G. Way
Purification and identification of secernin, a novel cytosolic protein that regulates exocytosis in mast cells
Way, G.; Morrice, N.; Smythe, C.; O'Sullivan, A.J.
Authors
N. Morrice
C. Smythe
A.J. O'Sullivan
Abstract
After permeabilization with the pore-forming toxin streptolysin-O mast cells can be triggered to secrete by addition of both calcium and a GTP analogue. If stimulation is delayed after permeabilization, there is a progressive decrease in the extent of secretion upon stimulation, eventually leading to a complete loss of the secretory response. This loss of secretory response can be retarded by the addition of cytosol from other secretory tissues, demonstrating that the response is dependent on a number of cytosolic proteins. We have used this as the basis of a bioassay to purify Secernin 1, a novel 50-kDa cytosolic protein that appears to be involved in the regulation of exocytosis from peritoneal mast cells. Secernin 1 increases both the extent of secretion and increases the sensitivity of mast cells to stimulation with calcium.
Citation
Way, G., Morrice, N., Smythe, C., & O'Sullivan, A. (2002). Purification and identification of secernin, a novel cytosolic protein that regulates exocytosis in mast cells. Molecular Biology of the Cell, 13(9), 3344-3354. https://doi.org/10.1091/mbc.e01-10-0094
Journal Article Type | Article |
---|---|
Publication Date | Sep 1, 2002 |
Deposit Date | Oct 1, 2008 |
Publicly Available Date | Oct 1, 2008 |
Journal | Molecular biology of the cell |
Publisher | American Society for Cell Biology |
Peer Reviewed | Peer Reviewed |
Volume | 13 |
Issue | 9 |
Pages | 3344-3354 |
DOI | https://doi.org/10.1091/mbc.e01-10-0094 |
Keywords | Permeabilized cells, Hematopoietic-cells, Chromaffin cells, Membrane-fusion, Streptolysin-O, Kinase-C, Secretion, RAC. |
Publisher URL | http://www.molbiolcell.org/cgi/content/full/13/9/3344 |
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