Molecular Human Reproduction, Vol. 8, No. 12, 1079-1086,
December 2002
© 2002 European Society of Human Reproduction and Embryology
Regulation of ovarian function |
High xylosyltransferase activities in human follicular fluid and cultured granulosa–lutein cells
1 Institut für Laboratoriums- und Transfusionsmedizin, Herz- und Diabeteszentrum Nordrhein-Westfalen, Universitätsklinik der Ruhr-Universität Bochum, Georgstraße 11, 32545 Bad Oeynhausen and 2 Frauenklinik, Bielefelder Institut für Fortpflanzungsmedizin, Städtische Kliniken Bielefeld-Rosenhöhe, Bielefeld, Germany
Follicular fluid proteoglycans play an important role in human oocyte maturation, including the development of a fluid-filled compartment and maintenance of the hypocoagulative state of the follicular fluid. Human xylosyltransferase (EC 2.4.2.26, XT) is the key enzyme in the biosynthesis of glycosaminoglycan chains in proteoglycans and is secreted into body fluids together with large proteoglycans. We investigated the XT activities in human follicular fluid and granulosa–lutein cells from women undergoing IVF procedures. The mean XT activity was determined as 17.7 mU/l, which is 20-fold higher than in serum and the highest XT activity ever found in body fluids. Cultured human granulosa–lutein cells secreted large amounts of XT (14.52 µU/106 cells), indicating that these cells are the main source of this enzyme in human follicular fluid. The XT from human follicular fluid was found to be associated with large chondroitin sulphate-containing proteoglycans. Furthermore, heparin was shown to bind strongly to the follicular fluid XT and to inhibit its enzyme activity. These findings indicate that XT may play a role in maintaining the haemostatic potential of the follicular fluid.
chondroitin sulphate/follicular fluid/heparan sulphate/proteoglycan/xylosyltransferase
3 To whom correspondence should be addressed. E-mail: cgoetting{at}hdz-nrw.de
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