报告题目: Roles of Receptor Activity Modifying Proteins in physiology and disease

报告人: Dr. Timothy Michael Skerry, 英国School of Medicine University of Sheffield，Department of Oncology and Metabolism的系主任

主持人: 罗剑 研究员

报告时间: 10月18日 13:30 （周二下午）

报告地点: 天美娱乐534报告厅

 

报告人简介：

Dr. Timothy Michael Skerry, B.Vet.Med, FRCVS, Cert SAO, PhD., Head of Department of Oncology and Metabolism, Professor of Orthopaedic Biology, School of Medicine University of Sheffield UK.

 

After 5 years in clinical practice, specialising in orthopaedics, I undertook a PhD at the RVC on Functional Adaptation in bone, where I was the first person to demonstrate the activation of osteocytes by loading of bone in vivo, after which I moved to Bristol in 1987 as a lecturer in surgery then anatomy. My group demonstrated that osteocytes within bone could bind PTH to cell surface receptors, used the technique of Differential RNA display (an early subtractive technology) to identify novel regulators of bone's response to loading. In 1995 I was appointed to a Chair in York University and established a large group and an international reputation in bone biology research following up our discovery of glutamate signalling in several non-neuronal tissues (bone, skin. megakaryocytes). In the late 1990s I started working on heteromeric receptors in cancer applications in York and subsequently at the RVC in London. I moved to Sheffield School of Medicine in 2005 to focus more on my research, and funded the development of a monoclonal antibody to RAMP3, a component of the AM2 receptor for cancer therapy. This antibody is now licensed to Fusion Antibodies, for development humanisation and preparation for clinical trials. In Sheffield the predominant focus of our work is now the calcitonin family of receptors which comprises the calcitonin and calcitonin-like receptors with additional interests in other GPCRs that interact with Receptor Activity Modifying Proteins (RAMPs)

 

报告摘要：

The receptor Activity Modifying Proteins (RAMPs) are a family of 3 human proteins that interact with different G protein-coupled receptors (GPCRs) to alter the effect of receptor activation.  For some receptors the presence of the RAMP alters ligand selectivity, while in others, it alters the trafficking of the receptor to the cell surface.  Finally, RAMPs can alter the response of the receptor to binding of the same ligand so that its presence changes the way the cell responds.  These effects have profound effects in physiology which lead to opportunities to influence disease processes.  Our major interest is the way that RAMP3 interacts with the calcitonin like-receptor to form an adrenomedullin-2 receptor, which may be a target for cancer therapy.