Cardiovascular disease (CVD) comprehensively describes a range of pathologies of the heart and/or blood vessels. These disorders differ markedly in time-scale of development, and relative contributory effects of genes and environment. Largely due to this breadth, and their causes and effects, the range of investigation, assessment, and treatment strategies available is large. The diversity of the diseases, disease processes, and genetic differences between individuals could obscure disease associations in terms of the proteomic signatures of each disorder. Thus, a panel of independent disease-related proteins considered together should be less prone to this noise and help provide much more robust analysis and indication of disease. The publication featured below and the reagents (multi-plex immunoassays or single target ELISA and antibodies) mentioned in this post may contribute in helping you to identify such diseases signature.

Recombinant protein expression and purification for therapeutic development or for in vitro studies can sometimes be a real challenge. It requires huge investments in both time and cost in order to obtain high yields of pure and active recombinant proteins. My aim in writing this post, is to give you a simple guide to easily establish optimal conditions for recombinant protein expression and production in E. Coli, of problematic unstable proteins of interest.

Kupffer primary cells are macrophages endogenous to the liver which have the ability to modulate hepatic inflammation and injury associated with various pathophysiologies and toxicities. Pro-inflammatory cytokines released by activated Kupffer cells, such as TNF-α and IL-6, are associated with up-regulation of acute-phase response proteins and suppression of CYP enzymes. For new biological entities, particularly immunomodulators, evaluating the potential for Kupffer cell activation is an emerging concept in preclinical development. Kupffer cells are estimated to comprise approximately 4-8% of total liver cell content and approximately 20% of non-parenchymal cells (Raccanelli and Rehermann, 2006).

As is already known, multiple families of small GTPases (Ras, Arf and Rho families) make up the Ras GTPase superfamily. Due to their role as molecular switches in cell signalling (active GTP-bound state vs inactive GDP-bound states) and in many other cellular responses (cytoskeletal reorganization, regulation of transcription, apoptosis…), these small GTPases are the subject of intense investigation to try to understand the mechanisms that regulate activation and inactivation of this proteins.

In this post, I invite you to discover a revolutionary way to study these cell signalling events by quantifying the level of active small GTPases in your experimental model.