Inhibition of exocytosis by intracellularly applied antibodies against a chromaffin granule-binding protein

Exocytotic secretion requires the interaction and fusion of secretory vesicles with the plasma membrane. This process could be mediated by specific recognition molecules acting as intracellular, membrane-bound receptors and ligands. One possible component of such a recognition site on the plasma mem...

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Bibliographic Details
Published in:	Nature (London) Vol. 339; no. 6227; pp. 709 - 712
Main Authors:	Schiweizer, Felix E, Schäfer, Theo, Tapparelli, Carlo, Grob, Marianne, Karli, Urs O, Heumann, Rolf, Thoenen, Hans, Bookman, Richard J, Burger, Max M
Format:	Journal Article
Language:	English
Published:	London Nature Publishing 29-06-1989 Nature Publishing Group
Subjects:	Adrenal Medulla - physiology Animals Antibodies - isolation & purification Antigen-Antibody Complex Biological and medical sciences Blood Carrier Proteins - immunology Carrier Proteins - isolation & purification Carrier Proteins - physiology Cattle Cell Line Cell Membrane - physiology Cell physiology Cells, Cultured Cellular biology chromaffin cells Chromaffin Granules - physiology Chromaffin System - physiology Exocytosis Fundamental and applied biological sciences. Psychology Medical research Membranes Molecular and cellular biology Molecular Weight Protease Inhibitors - pharmacology Proteins rats Secretion. Exocytosis Membrane protein Rat Antibody Rodentia Exocytosis Binding protein Vertebrata Mammalia Chromaffin granule Plasma membrane Immunoblotting assay Inhibition Micrography
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Summary:	Exocytotic secretion requires the interaction and fusion of secretory vesicles with the plasma membrane. This process could be mediated by specific recognition molecules acting as intracellular, membrane-bound receptors and ligands. One possible component of such a recognition site on the plasma membrane is a protein of relative molecular mass (Mr) 51,000 (51K) that has been isolated from bovine adrenal chromaffin cells. This protein binds strongly to chromaffin granules, the secretory vesicles of these cells. To determine the function of this membrane-anchored chromaffin granule-binding protein in exocytosis, we tested the effect of intracellularly injected antibodies on secretion. Here we show, by two independent techniques in two different cell types, that antibodies against this protein inhibit exocytosis. In rat pheochromocytoma cell cultures, monospecific antibodies, applied by erythrocyte ghost fusion, impair the release of 3H-noradrenaline. The same antibodies, introduced into individual chromaffin cells through a patch pipette, block exocytosis, as revealed by the measurement of membrane capacitance. These results demonstrate the functional involvement in exocytosis of a plasma membrane protein with high affinity for secretory vesicles.
Bibliography:	ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2
ISSN:	0028-0836 1476-4687
DOI:	10.1038/339709a0