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Blood, 1 October 2001, Vol. 98, No. 7, pp. 2152-2159
IMMUNOBIOLOGY
CD8+ T lymphocytes induce polarized
exocytosis of secretory lysosomes by dendritic cells with release of
interleukin-1 and cathepsin D
Stefania Gardella,
Cristina Andrei,
Lavinia Vittoria Lotti,
Alessandro Poggi,
M. Rosaria Torrisi,
M.
Raffaella Zocchi, and
Anna Rubartelli
From the Unit of Protein Biology, Laboratory of
Immunology, and Biotechnology Section of Roma, National Cancer
Research Institute, 16132 Genoa, Italy; Department of Experimental
Medicine and Pathology, University of Rome "La Sapienza," Rome,
Italy; Istituto Dermatologico San Gallicano IRCCS of Rome, Italy;
Laboratory of Tumor Immunology, San Raffaele Scientific Institute,
Milan, Italy.
We recently reported that human dendritic cells release the
leaderless secretory protein interleukin-1 (IL-1) following specific interaction with alloreactive T lymphocytes. To clarify the
molecular mechanism underlying this secretion, this study investigated
the intracellular trafficking of IL-1 in dendritic cells and the
signal(s) regulating its release. Results show that a fraction of the
intracellular IL-1 precursor colocalizes with the hydrolase
cathepsin D in endolysosomes of dendritic cells; secretion of both
proteins is elicited by stimuli that induce intracellular calcium
increases. Alloreactive CD8+ T lymphocytes generate a
Ca++ influx in dendritic cells followed by enrichment in
endolysosomes containing IL-1 and cathepsin D beneath the membrane
in contact with T cells. These events result in polarized exocytosis of
secretory lysosomes, mediated by microtubules, with release of IL-1
and cathepsin D toward the interacting CD8+ T cell.
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