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Pregnancy-Associated Plasma Protein-A (PAPP-A) in Ovine, Bovine, Porcine, and Equine Ovarian Follicles: Involvement in IGF Binding Protein-4 Proteolytic Degradation and mRNA Expression During Follicular Development

Physiologie de la Reproduction et des Comportements (S.M., P.M.), Université F. Rabelais de Tours, 37380 Nouzilly, France; Department of Molecular and Structural Biology (M.T.O., C.O.), University of Aarhus, 8000 Aarhus C, Denmark; Department of Clinical Biochemistry Statens Seruminstitut (M.C.), 2300 Copenhagen S, Denmark; Endocrine Research Unit (C.A.C.), Mayo Clinic and Mayo Foundation, Rochester, Minnesota 55905; Laboratoire de Génétique Moléculaire (I.L., M.V.), Faculté de Pharmacie, 75006 Paris, France; Institut National de la Recherche Agronomique (G.T.-K.), Génétique Cellulaire, 31326 Castanet-Tolosan, France; and Department of Medicine (J.Z.), University Hospital, Zürich CH-8091, Switzerland

Address all correspondence and requests for reprints to: Philippe Monget, Physiologie de la Reproduction et des Comportements, UMR 6073 Institut National de la Recherche Agronomique-Centre National de la Recherche Scientifique-Université François Rabelais de Tours, 37380 Nouzilly, France. E-mail: monget{at}tours.inra.fr

IGF binding protein-4 (IGFBP-4) proteolytic degradation is a common feature of preovulatory follicles from human, ovine, bovine, porcine, and equine ovary. In all these species, the protease is a zinc-dependent metalloprotease and its ability to degrade IGFBP-4 is IGF dependent. The human intrafollicular IGFBP-4-degrading protease has recently been identified as pregnancy-associated plasma protein-A (PAPP-A). The aim of this study was to investigate whether PAPP-A is also involved in IGFBP-4 degradation in ovine, bovine, porcine, and equine preovulatory follicles and to study the expression of PAPP-A mRNA in bovine and porcine granulosa cells from different classes of follicles. Immunoneutralization and immunoprecipitation with polyclonal antibodies raised against human PAPP-A inhibited IGFBP-4 proteolytic degradation in preovulatory follicular fluid from the four species studied. As previously reported for the intrafollicular proteolytic activity degrading IGFBP-4, recombinant human PAPP-A generated in vitro 17- and 10-kDa IGFBP-4-proteolytic fragments. Recombinant PAPP-A activity was also shown to be IGF dependent and was inhibited by heparin-binding domain-containing peptides. In all mammalian species studied, the PAPP-A sequences showed high degree of identity. Moreover, the PAPP-A gene was localized on porcine chromosome 1 (1q29–1q213), in agreement with the localization of human PAPP-A gene on human chromosome 9q33.1. In bovine and porcine ovaries, real-time quantitative RT-PCR showed that PAPP-A mRNA expression in granulosa cells was maximal in fully differentiated follicles and was positively correlated with expression of P450 aromatase and LH receptor mRNAs. Overall, these data show that PAPP-A is responsible for IGFBP-4 degradation in ovine, bovine, porcine, and equine preovulatory follicles. The high expression of PAPP-A mRNA in granulosa cells from large, differentiated follicles suggest that it is a new functional marker of follicular development.

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