Affinity purified tetanus toxin binds to isolated chromaffin granules and inhibits catecholamine release in digitonin‐permeabilized chromaffin cells

FEBS Letters

Lazarovici, Philip¹  Fujita, Ko⁴  Contreras, Margarita L.³  DiOrio, James P.⁵  Lelkes, Peter I.² 

[1] Department of Pharmacology and Experimental Therapeutics, Hadassah School of Medicine, Jerusalem 91010 Israel;Laboratory of Cell Biology, University of Wisconsin Medical School, Milwaukee Clinical Campus, Sinai Samaritan Medical Center, Milwaukee, WI 53201, USA;Department of Pharmacology and Toxicology, Michigan State University, MI 48824, USA;Section on GrowthFactors, NICHD, NIH, Bethesda, MD 20892, USA;Hemostasis Research Laboratory University of Wisconsin Medical School, Milwaukee Clinical Campus, Sinai Samaritan Medical Center, Milwaukee, WI 53201, USA

关键词: Chromaffin granule;    Tetanus toxin;    Catecholamine secretion;    Polysialoglyconjugate;    Exocytosis;    (Chromaffin cell);    GD1b;    galactosyl-N-acetylgalactosaminyl-[N-acetylneuraminyl -N-acetylneuraminyl]galactosylglucosylceramide;    GT1b;    galactosyl-N-acetylgalactosaminyl-[N-acetylneuraminyl-N-acetylneuraminyl-N-acetylneuraminyl]galactosylglucosylceramide;    TeToB;    tetanus toxin ‘B’ form;    affinity purified on a ‘G1b’ ganglioside gel;    TT;    tetanus toxin;   

DOI  :  10.1016/0014-5793(89)80943-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Tetanus toxin, a potent neurotoxin which blocks neurotransmitter release in the CNS, also inhibits Ca²⁺-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.

【 授权许可】

Unknown