Clusterin (CLU), also known as apolipoprotein J (ApoJ), is a 75-80 kDa heterodimeric disulfide-bonding protein involved in cellular debris clearance and apoptosis. It was first identified that in ram rete testis fluid clusterin showed signs of clustering with rat sertoli cells and erythrocytes, hence its name.
The precursor polypeptide chain undergoes proteolytic cleavage to remove the 22-mer secretory signal peptide, followed by the formation of the α and β chains between residues 227/228. For aiding protein folding of secreted proteins, CLU is a molecular chaperone and its three isoforms have been differentially implicated in pro- or antiapoptotic processes. Due to these roles, CLU is thought to be associated with a variety of oxidative stress-related diseases, including neurodegenerative diseases, cancers, inflammatory diseases, and aging.
Clusterin (CLU) has been reported to minimize the effects of oxidative condition in photoreceptors, thereby protecting the rods in S334ter-line3 Retinitis Pigmentosa retina. Neuronal nitric oxide synthase (nNOS) is the enzyme that is responsible for the synthesis of nitric oxide (NO) by neurons. Through the reduction of nNOS expression in S334ter-line3 rat retinas, it is concluded that clusterin regulates rod photoreceptor survival at least partly and by induction of nNOS synthase expression and its reduction by clusterin treatment.
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Clusterin Pipelines
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Recombinant Clusterin
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Pre-clinical
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