Purified lens junctional protein forms channels in planar lipid films.
Junctions isolated from bovine lenses were solubilized with the detergent octyl glucoside, and their protein(s) was reconstituted in unilamellar vesicles. The protein(s) appears as annular-shaped intramembrane particles approximately equal to 10 nm in diameter on the vesicles' fracture faces. The addition of the vesicle-containing junctional protein(s) to both sides of preformed lipid films induced voltage-dependent channels. The channels have a conductance of 200 pS in 0.1 M salt solutions and are thus large enough to account for the electrical coupling observed between intact lens fibers; they turn off when the magnitude of the voltage is increased and in the presence of octanol. Although the identity of the reconstituted channels as the communicating pathway between lens fibers remains to be proven, it is most likely that the reconstituted channels are formed by MIP-26, the major protein component of the isolated lens junctions.
G A
GA
Zampighi
J E
JE
Hall
M
M
Kreman
D000818:Animals; D020346:Aquaporins; D002417:Cattle; D004553:Electric Conductivity; D005136:Eye Proteins / Q000302:isolation & purification / Q000502:physiology*; D005614:Freeze Fracturing; D007365:Intercellular Junctions; D007473:Ion Channels; D008051:Lipid Bilayers; D008081:Liposomes; D008562:Membrane Glycoproteins; D008564:Membrane Potentials; D008970:Molecular Weight
D020346:Aquaporins; D005136:Eye Proteins; D007473:Ion Channels; D008051:Lipid Bilayers; D008081:Liposomes; D008562:Membrane Glycoproteins; C030328:aquaporin 0