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Abstract
Heparanase (HPSE) is an endoglycosidase that cleaves heparan
sulfate proteoglycans (HSPGs), major components of the
basement membrane (BM) and extracellular matrix (ECM).
Heparanase activity results in release of HSPG-bound
molecules including basic fibroblast growth factor (FGF2).
Structural and functional development of the corpus luteum
(CL) involves tissue remodeling, active angiogenesis and
steroid production. Heparanase-induced ECM and BM
breakdown as well as FGF2-stimulated endothelial
proliferation may have an important role in the regulation
of luteal function. Heparanase mRNA was detected by RT-PCR
in granulosa cells recovered from follicular fluid of in
vitro fertilization patients. Using sulfate labeled ECM,
heparanase enzymatic activity was determined in human
luteinized granulosa cells. Employing
immunohistochemistry, heparanase protein was predominantly
localized in theca interna cell layer of the mature antral
follicle, whereas in human corpora lutea, both luteinized
granulosa and theca cells were immunostained for
heparanase. During luteolysis heparanase was identified in
macrophages surrounding the forming corpus albicans. In
serially sectioned ovaries from unstimulated rats as well
as from eCG treated rats, expression of heparanase was
noted exclusively in the ovarian steroid-producing
interstitial tissue. Following an ovulatory dose of hCG,
heparanase was immunostained also in lutein cells of the
forming corpora lutea. Temporal expression of heparanase
in granulosa cells during the luteal phase and in
macrophages during luteal regression supports the
hypothesis that heparanase plays a role in human ovarian
ECM remodeling and may potentiate cellular migration and
growth factor bioavailability.
Key words:
Ovary
Corpus luteum
Follicle
Granulosa cells
Theca cells
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