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Vol. 10, Issue 5, 1463-1475, May 1999
Involves Exocytosis of Endolysosome-related Vesicles
§
and
*National Cancer Institute, 16132 Genova, Italy; Interleukin 1National Cancer
Institute of Genova, Biotechnology Section, Rome, Italy; Department
of Experimental Medicine and Pathology, University of Rome "La
Sapienza," 00167 Rome, Italy; §Istituto Dermatologico
San Gallicano, Istituto di Ricovero e Cura a Carattere
Scientifico, 00100 Rome, Italy; and Centre d'Immunologie de
Marseille-Luminy, 13288 Marseille, France
(IL-1), a secretory protein lacking a signal
peptide, does not follow the classical endoplasmic
reticulum-to-Golgi pathway of secretion. Here we provide the
evidence for a "leaderless" secretory route that uses regulated
exocytosis of preterminal endocytic vesicles to transport cytosolic
IL-1 out of the cell. Indeed, although most of the IL-1 precursor
(proIL-1) localizes in the cytosol of activated human monocytes, a
fraction is contained within vesicles that cofractionate with late
endosomes and early lysosomes on Percoll density gradients and display
ultrastructural features and markers typical of these organelles. The
observation of organelles positive for both IL-1 and the
endolysosomal hydrolase cathepsin D or for both IL-1 and the
lysosomal marker Lamp-1 further suggests that they belong to the
preterminal endocytic compartment. In addition, similarly to lysosomal
hydrolases, secretion of IL-1 is induced by acidotropic drugs.
Treatment of monocytes with the sulfonylurea glibenclamide inhibits
both IL-1 secretion and vesicular accumulation, suggesting that this
drug prevents the translocation of proIL-1 from the cytosol into the
vesicles. A high concentration of extracellular ATP and hypotonic
medium increase secretion of IL-1 but deplete the vesicular
proIL-1 content, indicating that exocytosis of
proIL-1-containing vesicles is regulated by ATP and osmotic conditions.
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