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Ascorbic acid has long been associated with fertility, but no consistent study of its mechanism of action in reproductive tissues has been made. This article considers how three of ascorbic acid's principal functions, namely its promotion of collagen synthesis, its role in hormone production, and its ability to protect cells from free radicals, may explain its reproductive actions. Data relating to both ovary and testis are reviewed since ascorbate accumulates in both tissues. Both gonads exhibit cycles of tissue remodeling and of peptide and steroid secretion that can be assumed to be ascorbate-dependent. Ascorbic acid may also prevent gametes from damage by free radicals during production and fertilization. Preliminary data on the concentrations of ascorbic acid in serum and follicular fluid from women undergoing in vitro fertilization are presented. They suggest that the supply of ascorbic acid to the ovary might be a limiting factor in the ability of the preovulatory follicle to grow in response to gonadotropin stimulation. It is concluded that ascorbic acid is a key compound in gonadal physiology on which further research is needed and that a reappraisal of its potential clinical value in the treatment of various types of male and female infertility would be timely.

Plasma protein adsorption patterns on colloidal drug carriers acquired after i.v. administration depend on their surface characteristics and are regarded as key factors for their in vivo organ distribution. Polymeric latex particles with strongly differing surface properties were synthesized as models for colloidal drug carriers for tissue-specific drug targeting via the intravenous route. Physicochemical characterization was performed for size, surface charge density, zeta potential, and surface hydrophobicity. The interactions with human plasma proteins were studied by way of two-dimensional polyacrylamide gel electrophoresis (2-D PAGE). Considerable differences in protein adsorption on the latex particles were detected with regard to the total amount of surface-bound protein on the various particle types as well as specific proteins adsorbed, for example, fibrinogen, albumin, and a recently identified plasma glycoprotein. Possible correlations between protein adsorption patterns and the physicochemical characteristics and topography of the polymeric surfaces are shown and discussed. Knowledge about protein-nanoparticle interactions can be utilized for the rational design of colloidal drug carriers and also may be useful for optimizing implants and medical devices.

The aim of this study was to locate sites of expression and deposition of collagen, fibronectin and laminin in the bovine ovary. RNA from the granulosa and basement membrane/theca fractions of maturing follicles and from corpora lutea of the early, middle and late luteal phase was probed with cDNAs for collagen types I and IV, fibronectin and laminin. Antisera against collagens I and IV were used in western analysis of protein from follicular fluid, granulosa, basement membrane/theca and corpus luteum. Collagen subunits alpha 1(I) and alpha 2(I) were expressed in the basement membrane/theca but not in the granulosa of the follicle. They were also expressed in all luteal extracts, especially those from the early phase. Collagen alpha 2(IV) was highly expressed in the basement membrane/theca and to a lesser extent in corpora lutea. Collagen alpha 3(IV) was expressed in the granulosa, basement membrane/theca and early corpus luteum. Fibronectin 1 and laminin B2 were expressed in all tissues. Laminin B1 was expressed in all tissues except the granulosa. Collagen IV was immunodetected in all follicle extracts, with the strongest signal in the basement membrane/theca. Collagen I occurred in all luteal extracts and in the basement membrane/theca but not in follicular fluid or the granulosa. These results demonstrate tissue-specific expression of ovarian structural proteins and suggest that changes occur during the progression from follicle to corpus luteum. The production of collagen IV in the follicle wall and of collagen I in the corpus luteum is consistent with previous biochemical studies. Evidence for collagen IV in the follicular antrum suggests that the follicle wall originates from granulosa as well as theca cells.(ABSTRACT TRUNCATED AT 250 WORDS)

Surface hydrophobicity and phagocytic uptake in vitro as well as the interactions with plasma proteins of commercially available polystyrene particles were strongly affected by fluorescent labelling. Particles synthesised by Paulke remained unchanged after labelling. The results show the importance of thorough surface characterization for using particles in test systems in vitro and in vivo.

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Melatonin, at concentrations and periods of exposure reflecting those present during the circadian cycle, was investigated for its influence on steroid production by granulosa cells cultured in serum-supplemented medium. At high (200 pg/ml) but not low (20 pg/ml) physiological concentrations, melatonin significantly stimulated progesterone production by human granulosa cells. This response was independent of the overall level of cell activity and was seen under the different culture conditions associated with different culture media. Exposure to melatonin for 8 h significantly stimulated progesterone secretion to a level similar to that achieved under continuous exposure, and the effect was reduced to control levels during subsequent periods in which no melatonin was added. Melatonin had no consistent effect on aromatase activity in the conversion of stored or serum-available androgen to oestradiol. Melatonin significantly stimulated progesterone production by bovine granulosa cells in vitro, at concentrations similar to those present during the endogenous nocturnal rise (100-400 pg/ml). This response to physiological conditions by human and bovine cells suggests a role for melatonin in the regulation of progesterone production by the ovary.