithelia, and chorioretinal epithelia. We named this protein
"parchorin" based on its highest enrichment in parietal cells and
choroid plexus. We obtained cDNA for parchorin from rabbit choroid
plexus coding a protein consisting of 637 amino acids with a predicted
molecular mass of 65 kDa. The discrepancy in size on 6%
SDS-polyacrylamide gel electrophoresis is considered to be due to its
highly acidic nature (pI = 4.18), because COS-7 cells transfected
with parchorin cDNA produced a protein with apparent molecular mass
of 120 kDa on 6% SDS-polyacrylamide gel electrophoresis. Parchorin is
a novel protein that has significant homology to the family of chloride
intracellular channels (CLIC), especially the chloride channel from
bovine kidney, p64, in the C-terminal 235 amino acids. When expressed
as a fusion protein with green fluorescent protein (GFP) in the LLC-PK1
kidney cell line, GFP-parchorin, unlike other CLIC family members,
existed mainly in the cytosol. Furthermore, when Cl The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AB035520.
Molecular Cloning and Characterization of a Novel Chloride
Intracellular Channel-related Protein, Parchorin, Expressed in
Water-secreting Cells*
,,
Laboratory of Pharmacology and Toxicology
and the § Department of Neuropathology and Neuroscience,
Graduate School of Pharmaceutical Sciences, The University of Tokyo,
Tokyo 113-0033, Japan and the ¶ Department of Molecular and Cell
Biology, University of California, Berkeley, California 94720
efflux from the cell was elicited, GFP-parchorin translocated to the
plasma membrane. These results suggest that parchorin generally plays a
critical role in water-secreting cells, possibly through the regulation
of chloride ion transport.
*
This study was supported in part by Japanese Ministry of
Education, Science, Sports and Culture Grants 09672216 and 10557219. Mass spectra were obtained at the University of California-San Francisco Mass Spectrometry Facility (A. L. Burlingame, Director), which is supported by the Biomedical Research Technology Program of the
National Center for Research Resources (National Institutes of Health
Grants NCRR BRTP RR01614 and RR08282).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.:
81-3-5841-4862; Fax: 81-3-5841-4867; E-mail:
urushi@mol.f.u-tokyo.ac.jp.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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