Abstract
Clusterin, a 70–80-kDa glycoprotein, is present in numerous physiological fluids such as plasma, urine, breast milk, cerebrospinal fluid, and semen.1–3 cDNA sequencing of human clusterin was reported in 1989.4 Although it has been given various names, including clusterin, apolipoprotein J, SP-40, 40, etc.,5 clusterin is now the internationally accepted name for this protein. It has potential amphipathic helical domains that allow it to bind to hydrophobic molecules, and potential heparin binding domains that are important for interaction with cell membranes and extracellular matrices.6 Although several functions of clusterin have been proposed, such as lipid transport,1 sperm maturation,7 regulation of the complement cascade,2 programmed cell death,5 and membrane recycling,5,8 the most likely is cell membrane protection, which was reported by Aronow et al.8
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Nishida, K., Kawasaki, S., Kinoshita, S. (1998). Clusterin may be Essential for Maintaining Ocular Surface Epithelium as a Non-Keratinizing Epithelium. In: Sullivan, D.A., Dartt, D.A., Meneray, M.A. (eds) Lacrimal Gland, Tear Film, and Dry Eye Syndromes 2. Advances in Experimental Medicine and Biology, vol 438. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-5359-5_89
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DOI: https://doi.org/10.1007/978-1-4615-5359-5_89
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