Olga Göransson, PhD, Associate Professor
Protein phosphorylation is a signalling mechanism that regulates most aspects of cellular life, and protein kinases constitute the largest family of enzymes encoded by the human genome. An overall aim of our research is to study the regulation and function of protein phosphorylation cascades with relevance to Type 2 Diabetes, with a particular focus on adipose tissue.
Presently, our main project evolves around the master upstream kinase LKB1 and its substrates in the AMP-activated protein kinase family (AMPK). AMPK acts as a fuel gauge, sensing and regulating cellular energy levels. Activated AMPK re-installs the AMP/ATP ratio by stimulating ATP-generating processes such as oxidation of nutrients, and inhibiting ATP-consuming synthetic pathways. In recent years, it has emerged that AMPK is also a critical regulator of systemic energy balance, responding to hormonal signals, such as the adipokines leptin and adiponectin. As a consequence, AMPK is an attractive target for the development of anti-diabetic drugs. In fact, positive effects of metformin, thiazolidinediones and exercise on insulin sensitivity, appears to be due to their ability to activate AMPK.
As a member of the LUDC project area "Cellular signalling in diabetes", we have a general interest in signal transduction pathways involved in the (dys)regulation of insulin sensitivity and production. We are engaged in various LUDC collaborations connecting to these issues, such as functionally investigating the diabetes risk gene TCF7L2, and signalling downstream of the neuroendocrine peptide CART.
Last updated: September 27, 2012
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