Ultrastructural localization of Charcot-Leyden crystal protein in human eosinophils and basophils.
The Charcot-Leyden crystal (CLC) protein with lysophospholipase activity and carbohydrate-binding properties is a characteristic constituent of eosinophils and basophils. We investigated its subcellular distribution using immunoelectron microscopy. Eosinophil progenitors, mature eosinophils and basophils all contained CLC protein in their cytosol and in the euchromatin of the nucleus. A minor population of granules in eosinophils, increasing in number with maturation, and a more abundant granule-population in basophils, were found to contain CLC protein. Double-labeling experiments showed, in eosinophils, that CLC protein-containing granules contain also eosinophil peroxidase, a characteristic specific granule protein. This suggests a relationship between the CLC protein-containing organelle and the specific granule. In basophils both the CLC protein positive and the negative granules showed the same characteristic particulate-like structure of the granular matrix and both share the same membrane marker CD63. In nasal polyps, macrophages were observed phagocytosing necrotic eosinophils. In these macrophages CLC protein-containing vesicles were observed, probably representing late endosomes. The dual (cytosolic/nuclear and granular) localization of CLC protein suggests that this protein enters both a secretory and a nonsecretory pathway during its biosynthesis, indicating functional roles for this protein both within the cell and extracellularly.
Calafat
J
J
Department of Cell Biology, The Netherlands Cancer Institute, Amsterdam.
Janssen
H
H
Knol
E F
EF
Weller
P F
PF
Egesten
A
A
D001491:Basophils / Q000378:metabolism / Q000648:ultrastructure*; D003460:Crystallization; D004804:Eosinophils / Q000378:metabolism / Q000648:ultrastructure*; D006023:Glycoproteins / Q000648:ultrastructure*; D006801:Humans; D008245:Lysophospholipase; D016253:Microscopy, Immunoelectron
D006023:Glycoproteins; D008245:Lysophospholipase; C011711:lysolecithin acylhydrolase