Monoclonal antibodies distinguish between storage and secreted forms of eosinophil cationic protein.
The toxic effects of eosinophils on parasites and cells are due largely to the secretion of various granule proteins, following stimulation. In order to study this secretory process (degranulation) further, we have raised mouse monoclonal antibodies against both human eosinophil granule extracts and secretion products. From immunocytochemical studies it appears that one antibody, EG1 , recognized both the storage and secreted forms of eosinophilcationic protein (ECP), whereas antibody EG2 only bound to ECP during secretion (and extraction). This antibody also bound to eosinophil protein-X (EP-X). As both antibodies stained eosinophils in formalin-fixed tissues, they were used to demonstrate sites of eosinophil activation and secretion in chronic urticaria. The capacity of monoclonal antibodies to detect differences between storage and secreted forms of proteins is an important property of these reagents with many potential applications in cell biology.
D000911:Antibodies, Monoclonal; D000936:Antigen-Antibody Complex; D001798:Blood Proteins / Q000032:analysis* / Q000378:metabolism; D002469:Cell Separation; D047091:Eosinophil Granule Proteins; D004804:Eosinophils / Q000166:cytology / Q000502:physiology*; D006801:Humans; D010587:Phagocytosis; D012260:Ribonucleases; D014581:Urticaria / Q000503:physiopathology
D000911:Antibodies, Monoclonal; D000936:Antigen-Antibody Complex; D001798:Blood Proteins; D047091:Eosinophil Granule Proteins; D012260:Ribonucleases