University of Pennsylvania
School of Dental Medicine
4001 Spruce Street
Philadelphia, PA 19104
Email - firstname.lastname@example.org
The retinal rod photoreceptor is a
highly polarized postmitotic cell type responsible for the initial
events in phototransduction. The outer segment portion of the
rod cell encloses densely packed, closed, flattened membranous
sacs referred to as disks which are stacked along the length of
the outer segment. The continuous processes of disk membrane formation
and shedding maintains the ROS at a constant length. The primary
focus of the work in this laboratory involves the characterization
of a fundamental cellular process, membrane fusion in maintaining
the structural integrity of the rod cell. To this end both promoters
of membrane fusion such as phospholipase induced membrane destablilizations
(as measured by 31P NMR) and fusion inhibitors such as cytoskeletal
proteins are being studied. It is essential that in order to maintain
its structural integrity, thereby function effectively, the ROS
must not undergo indiscriminate membrane fusion. At the same time,
membrane fusion events are necessary in the formation of new disks
from the plasma membrane and the phagocytosis of old disks by
the pigment epithelium. Thus by focusing on both the promoters
and inhibitors of ROS membrane fusion we can begin to determine
the regulatory elements in this process.
Recent Grant Support
Zeigler Foundation - E. Matilda Zeigler Award 2000-2008
National Eye Institute - P.I.
"Membrane Fusion in Retinal Rod Outer Segments" 1994 - 2008
Boesze-Battaglia, K., J. Dispoto and M. A. Kahoe. 2002. Selective Association of Photoreceptor Rom-1 With Triton X-100 Resistant Membrane Rafts from ROS Disk Membranes. J. Biol. Chem. 277, 41843-41849.
Kahn, M., Boesze-Battaglia, K., Stepp, D., Petrov, D., Huang, A., Mason, P-R, and Tulenko, T. Influence of Serum Cholesterol on Atherogenesis and Intimal Hyperplasia after Angioplasty, Inhibition by Amlodipine. Am J Physiol Heart Circ Physiol. Feb; 288:H591-600. 2005.
Boesze-Battaglia, K., Gretzula, C. and Schimmel, R.J. Membrane Cholesterol Raft Redistribution in Platelet Plasma Membrane Upon Agonist Stimulation. Macromolecular Symposia, 219, 59-71. 2005.
Damek-Poprawa, M., Krouse, J., Gretzula, C, and Boesze-Battaglia, K. A Novel Tetraspanin Fusion Protein, Peripherin-2, Requires a Region Upstream of the Fusion Domain for Activity, J. Biol. Chem. 280, 9217-24. 2005.
Boesze-Battaglia, K., Dave Besack,D. McKay, T., Zekavat, A., Otis, L., Jordan-Sciutto, K. and Shenker, B.J. Cholesterol-rich Membrane Microdomains Mediate Cell Cycle Arrest Induced by Actinobacillus actinomycetemcomitans Cytolethal Distending Toxin. Cellular Microbiology, 5, 823-826. 2006.
Damek-Poprawa, M., Golub,E. Otis, L., Harrison, G., Christine Phillips, C. and Boesze-Battaglia, K. Chondrocytes Utilize A Cholesterol Dependent Lipid Translocator to Externalize Phosphatidylserine. Biochemistry. 45, 3325-3328. 2006.
Boesze-Battaglia, K. Isolation of membrane rafts and signaling complexes. Methods. Mol. Boil. 332, 169-179. 2006.
Boesze-Battaglia, K., Stefano, F.P., Fitzgerald, C and Muller-Weeks, S. Rom-1 Potentiates Photoreceptor Specific Membrane Fusion Processes. Exp. Eye Res. 84, 22-31. 2007.
Boesze-Battaglia, K., Pankoski-Walker, L., Gretzula, C., Otis, L., Morris, F., Yeagle, P.L., Albert, A., and Damek-Poprawa, M.. The tetraspanin protein, peripherin-2, complexes with melanoregulin, a putative fusion regulator. Biochemistry, 46, 1256-1272. 2007.
Edrington, T. C. V, Lapointe, R., Yeagle, P.L, Gretzula, C.L. and Boesze-Battaglia, K. Peripherin-2: an intracellular analogy to viral fusion proteins. Biochemistry, 2007, epud ahead of print PMID 17323721.
Edrington, T.C. V Yeagle, P.L., Gretzula, C.L., and Boesze-Battaglia, K.. Calcium dependent association of calmodulin with the C-terminal domain of the tetraspanin protein peripherin/rds. Biochemistry 2007, epub PMID 17323925.