Localization of Charcot‐Leyden crystal protein in individual morphological phenotypes of human basophils stimulated by f‐Met peptide

Abstract

Seven individual f-Met peptide-activated human basophil phenotypes labelled by an ultrastructural immunogold method to detect subcellular sites of Charcot-Leyden crystal protein showed changing distributions of this protein which document the capability of human basophils to undergo complex release and recovery reactions that may be pertinent to the functions of Charcot-Leyden crystal protein and the capabilit

Glutathione disrupts galectin-10 Charcot-Leyden crystal formation to possibly ameliorate eosinophil-based diseases such as asthma

“…Our previous work with Gal-10 indicated that EGFP-tagged lectin is primarily distributed in the nucleus of HeLa cells [25] . Other reports have shown that Gal-10 is also located in the cytoplasm [ 17 , 36 , 64 ] . However, a recent study showed that Gal-10 is not stored in granules but rather resides in the peripheral cytoplasm of human eosinophils [38] .…”

“…Gal-10 can be found in cells within the nucleus [ 16 , 25 , 26 ] , granules [10] , cytoplasm [ 17 , 36 ] , outer-cell membrane [37] and inner-cell membranes [38] . This suggests that there could be several partners to which Gal-10 can bind and regulate distribution and/or transport through cell membranes, as well as possibly regulating the function of these partners.…”

Selective Recognition of Mannose by the Human Eosinophil Charcot-Leyden Crystal Protein (Galectin-10): A Crystallographic Study at 1.8 Å Resolution,

“…The CLC protein was also localized to the nucleus and cytoplasm during basophil activation and degranulation (34,35). While the role of the CLC protein in the nucleus after basophil activation remains unclear, it has been suggested that this protein might bind to the nuclear matrix or chromatin and/or play a role in transcription and RNA processing (35).…”

“…The CLC protein was also localized to the nucleus and cytoplasm during basophil activation and degranulation (34,35). While the role of the CLC protein in the nucleus after basophil activation remains unclear, it has been suggested that this protein might bind to the nuclear matrix or chromatin and/or play a role in transcription and RNA processing (35). In light of the structural similarity between the CLC protein and the galectin family of proteins, further support for the potential role of the nuclear CLC protein in RNA processing is provided by galectin-3 and galectin-1, which play a role in pre-mRNA splicing (36,37).…”