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Mast cell degranulating peptide binds to RBL-2H3 mast cell receptors and inhibits IgE binding |
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| Authors: | Angeliki Buku Joseph A. Price Milton Mendlowitz Sandra Masur |
| Affiliation: | a Department of Physiology and Biophysics, Mount Sinai School of Medicine, New York, NY 10029, USA b Department of Pathology, College of Osteopathic Medicine, Oklahoma State University, Tulsa, OK 74107, USA c Department of Molecular Cardiology, Mount Sinai School of Medicine, New York, NY 10029, USA d Departments of Ophthalmology and Physiology and Biophysics, Mount Sinai School of Medicine, New York, NY 10029, USA |
| Abstract: | Fluorescent and biotinylated analogs of mast cell degranulating (MCD) peptide were synthesized and the labels fluoresceinisothiocyanate and N-hydroxysuccinimidobiotin were conjugated at position 1 in the MCD peptide sequence. The analogs with these moieties retained histamine-releasing activity as high as that of the parent MCD peptide in rat peritoneal mast cell assays. These labeled analogs were used in rat basophilic leukemia cells (RBL-2H3) to demonstrate by confocal microscopy and flow cytometry the specific binding of MCD peptide to mast cell receptors. Consequently MCD peptide was found to compete with and inhibit the binding of fluorescent IgE on RBL cells as monitored by flow cytometry. Thus MCD peptide may prove to be useful in the study of IgE receptor-bearing cells. |
| Keywords: | Fluorescent and biotinylated MCD peptide Flow cytometry Confocal microscopy Fluorescent IgE |
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