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MBC in Press, published online ahead of print July 11, 2002
Mol. Biol. Cell 10.1091/mbc.E01-10-0094

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Submitted on October 16, 2001
Revised on May 10, 2002
Accepted on June 5, 2002

Purification and identification of Secernin, a novel cytosolic protein that regulates exocytosis in mast cells

Gemma Way1, Nicholas Morrice2, Carl Smythe2, and Antony J. O'Sullivan1*

1 Department of Biological and Biomedical Sciences, University of Durham, South Road, Durham, DH1 3LE, United Kingdom
2 Division of Cell Signalling, School of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland

* Corresponding author. E-mail address: a.j.osullivan{at}durham.ac.uk.

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 following 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 upon a number of cytosolic proteins. We have used this as the basis of a bioassay to purify Secernin 1, a novel 50kD 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.




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