- Title
- Cytokine properties of CD23 on human Eosinophilic cells
- Creator
- Ferreira, Lauren
- Subject
- Cytokines
- Subject
- CD23 antigen
- Subject
- Eosinophil
- Date Issued
- 2007
- Date
- 2007
- Type
- Thesis
- Type
- Masters
- Type
- MSc
- Identifier
- vital:10333
- Identifier
- http://hdl.handle.net/10948/503
- Identifier
- http://hdl.handle.net/10948/d1012001
- Identifier
- Cytokines
- Identifier
- CD23 antigen
- Identifier
- Eosinophil
- Description
- CD23, the low affinity IgE receptor, is expressed by various cell types and has numerous functions depending on the form of the protein, its interaction with various ligands and the type of cell involved. CD23 is pivotal in the regulation of IgE, with the soluble form involved in up-regulation, while the membrane bound form is involved in the down-regulation. It is clear why it is believed to be a central molecule in allergic responses, and a therapeutic target for the treatment of allergic disease. In this study a recombinant form of the entire extracellular domain of the protein, exCD23, was produced by PCR cloning and expressed in E. coli. His•Tag™s were introduced onto the C-terminus and N-terminus, respectively, in order to simplify the purification procedure. After renaturation and purification, the recombinant exCD23 bound IgE, indicating its activity. From the IgE binding studies it was established that the position of the tag did not influence the binding. GST•Tagged™ exCD23 was also produced in an attempt to increase the solubility of the recombinant protein, but this proved unsuccessful. Butyrate differentiated EoL-1 cells were treated with the Nterminal His•Tagged™ exCD23, and the protein appeared to suppress the secretion of the constitutively expressed cytokines, especially IL-8 and IFN- , when compared to untreated cells. In addition, treatment of the EoL-1 cells with exCD23 had a significant proliferative effect, but could not induce differentiation of this cell line into mature eosinophilic-like cells.
- Format
- xix, 180 leaves
- Format
- Publisher
- Nelson Mandela Metropolitan University
- Publisher
- Faculty of Science
- Language
- English
- Rights
- Nelson Mandela Metropolitan University
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NMMU School of BioMolecular and Chemical Sciences
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