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J Biol Chem, Vol. 275, Issue 16, 12023-12031, April 21, 2000
From the Departments of In mammalian cells, activation of a
Golgi-associated phospholipase D by ADP-ribosylation factor results in
the hydrolysis of phosphatidylcholine to form phosphatidic acid (PA).
This reaction stimulates the release of nascent secretory vesicles from
the trans-Golgi network of endocrine cells. To understand the role of
PA in mediating secretion, we have exploited the transphosphatidylation activity of phospholipase D. Rat anterior pituitary GH3 cells, which
secrete growth hormone and prolactin, were treated with 1-butanol
resulting in the synthesis of phosphatidylbutanol rather than PA. Under
these conditions transport from the ER through the Golgi apparatus and
secretion of polypeptide hormones were inhibited quantitatively.
Furthermore, the in vitro synthesis of phosphatidylinositol
4,5-bisphosphate (PtdIns(4,5)P2) by Golgi membranes was
inhibited quantitatively. Most significantly, in the presence of
1-butanol the architecture of the Golgi apparatus was disrupted,
resulting in its disassembly and fragmentation. Removal of the alcohol
resulted in the rapid restoration of Golgi structure and secretion of
growth hormone and prolactin. Our results suggest that PA stimulation
of PtdIns(4,5)P2 synthesis is required for maintaining the
structural integrity and function of the Golgi apparatus.
Inhibition of Phosphatidic Acid Synthesis Alters the Structure of
the Golgi Apparatus and Inhibits Secretion in Endocrine Cells*
,¶
Developmental and Molecular
Biology, § Molecular Pharmacology, and ¶ Anatomy and
Structural Biology, Albert Einstein College of Medicine,
Bronx, New York 10461
*
This work was supported by National Institutes of Health
Grants DK21860 (to D. S.) and GM55692 (to J. M. B.) and
in part by a grant from the Juvenile Diabetes Foundation (to D. S.). Core support was provided by National Institutes of Health Cancer
Center Grant P30CA13330.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Dept. of
Developmental and Molecular Biology, Albert Einstein College of
Medicine, 1300 Morris Park Ave., Bronx, NY 10461. Tel.: 718-430-2653;
Fax: 718-430-8567; E-mail: shields@aecom.yu.edu.
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