Sepsis is a recognized global health problem.
It affects over 30 million people worldwide annually and is the largest killer of children → 5 million each year.
As already mentioned in Focus on Clusterin! - part one, clusterin is able to form complexes with immunoglobulins, components, paraoxonase, leptin, lipids, heparin, bacteria, complement and others. It can also bind to beta amyloid and inhibit formation of its fibrils.
Clusterin has been connected to a plethora of functions such as phagocyte recruitment, reduced aggregation of serum proteins, prevention of complement attack, apoptosis inhibition, membrane remodeling, lipid transport, hormone transport, matrix metalloproteinase inhibition and reduction of oxidative stress.
Read more
Clusterin is one of the central stress response proteins. It exists in two variants. The major longer secreted form of clusterin (sCLU) exerts an anti-apoptotic function and the nuclear form (nCLU) has a pro-apoptotic function.
sCLU binds extracellularly to stressed and unfolded proteins to form a clusterin – damaged protein complex. This complex is subjected to either interaction with other chaperones in order to refold the damaged protein or interaction with cellular receptors resulting in lysosomal or proteasomal degradation inside the cell.
Read more