Plasma proinsulin, C-peptide and sex hormone concentrations in regularly menstruating premenopausal females with ovulatory and anovulatory menstrual cycles.

AIM: Highly active females are at risk of athletic menstrual irregularities including anovulatory menstrual cycles, oligomenorrhea and even amenorrhea. On the other hand, the functional relationship between endocrine pancreas and ovaries is supported by numerous studies indicating that disturbed female sex hormone secretion coexists with insulin resistance and glucose intolerance. However, the relationship between circulating beta islet and ovarian hormones in regularly menstruating active women with ovulatory and anovulatory menstrual cycle has not been studied. METHODS: A total of 32 regularly menstruating women participated in the study. Prospective subjects monitored their BBT for 3 months before the study. The determination of plasma progesterone levels between days 5-8 and again between days 19-22 of the menstrual cycles made possible the classification of subjects as ovulating or non-ovulating. Plasma 17-beta-estradiol, testosterone, insulin, proinsulin, C-peptide and glucose concentrations were assayed on the same menstrual cycle days as progesterone. RESULTS: There were no differences in circulating insulin, C-peptide and glucose between non-ovulating and ovulating women. In contrast, in non-ovulating subjects plasma proinsulin concentrations between days 19-22 were slightly, but significantly higher than between days 5-8 of the menstrual cycle (P<0.05). Exclusively in non-ovulating women significant and positive correlation was noted between circulating proinsulin and 17-beta-estradiol in data collected from both days 5-8 and 19-22 of the menstrual cycle (P<0.008). CONCLUSIONS: Our results indicate that in the face of low circulating progesterone and subsequent anovulation circulating 17-beta-estradiol slightly, but significantly, affect either pancreatic beta-cell biosynthetic activity or proinsulin hepatic and/or renal clearance.

Uptake of radiolabeled morphiceptin and its analogs by experimental mammary adenocarcinoma: in vitro and in vivo studies.

Morphiceptin (Tyr-Pro-Phe-Pro-NH(2)) and its analogs modified at position 3: [D-Phe(3)]morphiceptin, [D-ClPhe(3)]morphiceptin and [D-Cl(2)Phe(3)]morphiceptin were synthesized and labeled with [(125)I] or [(131)I]. Their binding to membranes isolated from experimental adenocarcinoma was examined in vitro with the use of a cross-linking assay followed by the Western blot technique. The radioactive complex had molecular weight of about 65 kDa and was detectable by anti-mu-opioid receptor polyclonal antibody. Expression of the mu-opioid receptor in mouse mammary adenocarcinoma was confirmed by reverse transcriptase-polymerase chain reaction. The binding studies showed the highest affinity and capacity for [D-Phe(3)]morphiceptin (K(d) 0.39 and B(max) 1112) and [D-ClPhe(3)]morphiceptin (K(d) 1.8 and B(max) 220). Morphiceptin and its D-Cl(2)Phe analog had significantly lower B(max) values (131 and 83, respectively). Biodistribution experiments in tumor-bearing C3H/Bi mice with the use of the (131)I-labeled peptides confirmed the results of our in vitro studies. The highest accumulation of radioactive peptides in the tumor tissue was also found for peptides with D-Phe and D-ClPhe.

Uptake of radiolabelled alpha-fetoprotein by experimental mammary adenocarcinoma and adenoma: in vivo and in vitro studies.

The biodistribution of iodine-labelled alpha-fetoprotein ( I-AFP) in experimental mammary tumours was studied. C3H mice with subcutaneously transplanted mammary adenocarcinoma and Sprague-Dawley rats treated with -methyl- -nitrosourea for mammary adenoma induction were used as animal models. The accumulation of labelled I-AFP in mouse mammary adenocarcinoma was significantly higher than that in rat mammary adenoma. The tumour/muscle radioactivity ratios increased with time and, 48 h after intravenous injection, were estimated as 23.4 and 6.7, respectively. For experiments, extracts from both mammary tumours were prepared. The extracts were subjected to sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE), transferred to polyvinylidene difluoride (PVDF) membranes and incubated with I-AFP. A single major AFP-binding protein with a molecular weight of about 30 kDa was detected in both extracts. The amount of AFP-binding protein was clearly higher for adenocarcinoma than for adenoma. In the presence of cross-linking reagent, I-AFP formed a complex (about 100 kDa) with adenocarcinoma proteins.