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Endobrevin/VAMP8 mediates exocytotic release of hexosaminidase from rat basophilic leukaemia cells
Author(s) -
Lippert Undine,
Ferrari David M.,
Jahn Reinhard
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.06.057
Subject(s) - exocytosis , microbiology and biotechnology , degranulation , basophilic , histamine , mast cell , secretory vesicle , biology , endosome , hexosaminidase , lipid bilayer fusion , chemistry , biochemistry , secretion , immunology , membrane , receptor , enzyme , endocrinology , medicine , pathology , intracellular
Mast cells are important players in innate immunity and mediate allergic responses. Upon stimulation, they release biologically active mediators including histamine, cytokines and lysosomal hydrolases. We used permeabilized rat basophilic leukaemia cells as model to identify R‐SNAREs (soluble NSF ( N ‐ethylmaleimide‐sensitive fusion protein)) mediating exocytosis of hexosaminidase from mast cells. Of a complete set of recombinant mammalian R‐SNAREs, only vesicle associated membrane protein (VAMP8)/endobrevin consistently blocked hexosaminidase release, which was also insensitive to treatment with clostridial neurotoxins. Thus, VAMP8, which also mediates fusion of late endosomes and lysosomes, plays a major role in hexosaminidase release, strengthening the view that mast cell granules share properties of both secretory granules and lysosomes.