Molecular biology of Clusterin

The protein itself is a disulfide-linked heterodimeric protein, rich in sialic acid containing about 30% of N-linked carbohydrate. Truncated forms of targeting to the nucleus have been identified. Polypeptide chain precursor by proteolytic cleavage to remove a secretory signal peptide of 22 amino acids, and subsequently between residues 227/228 generates the α and β chains. They are assembled in an anti-parallel manner, to obtain a heterodimeric molecule, wherein five disulfide bridges connecting the centers of the cysteine-rich, and is flanked by two predicted α-helical coiled-coil and three predicted amphiphilic α-helix.

A ≈ 40 kDa mature protein smear in reducing SDS-PAGE immunoblotting. For the precursor form of a 60-kDa protein appears.

The protein has been implicated in a variety of activities, including programmed cell death, regulate complement-mediated cell lysis, membrane recycling, cell adhesion and src-induced phase transition. As part of the complement attack complex, which serves as a complement inhibitor.

Its ability to bind to and form complexes with numerous partners, such as immunoglobulins, lipids, heparin, bacteria, complement components, paraoxonase, beta-amyloid protein, leptin, and others. Clusterin has been given too many functions, such as macrophage recruitment, aggregation induced complement attack prevention, inhibition of apoptosis, membrane remodeling, lipid transport, hormone transport and / or removal and matrix metalloproteinase inhibition.