DESCRIPTION
Cancer cell biology, gene target, biomarker discovery and cancer cell imaging are the main areas of interest. Also small molecule and mini-gene therapeutic approaches in breast cancer cells to inhibit chemotaxis. Research includes development of fluorescence life time imaging microscopy (FLIM) for in vivo imaging, as well as imaging of patient samples.
Associated research programmes
Associated staff research interests
Interests:
The laboratory is interested in how cancer cells are able to dissociate from the primary tumour, invade the surrounding tissue and subsequently metastasise to distal sites. Tissue invasion and migration require cancer cells to reorganise their actin cytoskeleton as well as adhere to and degrade the surrounding extracellular matrix. It is well established that cytoskeletal rearrangement, cell adhesion formation and turnover is regulated by Rho GTPases, Rho, Rac and Cdc42. PAKs are serine/threonine kinases that operate downstream of Rho GTPases to control cytoskeletal organisation and substratum adhesion. The PAK family can be sub-divided into two groups; Group 1 PAKs (1-3) and Group 2 PAKs (4-6) based on sequence homology and members of both groups are activated by growth factor signalling pathways. We use live cell imaging, biochemical and molecular approaches to investigate the role of PAK family kinases in cancer cell migration, adhesion and invasion.
Tel:
020 7848 8300
Fax:
020 7848 6220
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Interests:
Cancer, kinase signalling pathways, PSKs, apoptosis, cytoskeleton, cell shape, migration, cell cycle and prostate
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Interests:
Our main objective is the identification and functional characterisation of protein kinases which are over-expressed and/or activated in malignant prostate tissues and to target these proteins or their downstream substrates for therapy.
Most recently, we have focused on a novel family of protein kinases which we have called prostate-derived sterile 20-like kinases (PSKs/TAOs) 1-3. These proteins regulate microtubules and play key roles in controlling mitogen-activated protein kinase (MAPK) signalling pathways and also the microtubule-based spindle in dividing cancer cells. Current projects are using a wide range of cell and molecular techniques to investigate the functional roles for PSKs and in particular their regulation of cancer cell division and motility.
Tel:
020 7848 8302
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Interests:
Interests are broadly based in defining signal transduction pathways, their action, functional status, prognostic and therapeutic potential in cancer. The research is particularly focused around the protein kinase C superfamily and growth factor receptor action and pathophysiology.
As membrane and protein complex associated protein kinases, these signal transducers operate in spatially restricted compartments and serve highly localised roles in controlling signal outputs. Recent studies have focused on spatial and dynamic aspects of signalling propagated through and/or influenced by these kinases, including the conformational nature of nucleotide binding (and the influence of interventions at this binding site), single molecule analysis of growth factor receptor behaviour, controls acting on the HGF-cMet growth factor signalling pathway, integrin actions in migration, the localisation of signals during migration and general roles in proliferation and survival.
Application of molecular insights derived from the studies on these kinases and the methods developed for this purpose are significant current objectives. This includes drug development activities, biomarker discovery and biomarker methodologies.
Tel:
020 7848 6835
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The Ameer-Beg group aims to further our understanding of cell signalling dynamics and control. We develop optical instrumentation to address fundamental biological questions regarding the dynamic interaction of protein partners within the cellular membrane. The group’s interests range from high-resolution imaging of tumours using multiphoton fluorescence lifetime imaging to the interrogation of single-molecules within cellular membranes.
Our group is intimately involved in an initiative to develop ‘optical proteomic technology for in situ analysis of protein interaction networks’. Involving a number of research groups within the college aims to develop high-throughput/content optical screening approaches for cell based assays of protein-protein interactions. As part of a strategic programme of research within the biophysics community at KCL, we have established a novel high-throughput fluorescence lifetime/anisotropy imaging/FRET-based assay that identifies perturbations in intramolecular interactions using molecular librariesin mammalian cells.
The Cell Imaging and Biodynamics group is part of the joint UCL/KCL Comprehensive Imaging Centre where we will develop high-resolution multiphoton FLIM for measurement of FRET within thick biological specimens. We aredeveloping adaptive optics techniques to improve multiphoton imaging at depth within biological specimens.
The group is currently developing novel single-molecule imaging methods to observe protein-protein interactions at the cell membrane using a combination of super-resolution techniques and fluorescence lifetime spectroscopy as part of a collaboration seeking to unravel the dynamics of complex signalling networks.
Tel:
020 7848 6558
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Interests:
Cancer Cell Motility and Imaging
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CONTACTS FOR FURTHER INFORMATION
Professor Tony Ng
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