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J Biol Chem, Vol. 274, Issue 24, 16754-16759, June 11, 1999
cAMP Regulates Ca2+-dependent Exocytosis
of Lysosomes and Lysosome-mediated Cell Invasion by
Trypanosomes
Ana
Rodríguez,
Iñigo
Martinez,
Albert
Chung,
Catherine H.
Berlot§, and
Norma W.
Andrews
From the Departments of Cell Biology and § Cellular and
Molecular Physiology, Yale University School of Medicine, New
Haven, Connecticut, 06520
Ca2+-regulated exocytosis,
previously believed to be restricted to specialized cells, was recently
recognized as a ubiquitous process. In mammalian fibroblasts and
epithelial cells, exocytic vesicles mobilized by Ca2+ were
identified as lysosomes. Here we show that elevation in intracellular
cAMP potentiates Ca2+-dependent exocytosis of
lysosomes in normal rat kidney fibroblasts. The process can be
modulated by the heterotrimeric G proteins Gs and
Gi, consistent with activation or inhibition of adenylyl cyclase. Normal rat kidney cell stimulation with isoproterenol, a
-adrenergic agonist that activates adenylyl cyclase, enhances Ca2+-dependent lysosome exocytosis and cell
invasion by Trypanosoma cruzi, a process that involves
parasite-induced [Ca2+]i transients and fusion of
host cell lysosomes with the plasma membrane. Similarly to what is
observed for T. cruzi invasion, the actin cytoskeleton acts
as a barrier for Ca2+-induced lysosomal exocytosis. In
addition, infective stages of T. cruzi trigger elevation in
host cell cAMP levels, whereas no effect is observed with noninfective
forms of the parasite. These findings demonstrate that cAMP regulates
lysosomal exocytosis triggered by Ca2+ and a parasite/host
cell interaction known to involve
Ca2+-dependent lysosomal fusion.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.

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Copyright © 1999 by the American Society for Biochemistry and Molecular Biology.
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