The membrane protein syntaxin (originally named HPC-1) is involved in vesic
le trafficking and required for neurotransmitter release at nerve terminals
. The presence of syntaxin on target membranes is hypothesized to confer sp
ecificity to targeting and fusion via interactions with complementary vesic
le-associated proteins. To elucidate the function of syntaxin 1A in exocyto
sis, HPC-1/syntaxin 1A-reduced PC12h cells (PC12h/Delta syx) that were stab
ly transfected with a plasmid for antisense syntaxin 1A expression were con
structed. Depolarizing stimulation of PC12h/Delta syx enhanced dopamine rel
ease, compared with PC12h, There was a strong inverse correlation between s
yntaxin 1A protein expression and enhancement of dopamine release. Reductio
n of syntaxin 1A had no effect on increase of the cytoplasmic free Ca2+ con
centration by depolarized stimulation. Moreover, PC12h/Delta syx clones sim
ilarly enhanced of exocytosis by native secretagogues, These results indica
te that syntaxin 1A has more than one function in exocytosis.