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Glycosyl Phosphatidylinositol-Anchored Ceruloplasmin Is Expressed by Rat Sertoli Cells and Is Concentrated in Detergent-Insoluble Membrane Fractions¹

^a Department of Biology, Bucknell University, Lewisburg, Pennsylvania 17837

The copper-binding protein, ceruloplasmin, is both a serum component and a secretory product of Sertoli cells. Studies on serum ceruloplasmin have demonstrated it to be a ferroxidase that is essential for iron transport throughout the body. We report here that a glycosyl phosphatidylinositol (GPI)-anchored form of ceruloplasmin is expressed by Sertoli cells. Sertoli cell GPI-anchored proteins were selectively released by phosphatidylinositol-specific phospholipase C and were analyzed by Western blotting. A 135-kDa band was identified as ceruloplasmin by multiple antibody recognition and by amino acid sequence analysis. The presence of the GPI anchor on ceruloplasmin was confirmed by Triton X-114 phase partitioning experiments and by recognition with an antibody to the GPI anchor. GPI-anchored ceruloplasmin was enriched in detergent-insoluble glycolipid-enriched membrane microdomains (DIGs) of Sertoli cells. This is the first report of GPI-anchored ceruloplasmin in Sertoli cells and the first study of GPI-anchored ceruloplasmin in DIGs. We suggest that GPI-anchored ceruloplasmin may be the dominant form expressed by Sertoli cells and that Sertoli cell DIGs may play a role in iron metabolism within the seminiferous tubule.

¹ Financial support for this research was received from Dr. James Kase, M.D., F.A.C.S.

² Correspondence: FAX: 570 577 3537; nyquist{at}bucknell.edu

³ Current address: University of Pennsylvania Medical School; fortna{at}mail.med.upenn.edu

⁴ Current address: Johns Hopkins University; haw2{at}jhunix.hcf.jhu.edu

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