Interleukins (ILs) are known best for their involvement in the immune system and their role during inflammation. In the ovary, a growing body of evidence suggests that the ovarian follicle is a site of inflammatory reactions. Thus ovarian cells could represent sources and targets of ILs. Since then, the IL-1 system components (IL-1 , IL-1 , IL-1 receptor antagonist, IL-1 receptors) have been demonstrated to have several sites of synthesis in the ovary. These factors have been localized in the various ovarian cell types, such as the oocyte, granulosa and theca cells, in several mammalian species. IL-1-like bioactivity has been reported in human and porcine follicular fluid at the time of ovulation. The role of IL-1 in local processes is still poorly known, although there is evidence for involvement in the ovulation process, and in oocyte maturation. More precisely, IL-1 may be involved in several ovulationassociated events such as the synthesis of proteases, regulation of plasminogen activator activity, prostaglandin and nitric oxide production. IL-1 also regulates ovarian steroidogenesis. These different aspects of the involvement of the IL-1 system in important aspects of female reproduction are discussed.

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Natural antimicrobial peptides are present in different compartments (eggshell, egg white, and vitelline membranes) of the hen egg and are expected to be involved in the protection of the embryo during its development and to contribute to the production of pathogen-free eggs. In the present study, we used vitelline membranes from hen (Gallus gallus) eggs as a source of avian ␤-defensin 11 (AvBD11). A purification scheme using affinity chromatography and reverse-phase chromatography was developed. Purified AvBD11 was analyzed by a combination of mass spectrometry approaches to characterize its primary sequence and structure. A monoisotopic molecular species at [M ؉ H]؉ of 9,271.56 Da was obtained, and its N-and C-terminal sequences were determined. We also examined posttranslational modifications and identified the presence of 6 internal disulfide bonds. AvBD11 was found to exhibit antimicrobial activity toward both Gram-positive and Gram-negative bacteria.The avian egg is a unique and original biological system which is formed according to a well-defined spatial and temporal sequence as it passes along the reproductive tract of the hen. The segments of the oviduct involved in the egg formation are the infundibulum, the magnum, the isthmus, and the uterus. Each segment expresses and secretes specific molecules that become successively incorporated into the vitelline membranes in the infundibulum, the egg white in the magnum, the eggshell membranes in the isthmus, and the eggshell in the uterus. Thus, the hen deposits into the egg, which can be considered a closed chamber, all the nutrients and protective systems that are necessary to support the development of an embryo during 21 days of incubation. Recently, transcriptomic and proteomic approaches have identified almost 1,000 putative proteins and peptides in the various compartments of eggs (6). Among these are a number of polypeptides that are likely to resist microbial contamination of the eggs, some of which belong to the family of avian ␤-defensins (AvBDs).A total of 14 avian ␤-defensin genes have been identified through in silico studies. Because most of them were simultaneously described by two research groups, some confusion was generated due to different nomenclatures (9,10,18,31). In a collaborative venture, we proposed a novel nomenclature that adopted the numbering system used by Xiao et al. (31) and replaced the term "gallinacin," used formerly by Lehrer's group, with "avian ␤-defensin" (AvBD) (19). AvBDs are small cationic nonglycosylated peptides (1 to 9 kDa). Some of them were successfully tested for their antimicrobial activity, including chicken AvBDs AvBD1, -2, -7, and -9, turkey AvBD1 and -2, ostrich AvBDs AvBD1, -2, -7, and -8, and penguin AvBD103b (3, 30). In mammals, ␤-defensins are molecules of innate and adaptive immunity, with a broad spectrum of antimicrobial activity (1). ␤-Defensin molecules possess six highly conserved cysteines with the following consensus sequence motif, where C is a cysteine, G a glycine, and X any amino acid: X...

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