Analysis of follicular fluid hormone concentrations and granulosa cell mRNA levels for the inhibin-activin-follistatin system: relation to oocyte and embryo characteristics

Fujiwara, Toshihiro; Lambert-Messerlian, Geralyn; Sidis, Yisrael; Leykin, Lucy; Isaacson, Keith; Toth, Thomas L.; Schneyer, Alan L.

doi:10.1016/s0015-0282(00)00652-x

Cited by 33 publications

(31 citation statements)

References 33 publications

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“…Several authors employ stimulation protocols with HMG, thus shifting away from the ideal baseline. [37]…”

Section: Discussionmentioning

confidence: 99%

“…Most studies relating steroid hormones with reproductive outcomes use in vitro fertilization as a laboratory technique and thus are limited in their results. [4567] Furthermore, in case of sperm injection, fertilization results do not clearly depend on seminal parameters, probably due to the strict selection of a reduced number of sperms, oocyte quality being the critical factor. [89]…”

Section: Introductionmentioning

confidence: 99%

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Follicular steroid hormones as markers of oocyte quality and oocyte development potential

et al. 2014

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CONTEXT:Various components of follicular fluid are suggested as biochemical predictors of oocyte quality. Previous studies of follicular steroid hormone levels have shown disparate results when related with fertilization outcomes.AIM:The objective of the study was to relate the levels of steroid hormones of each individual follicle with oocyte maturation, fertilization results, embryo quality, and pregnancy rates.SETTINGS AND DESIGN:Prospective cohort study in a university hospital.METHODS:In 31 patients, who underwent intracytoplasmic sperm injection, it was performed an ultrasound guided aspiration of follicular fluid of the first two mature follicles from each ovary. Follicular levels of estradiol, progesterone, testosterone, and dehydroepiandrosterone sulfate were measured by chemiluminescent immunoassay.STATISTICAL ANALYSIS:Generalized estimating equation model.RESULTS:In follicular fluids with mature oocyte presence, in normal as well as in failed fertilization, there was a positive correlation between follicular testosterone and progesterone (r = 0.794, P = 0.0001 and r = 0.829, P = 0.0001). Progesterone levels were higher in cases of normal fertilization compared to failed fertilization (P = 0.003). B quality embryos came from oocytes immersed in follicular fluids with higher estradiol values and higher estradiol/progesterone and estradiol/testosterone ratios than those of C quality (P = 0.01; P = 0.0009; P = 0.001). Estradiol levels were higher in patients who achieved pregnancy (P = 0.02).CONCLUSION:The analysis of follicular hormone composition could be considered as an additional tool in oocyte selection.

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“…Several authors employ stimulation protocols with HMG, thus shifting away from the ideal baseline. [37]…”

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Follicular steroid hormones as markers of oocyte quality and oocyte development potential

et al. 2014

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“…Human follicular fluid was obtained by aspiration of follicles from well-characterized normal volunteers and women with PCOS, as previously described (24,25). These patients also gave informed consent, and the study protocol was approved by the Institutional Review Board for human studies at the Massachusetts General Hospital and Partners Healthcare Organizations.…”

Section: Human Specimensmentioning

confidence: 99%

Differential Distribution of Follistatin Isoforms: Application of a New FS315-Specific Immunoassay

Schneyer¹,

Wang²,

Sidis³

et al. 2004

The Journal of Clinical Endocrinology & Metabolism

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Follistatin (FST) is a monomeric activin-binding and neutralization protein that has at least three isoforms in human tissues and fluids. The full-length FS315 protein has an acidic 26-residue C-terminal tail that is not present in the shortest form, FS288, due to alternative splicing. An intermediate form, FS303, was identified in follicular fluid that is presumably derived by proteolytic processing of this tail domain. Interestingly, the biochemistry of each of these three isoforms is distinct, including their ability to bind to cell surface proteoglycans, an activity that ranks in the order FS288 > FS303 > FS315. This would suggest that the soluble, circulating FST isoform is likely to be FS315, a hypothesis supported by previous determinations that the serum and follicular fluid forms of FST are biochemically distinct. To test this hypothesis, we developed an immunoassay that is specific for full-length FS315. This assay was validated for use with human serum and follicular fluid samples and then used to examine FST in these fluid compartments. Our results indicate that FS315 is indeed the major circulating FST isoform but is undetectable in follicular fluid samples aspirated from normal women or women with polycystic ovary syndrome. These observations confirm the compartmentalization of FST isoforms according to their biochemical properties and biological actions so that the most soluble form is found in the circulation, whereas the forms that bind to cell surface proteoglycans are found in tissue compartments such as the ovarian follicle. They also confirm that the source of FST in human serum is not the ovarian follicle.

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“…The oligomers used for the FS and ␤-actin probes were generated by performing PCR on human granulosa cell cDNA using previously described primer sets (24). The forward FSRP primer spanned the first intron, and its sequence was CGCCCGGTG-GTGTTTG.…”

Section: Northern Analysismentioning

confidence: 99%

Human Follistatin-Related Protein: A Structural Homologue of Follistatin with Nuclear Localization

Tortoriello

Sidis

Holtzman³

et al. 2001

Endocrinology

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Follistatin-related protein is a recently discovered glycoprotein that is highly homologous in both primary sequence and exon/intron domain structure to the activin-binding protein, follistatin. We explored their potential for functional redundancy by investigating the relative affinities and kinetics of their interactions with activin, bone morphogenic protein-6, and bone morphogenic protein-7 and by exploring their expression and distribution in human tissues and cells. Follistatin and follistatin-related protein mRNA were ubiquitous by Northern analyses, although their sites of peak distribution differed, with follistatin-related protein and follistatin predominating in the placenta and ovary, respectively. Follistatin-related protein, like follistatin, preferentially bound activin with high affinity and in an essentially irreversible fashion. Although follistatin-related protein, like follistatin, possesses a signal sequence and no known nuclear localization signals, its secretion was undetectable in most cell lines by RIA. Intriguingly, follistatin-related protein was identified as a nuclear protein in human granulosa cells and all human cell lines tested. Furthermore, Western analyses of CHO cells transfected with human follistatin-related protein revealed this protein to reside within the insoluble nuclear protein fraction. We conclude that despite its remarkably high level of similarity to follistatin with regard to structure and activin binding kinetics, follistatin-related protein is a nuclear as well as a secretory protein that may perform distinct intracellular actions.

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Analysis of follicular fluid hormone concentrations and granulosa cell mRNA levels for the inhibin-activin-follistatin system: relation to oocyte and embryo characteristics

Cited by 33 publications

References 33 publications

Follicular steroid hormones as markers of oocyte quality and oocyte development potential

Follicular steroid hormones as markers of oocyte quality and oocyte development potential

Differential Distribution of Follistatin Isoforms: Application of a New FS315-Specific Immunoassay

Human Follistatin-Related Protein: A Structural Homologue of Follistatin with Nuclear Localization

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