Dr. Rane's Laboratory
by
Kathleen H. Sauer
—
last modified
Feb 27, 2008 03:24 PM
My laboratory is currently working on the role of exocytosis in neutrophil priming by directly inhibiting the interaction of the SNARE proteins that mediate granule exocytosis. We are using a novel approach, generating TAT-fusion peptides mimicking the two coiled-coil domains of SNAP-23 and the coiled-coil SNARE domain of other SNARE proteins such as syntaxin 4 and VAMP-2, to inhibit neutrophil exocytosis. Our goal is to elucidate if granule exocytosis is necessary for neutrophil priming and also to determine if p38 MAPK activation contributes to priming mechanisms independently of exocytosis.
PI: Silvia M. Uriarte, Ph.D.
Dates: 07/01/2007 – 06/30/2009
Title: "Mechanisms of neutrophil priming"
The goal of this project is to examine the role of granule exocytosis in neutrophil priming by directly inhibiting the interaction of SNARE proteins that mediate granule exocytosis Role: PI
Research Technicians
Junyi Le- Molecular biology techniques and protein purificationResearch Support
Agency: American Heart AssociationPI: Silvia M. Uriarte, Ph.D.
Dates: 07/01/2007 – 06/30/2009
Title: "Mechanisms of neutrophil priming"
The goal of this project is to examine the role of granule exocytosis in neutrophil priming by directly inhibiting the interaction of SNARE proteins that mediate granule exocytosis Role: PI


