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J Biol Chem, Vol. 274, Issue 24, 16901-16906, June 11, 1999
From the Department of Medicine, Cardiovascular Research, Brigham
and Women's Hospital, Harvard Medical School, Boston, Massachusetts
02115
This study examines the role of sphingolipids in
mediating the apoptosis of PC12W cells induced by the angiotensin II
type 2 (AT2) receptor. PC12W cells express abundant
AT2 receptor but not angiotensin II type 1 receptor and
undergo apoptosis when stimulated by angiotensin II. AT2
receptor-induced ceramide accumulation preceded the onset of caspase 3 activation and DNA fragmentation. AT2 receptor-induced
ceramide accumulation did not result from the degradation of complex
sphingolipids (SL) such as sphingomyelin or glycosphingolipids, as no
changes in neutral or acidic sphingomyelinase activities, sphingomyelin
level, nor in cellular glycolipid composition were observed.
AT2 receptor activated serine palmitoyltransferase with a
maximum time of 24 h after angiotensin II stimulation. The
AT2 receptor-induced accumulation of ceramide was blocked by inhibitors of the de novo pathway of SL synthesis,
-chloro-L-alanine and fumonisin B1.
Inhibition of the de novo biosynthesis of SLs by fumonisin
B1 and -chloro-L-alanine completely
abrogated the AT2 receptor-mediated apoptosis. Pertussis
toxin and orthovanadate blocked AT2 receptor-mediated
ceramide production. Taken together our data demonstrate that in PC12W
cells the stimulation of AT2 receptor induces the
activation of de novo pathway, and a metabolite of this
pathway, possibly ceramide, mediates AT2 receptor-induced apoptosis.
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