Way, G. and Morrice, N. and Smythe, C. and O'Sullivan, A. J. (2002) 'Purification and identification of secernin, a novel cytosolic protein that regulates exocytosis in mast cells.', Molecular biology of the cell., 13 (9). pp. 3344-3354.
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.
|Keywords:||Permeabilized cells, Hematopoietic-cells, Chromaffin cells, Membrane-fusion, Streptolysin-O, Kinase-C, Secretion, RAC.|
|Full text:||PDF - Published Version (527Kb)|
|Publisher Web site:||http://dx.doi.org/10.1091/mbc.E01-10-0094|
|Publisher statement:||© 2002 by The American Society for Cell Biology|
|Record Created:||01 Oct 2008|
|Last Modified:||26 Aug 2011 14:24|
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