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

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)-a...

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Bibliographic Details
Published in:Biology of reproduction 1999-10, Vol.61 (4), p.1042-1049
Main Authors: FORTNA, R. R, WATSON, H. A, NYQUIST, S. E
Format: Article
Language:English
Subjects:
Animals
Biological and medical sciences
Blotting, Western
Cell Adhesion
Cells, Cultured
Ceruloplasmin - metabolism
Detergents - pharmacology
Electrophoresis, Polyacrylamide Gel
Fundamental and applied biological sciences. Psychology
Glycosylphosphatidylinositols - metabolism
Male
Mammalian male genital system
Morphology. Physiology
Rats
Rats, Sprague-Dawley
Sertoli Cells - metabolism
Solubility
Type C Phospholipases - metabolism
Vertebrates: reproduction
Online Access:Get full text
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Summary: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.
ISSN:0006-3363
1529-7268
DOI:10.1095/biolreprod61.4.1042