[Hormone receptors and tumor markers in cancer of the endometrium].
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Biomedical subjects
Publications and source records attributed to P Franchimont.
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The structure of inhibin is known: it consists in a heterodimer constituted by one alpha and one beta subunits. The homodimer of beta A or the heterodimer beta A or the heterodimer beta A-beta B called activin A and B stimulates the release and the synthesis of FSH by gonadotrophs. Inhibin displays actions at hypophyseal, hypothalamic and gonadal levels. Produced by granulosa cells in female and by Sertoli cells in male, inhibin synthesis is stimulated by FSH, and reduced by hypophysectomy and progesterone. At the present time, there is no evidence for a signal from germinal cells to modify inhibin production. Inhibin secretion evolves with follicular maturation as aromatase activity whereas luteinization arrests its production. Nevertheless it seems to exist large difference in the regulation of inhibin secretion from one species to the other. Sperm inhibin levels are correlated with spermatozoa number. Its administration to the sheep induce either an anovulation or an increase of ovulation rate according to the scheme of treatment.
One of the major side effects induced by the in vivo administration of the murine monoclonal antibody OKT3 is a spontaneously reversible clinical syndrome associating in variable proportions depending on the patient: fever, chills, headaches, diarrhea and seldomly meningismus. Sera from 3 renal allograft recipients treated with OKT3 were studied and showed that a massive although transient release of some cytokines namely, Tumor Necrosis Factor alpha, Interleukin 2 and Interferon gamma is observed following the first OKT3 injection.
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79 women who had been menopausal for less than 36 months and who had not received any form of treatment to prevent bone loss were randomly assigned to a 12-month regimen of calcium 500 mg/day or calcium 500 mg plus intranasal salmon calcitonin 50 IU/day for 5 days per week. After 12 months of treatment bone mineral density had decreased in the calcium-only group by a mean of 3.16 (SEM 0.6)% (p less than 0.01) but had increased in the calcium plus calcitonin group by 1.38 (0.8)% (NS). The difference in response between the two treatment groups was also highly significant (p less than 0.01), as was the difference between values for hydroxyprolinuria/creatininuria (p less than 0.01). Endogenous calcitonin levels rose significantly in the calcium group but remained unchanged in calcitonin-treated patients. Treatment by calcitonin and calcium was not followed by increased secretion of parathyroid hormone. The findings suggest that intranasal calcitonin can counteract early postmenopausal bone loss.
Proteoglycan metabolism was studied by a specific human cartilage proteoglycan radioimmunoassay in human chondrocytes cultivated in clusters. In this culture system, after a few days, previously dissociated chondrocytes were aggregated. They then synthesized a new cartilage matrix and were morphologically differentiated; they had a round shape and were situated inside small individual cavities (lacunae). The amounts of proteoglycan released into culture medium and present in chondrocyte clusters were maximal on the third to fifth day of culture; production decreased and stabilized from the 10th day to the end of culture. During the first days of culture, monomeric proteoglycans were present in large proportion; they gradually decreased between the sixth and 11th day of culture. These results suggest a modified synthesis of proteoglycan and hyaluronic acid during cultivation.
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Human epidermal growth factor has been isolated from a concentrated chromatographic eluate of human urine. The purification method utilizes six chromatographic steps including adsorption to aminoethylcellulose (AE-11), gel filtration on Sephadex G-50, carboxymethylcellulose (CM-52) chromatography, ion-exchange HPLC and reverse-phase HPLC. The final product appears homogeneous and identical to pure gamma-urogastrone when analyzed by polyacrylamide gel electrophoresis and reverse-phase HPLC using two eluent systems. The yield of the method described above allowed the development of a sensitive radioimmunoassay system for this growth factor.
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A double-blind multicenter study comparing the effect of placenta eluted IgG and venoglobulins in the treatment of rheumatoid arthritis was conducted in 113 hospitalized patients. Rheumatoid arthritis was severe, classical (92 cases) or definite (21 cases), seropositive in 87 cases, with nodules in 32 cases; the mean duration of the disease was 10 years. The majority of patients had previously received numerous slow-acting drugs without result or with side-effects. A statistically significant decrease of all the quantitative indices but one (grip strength) was obtained with both products on the 8th day of treatment; the effect of placenta eluted IgG was statistically superior for the number of swollen joints (P less than 0.025), Ritchie's index (P less than 0.0005) and some extra-articular manifestations. There was no significant decrease in associated treatments and biological parameters (erythrocyte sedimentation rate, rheumatoid factor). Tolerance was excellent; some cases of benign venulitis were observed; treatment was never discontinued on account of side-effects. Further placebo-controlled of each of these immunoglobulins of placental origin are needed for firm conclusions to be drawn.
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Seventy-eight patients, 40 suffering from cervical arthrosis and 38 from lumbar arthrosis, received for a period of two weeks paracetamol or a new preparation of glaphenine, in a double blind study. The two drugs were found to have the same efficiency on the subjective parameters but high bioavailability glaphenine seems to have an effectiveness in the range of articulatory movements, which is not found with paracetamol. The side effects were quite equivalent.
The lectin-binding capacity of 96 normal human IgG, assessed by solid-phase radioimmunoassay, strikingly varied according to the lectin considered. Indeed, half of the IgG samples exhibited peanut agglutinin (PNA)- and pokeweed mitogen-specific binding capacities superior or equal to 4%, whereas less than 15% of IgG similarly bound to concanavalin A (Con A) and to phytohemagglutinin. The ability of those IgG to inhibit the Fc receptor (Fc-R) function of human monocytes, measured by a classical rosette assay, was inversely correlated to their binding ratios to PNA and Con A only. By affinity chromatography, three groups of IgG were separated: the IgG purified on agarose-PNA columns slightly reduced the Fc-R function (40-45% inhibition); the IgG purified on Sepharose-Con A columns exhibited the highest inhibitory properties (80-85% inhibition); the IgG that did not bind to PNA and Con A columns possessed intermediate inhibitory properties (65-70% inhibition). The different effect of IgG on Fc receptors was conserved when monocytes were first treated by trypsin and was unrelated to their specific binding to human monocytes, to their subclasses, and to their C1q- or protein A-binding capacities. Incubation of monocytes with D-galactose (10 mM) significantly improved their capacity to form IgG rosettes, whereas their incubation with D-mannose (10 mM) significantly reduced the Fc-R function. Scatchard plots of 125I-IgG1 myeloma protein binding to monocytes were linear under basal conditions, as well as after a prior incubation of the cells with D-galactose or D-mannose. Monocytes bound about 16,000 molecules of IgG1 per cell in each instance. In contrast, the mean association constant (Ka) for IgG1 binding was 2.59 +/- 0.50 X 10(8) M-1 under basal conditions, 4.4 +/- 0.75 X 10(8) M-1 after D-galactose incubation, and 1.35 +/- 0.50 X 10(8) M-1 after D-mannose incubation. These data suggest that the level of human monocyte Fc-R function blockade induced by human IgG depends mainly on the presence of "accessible" galactosyl or mannosyl residues in the Fc domain and that the modulation of the Fc-R function induced by these carbohydrates is due to a change in the affinity rather than in the number of single class of high-affinity binding sites.