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Affinity purified tetanus toxin binds to isolated chromaffin granules and inhibits catecholamine release in digitonin‐permeabilized chromaffin cells
Author(s) -
Lazarovici Philip,
Fujita Ko,
Contreras Margarita L.,
DiOrio James P.,
Lelkes Peter I.
Publication year - 1989
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 - 10.1016/0014-5793(89)80943-3
Subject(s) - digitonin , toxin , chromaffin cell , adrenal medulla , neurotoxin , biochemistry , granule (geology) , chemistry , intracellular , biology , catecholamine , membrane , endocrinology , paleontology
Tetanus toxin, a potent neurotoxin which blocks neurotransmitter release in the CNS, also inhibits Ca 2+ ‐induced catecholamine release from digitonin‐permeabilized, but not from intact bovine chromaffin cells. In searching for intracellular targets for the toxin we studied the binding of affinity‐purified tetanus toxin to bovine adrenal chromaffin granules. Tetanus toxin bound in a neuraminidase‐sensitive fashion to intact granules and to isolated granule membranes, as assayed biochemically and visualized by electron microscopic techniques. The binding characteristics of the toxin to chromaffin granule membranes are very similar to the binding of tetanus toxin to brain synaptosomal membranes. We suggest that the toxin‐binding site is a glycoconjugate of the G1b type (a polysialoganglioside or a glycoprotein‐proteoglycan) which is localized on the cytoplasmic face of the granule membrane and might directly be involved in exocytotic membrane fusion.