Recently an isoform of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) was isolated from rabbit brain which catalyzes fusion of membrane of membranes containing plasmenylethanolamine lipids, which readily adopt an inverted hexagonal phase. Here, we demonstrate that this GAPDH isoform can catalyze fusion between naturally occurring subcellular membranes involved in insulin exocytosis. With purified pancreatic islet b-cell plasma membranes and secretory granules, the GAPDH isoform catalyzes fusion of the two membrane populations in a manner that is inhibited by monoclonal antibodies directed against GAPDH. Both membrane compartments were required, and the GAPDH isoform did not catalyze fusion of one secretory granule population with another. HIT insulinoma cells were demonstrated to contain a similar fusion-catalyzing activity in cytosol. The fusion factors failed to catalyze fusion of membranes which had been depleted of plasmenylethanolamine species by exposure to acid. Such treatment has been demonstrated by electrospray ionization tandem mass spectrometry to destroy the plasmenylethanolamine species in these membranes.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR000954-22
Application #
6118512
Study Section
Project Start
1998-08-01
Project End
1999-07-31
Budget Start
1997-10-01
Budget End
1998-09-30
Support Year
22
Fiscal Year
1998
Total Cost
Indirect Cost
Name
Washington University
Department
Type
DUNS #
062761671
City
Saint Louis
State
MO
Country
United States
Zip Code
63130
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