Clusterin (CLU, SGP-2, TRPM-2, ApoJ, CLI) is ubiquitously expressed and highly conserved in mammalian tissues and fluids. Its structural and functional features are still not completely understood. Two promoters, P1 and P2 (P2 is epigenetically regulated), drive the expression of at least three alternative mRNAs from CLU gene (nine exons and eight introns). The protein is an heterodimer composed by an Î±-chain and a Î²-chain, linked by five disulphide bounds, with amphipathic helices and intrinsically disordered, coil-like and molten globule-like regions. About 30% of the mass of the mature protein is made of carbohydrates. CLU may prevent uncontrolled membrane attack complex activity and thus play an important role to control terminal complement-mediated damage, chronic inflammation, autoimmunity and female tolerance to seminal antigens. The binding of human CLU by pathogens may elicit immune escape. Single nucleotide polymorphisms have been identified but not clearly linked to diseases yet.
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