Investigating the interaction between the tetraspanin CD82 and gangliosides, and, The binding partners of CLEC14A and the function of the CLEC14A extracellular domain

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http://eprints.org/relation/isVersionOf http://etheses.bham.ac.uk/id/document/54311 http://eprints.org/relation/isVolatileVersionOf http://etheses.bham.ac.uk/id/document/54311 http://eprints.org/relation/isIndexCodesVersionOf http://etheses.bham.ac.uk/id/document/54311 archive 4031 disk0/00/00/31/04 2013-06-13 13:07:19 2022-12-31 03:40:14 2013-06-13 13:07:19 thesis show 0 Lodhia Puja Sundaresan R. Noy P. University of Birmingham Investigating the interaction between the tetraspanin CD82 and gangliosides, and, The binding partners of CLEC14A and the function of the CLEC14A extracellular domain unpub QR180 RC0254 10col_mede Project 2 has full embargo until end December 2016, thereafter, e-copy remains restricted (option C) until December 2022. Emailed author on 09/01/17 and 03/02/17 about post-embargo choice. Received no reply from either email. Processing thesis with option C until December 2022 as previously stated. 28/02/17 HC Project 1: CD82 is a tetraspanin involved in tumour metastasis suppression. It is downregulated in several cancers including breast, liver and prostate cancer. Although interactions with gangliosides and cholesterol have been demonstrated, no ligand has yet been identified to directly target CD82. CD82 interaction with gangliosides has been explored by immunoprecipitation from cell lysates. However, direct interaction of purified full length CD82 protein with ganglioside has not yet been shown. This study demonstrates the interaction of full length CD82 protein with the ganglioside GM2 by ELISA, and did not require the presence of any other components of the cell membrane. This interaction was further explored by surface plasmon resonance and solid state NMR techniques. Project 2: CLEC14A is tumour endothelial marker (TEM). It is upregulated by reduced shear stress and facilitates angiogenesis. However, the biological activity of CLEC14A is poorly characterised. This study validates two binding partners of CLEC14A by co-immunoprecipitation and mass spectrometry. The activity of the CLEC14A extracellular domain (ECD) was also investigated. Flow cytometry revealed that CLEC14A-ECD is able to bind to the surface of human umbilical vein endothelial cells (HUVECS). However, treatment of HUVECS with 20 ug/ml CLEC14A-ECD did not affect cell motility in scratch wound assays. The cleavage site of CLEC14A by the intra-membrane serine protease rhomboid-like protein 2 (Rhbdl2) was also explored. These results will increase the understanding of the biological activity of CLEC14A and will aid the intelligent design of drugs targeting CLEC14A to inhibit tumour angiogenesis. 2012-12 2012-08 graduation eng author unchecked This unpublished thesis/dissertation is copyright of the author and/or third parties. The intellectual property rights of the author or third parties in respect of this work are as defined by The Copyright Designs and Patents Act 1988 or as modified by any successor legislation. Any use made of information contained in this thesis/dissertation must be in accordance with that legislation and must be properly acknowledged. Further distribution or reproduction in any format is prohibited without the permission of the copyright holder. ubira@lists.bham.ac.uk public 74 University of Birmingham Institute of Biomedical Research m_rs na 2012-12 graduation