The ubiquitously expressed pICln protein forms homomeric complexes in vitro.
Endothelial cells contain a cell-volume sensitive chloride conductance with biophysical properties similar to those of a ubiquitously expressed chloride current that is activated by cell swelling. The latter current has been associated with the ICln protein (pICln) which may be the chloride channel itself or, alternatively, a channel regulator. We were therefore interested in whether pICln is involved in the endothelial volume-sensitive chloride current. As a first step, we have cloned human pICln and studied its expression at the protein level. Using a polyclonal antiserum raised against human pICln we found a widespread expression of pICln, both in endothelial cells and in other cell lines. A characteristic feature of pICln is its anomalous migration during denaturing polyacrylamide gel electrophoresis. We also demonstrate that bacterially expressed pICln forms homomeric complexes in vitro.
Buyse
G
G
Laboratory of Physiology, Catholic University of Leuven (K.U. Leuven), Belgium.
de Greef
C
C
Raeymaekers
L
L
Droogmans
G
G
Nilius
B
B
Eggermont
J
J
D001483:Base Sequence; D002118:Calcium / Q000737:chemistry; D018118:Chloride Channels / Q000737:chemistry* / Q000235:genetics; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000235:genetics; D003902:Detergents; D006801:Humans; D007158:Immunologic Techniques; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D008970:Molecular Weight; D012995:Solubility
D018118:Chloride Channels; D018076:DNA, Complementary; D003902:Detergents; D046911:Macromolecular Substances; D002118:Calcium