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Photo-Induced Cross-Linking of Unmodified Proteins (PICUP) Applied to Amyloidogenic Peptides
Published on: January 12, 2009
The ubiquitously expressed pICln protein forms homomeric complexes in vitro
G Buyse1, C de Greef, L Raeymaekers
1Laboratory of Physiology, Catholic University of Leuven (K.U. Leuven), Belgium.
Biochemical and Biophysical Research Communications
|January 26, 1996
Summary
The study investigated the role of the pICln protein in endothelial cell volume-sensitive chloride currents. Researchers found widespread expression of pICln in various cells, suggesting its involvement in regulating these currents.
Area of Science:
- Cell biology
- Ion channel physiology
- Molecular biology
Background:
- Endothelial cells possess a chloride conductance sensitive to cell volume.
- This conductance shares properties with a swelling-activated chloride current linked to the pICln protein.
- pICln may function as a chloride channel or a regulator.
Purpose of the Study:
- To investigate the potential involvement of pICln in the endothelial volume-sensitive chloride current.
- To clone human pICln and characterize its protein expression.
Main Methods:
- Cloning of human pICln.
- Protein expression analysis using a polyclonal antiserum.
- Electrophoresis to study protein migration.
- In vitro complex formation assay for bacterially expressed pICln.
Main Results:
- Human pICln was successfully cloned.
- Widespread expression of pICln protein was detected in endothelial cells and other cell lines.
- pICln exhibited anomalous migration during SDS-PAGE.
- Bacterially expressed pICln formed homomeric complexes in vitro.
Conclusions:
- pICln is widely expressed, including in endothelial cells.
- The protein's characteristics suggest a role in cellular chloride transport mechanisms.
- Further studies are warranted to elucidate pICln's specific function in endothelial volume regulation.
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