Activity and form of sulfated glycoprotein 2 (clusterin) from cultured Sertoli cells, testis, and epididymis of the rat

Abstract

Sulfated glycoprotein 2 (SGP 2) is a 73-kDa highly glycosylated disulfide- linked heterodimer. It is a major secreted protein of Sertoli cells, is found in high abundance within the seminiferous tubule fluid (STF) and epididymal fluid (EPF), and can be found on the surface of spermatozoa. Due to its high abundance and location it is believed to play a major role in the development of spermatozoa; however, its specific function(s) within the reproductive tract is not known. Purified and renatured SGP 2 were found to have the ability to inhibit complement activity with a mean concentration of 66 mg/ml for 50% inhibition. Extraction of epididymal sperm with various reagents showed that a major fraction of the SGP 2 in EPF was free or was loosely associated with the spermatozoa whereas a smaller fraction was more tightly associated and disruption of the lipid bilayer was required for its complete removal. Ultracentrifugation techniques and gel permeation chromatography revealed that SGP 2 in plasma, STF, and EPF formed complexes with other proteins and/or lipids but was not specifically associated with the apolipoprotein-like particles containing apolipoprotein A1 (apo A1).