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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

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 G_s and G_i, 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.

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