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(Received for publication, December 20, 1995, and in revised form, March 6, 1996)
From the Mitsubishi Kasei Institute of Life Sciences, Machida,
Tokyo 194, Japan and Protein kinase C-mediated phosphorylation of a
25-kDa synaptosome-associated protein (SNAP-25) was examined in
living PC12 cells. Phorbol 12-myristate 13-acetate treatment
enhanced high potassium-induced [3H]-norepinephrine
release, and a 28-kDa protein recognized by an anti-SNAP-25 antibody
was phosphorylated on Ser residues. The molecular size of the
phosphorylated band decreased slightly following treatment with
Clostridium botulinum type A neurotoxin, whereas the band
disappeared after treatment with botulinum type E neurotoxin,
indicating that the 28-kDa protein was SNAP-25. A phosphorylation is
likely to occur at Ser187, as this is the only Ser residue
located between the cleavage sites of botulinum type A and E
neurotoxins. SNAP-25 of PC12 cells was phosphorylated by purified
protein kinase C in vitro, and the amount of syntaxin
co-immunoprecipitated with SNAP-25 was decreased by phosphorylation.
These results suggest that the phosphorylation of SNAP-25 may be
involved in protein kinase C-mediated regulation of catecholamine
release from PC12 cells.
Volume 271, Number 24,
Issue of June 14, 1996
pp. 14548-14553
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
POSSIBLE INVOLVEMENT IN PROTEIN KINASE C-MEDIATED REGULATION
OF NEUROTRANSMITTER RELEASE
,
and
Department of Veterinary Science,
College of Agriculture, University of Osaka Prefecture, Sakai, Osaka
593, Japan
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