Tetanus toxin-sensitive VAMP-related proteins are present in murine macrophages.
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 (Mphi) exposed to TeTx, we have shown that: (1) VAMP-related proteins are also present in Mphi and (2) such proteins are sensitive to TeTx proteolytic cleavage. The demonstration that TeTx acts on VAMP-related proteins also in Mphi offers a new and useful tool for molecular studies on Mphi exocytosis.
Pitzurra
L
L
Department of Experimental Medicine and Biochemical Sciences, University of Perugia, Italy.
Rossetto
O
O
Chimienti
A R
AR
Blasi
E
E
Bistoni
F
F
D000818:Animals; D002478:Cells, Cultured; D017737:Macrophages, Peritoneal / Q000378:metabolism*; D008565:Membrane Proteins / Q000032:analysis* / Q000378:metabolism; D051379:Mice; D050683:R-SNARE Proteins; D013744:Tetanus Toxin / Q000378:metabolism*
D008565:Membrane Proteins; D050683:R-SNARE Proteins; D013744:Tetanus Toxin