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J Biol Chem, Vol. 273, Issue 16, 9842-9851, April 17, 1998

Lysosomal Enzyme Trafficking between Phagosomes, Endosomes, and Lysosomes in J774 Macrophages
ENRICHMENT OF CATHEPSIN H IN EARLY ENDOSOMES

Volker Claus, Andrea Jahraus^§, Torunn Tjelle^¶, Trond Berg^¶, Heidrun Kirschke, Heinz Faulstich, and Gareth Griffiths^§

From the  Max Planck Institute for Medical Research, Heidelberg, ^§ EMBL, 69117 Heidelberg, Germany, ^¶ Department of Biology, University of Oslo, Oslo, 0316 Norway, and  Department of Biochemistry, University of Halle, D-06097 Halle, Germany

In this study we take advantage of recently developed methods using J774 macrophages to prepare enriched fractions of early endosomes, late endosomes, dense lysosomes, as well as phagosomes of different ages enclosing 1-µm latex beads to investigate the steady state distribution and trafficking of lysosomal enzyme activity between these organelles. At steady state these cells appear to possess four different cellular structures, in addition to phagolysosomes, where acid hydrolases were concentrated. The first site of hydrolase concentration was the early endosomes, which contained the bulk of the cellular cathepsin H. This enzyme was acquired by phagosomes significantly faster than the other hydrolases tested. The second distinct site of lysosomal enzyme concentration was the late endosomes which contain the bulk of cathepsin S. The third and fourth large pools of hydrolases were found in two functionally distinct types of dense lysosomes, only one of which was found to be secreted in the presence of chloroquine or bafilomycin. Among this secreted pool was soluble furin, generally considered only as a membrane-bound trans-Golgi network resident protein. Thus, the organelles usually referred to as "lysosomes" in fact encompass a growing family of highly dynamic but functionally distinct endocytic organelles.

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