Areas of Interest
My research has two primary goals. The first is to elucidate
the molecular basis of visual excitation and adaptation. The
basic approach is to use electrophysiological and
pharmacological techniques to study phototransduction of
individual photoreceptor cells. The second, done in
collaboration with Dr. Terasaki, is to study membrane disruption
and repair using combined electrophysiological and optical
techniques.
Lab Rotation Projects
Fein/Terasaki Lab
Cell Wounding Project
We have developed an electrophysiological method for
studying plasma membrane wound repair in single cells. Large
plasma membrane disruptions in starfish oocytes, made by
femtosecond pulses from a Ti-Sapphire laser, are repaired within
a few seconds as shown by stabilization of membrane electrical
properties and restoration of dye exclusion. The membrane
potential after wounding is sensitive to the extracellular Cl-
concentration but not to that of Na+, K+ or H+ indicating that
Cl- permeable intracellular membranes have fused with the plasma
membrane. We believe that cell wounding provides a novel means
for the electrophysiological analysis of chloride permeable
intracellular membranes that have been translocated to the
plasma membrane.
Selected Publications
Fein, A., and Terasaki, M. 2005. Rapid increase in plasma
membrane chloride permeability during wound resealing in
starfish oocytes. J. Gen. Physiol. 126: 151-159.
Fein, A. 2003. Inositol 1,4,5-trisphosphate-induced calcium
release is necessary for generating the entire light response of
Limulus ventral photoreceptors. J. General Physiology. 121:
441-449.
Fein, A. and S. Bernaski. 2000. Divergent mechanisms for
phototransduction of invertebrate microvillar photoreceptors.
Visual Neuroscience 17: 911-917.
Tertyshnikova, S. and A. Fein. 2000. Dual regulation of
calcium mobilization by inositol 1,4,5-trisphosphate in a living
cell. J. Gen. Physiol. 115: 481-489.
La Plante, J.M., O'Rourke, F., Lu, X., Fein, A., Olsen, A.
and M.B. Feinstein. 2000. Cloning of a human cDNA which encodes
CHERP, a novel Calcium Homeostasis Endoplasmic Reticulum
Protein: regulated expression of antisense cDNA depletes CHERP,
inhibits intracellular calcium mobilization by thrombin and
decreases cell proliferation in HEL cells. Biochemical J. 348:
189-199. |
