The light chain of tetanus neurotoxin (TeTx) is a zinc endopeptidase specific for VAMP/synaptobrevin (VAMP), a 120-amino-acid integral protein previously described in the small synaptic vesicles of neuronal cells. TeTx has been shown to be active also on nonneuronal cells. By SDS-PAGE and quantitative immunoblotting on proteins derived from murine macrophages (M phi) exposed to TeTx, we have shown that: (1) VAMP-related proteins are also present in M phi and (2) such proteins are sensitive to TeTx proteolytic cleavage. The demonstration that TeTx acts on VAMP-related proteins also in M phi offers a new and useful tool for molecular studies on M phi exocytosis.
Tetanus toxin-sensitive VAMP-related proteins are present in murine macrophages / Pitzurra, L; Rossetto, O; Chimienti, Ar; Blasi, Elisabetta; Bistoni, F.. - In: CELLULAR IMMUNOLOGY. - ISSN 0008-8749. - ELETTRONICO. - 169:(1996), pp. 113-116.
Tetanus toxin-sensitive VAMP-related proteins are present in murine macrophages
BLASI, Elisabetta;
1996
Abstract
The light chain of tetanus neurotoxin (TeTx) is a zinc endopeptidase specific for VAMP/synaptobrevin (VAMP), a 120-amino-acid integral protein previously described in the small synaptic vesicles of neuronal cells. TeTx has been shown to be active also on nonneuronal cells. By SDS-PAGE and quantitative immunoblotting on proteins derived from murine macrophages (M phi) exposed to TeTx, we have shown that: (1) VAMP-related proteins are also present in M phi and (2) such proteins are sensitive to TeTx proteolytic cleavage. The demonstration that TeTx acts on VAMP-related proteins also in M phi offers a new and useful tool for molecular studies on M phi exocytosis.
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