[Laparoscopic surgery versus laparotomy. Comparative analysis of stress markers].

The place of laparoscopic surgery continues to increase in the field of surgery in our specialty. Although the advantages would seem to be obvious, it seemed to us interesting to quantify, if possible, the parameters of operative stress and compare laparoscopic surgery with conventional surgery. Markers studied are Prolactin, Cortisol, Adrenaline, Nor-Adrenaline, Dopamine and the Beta-Endorphins.

[In vitro fertilization. Analysis of results after the first 2 years' activity].

413 menstrual cycles were monitored in the first two years of the work of the In-Vitro Fertilization Unit in La Pitié-Salpêtrière. On-going pregnancies were achieved from the very first months of activity, with a level which stayed relatively constant in the first year. Technical changes were introduced and in particular a higher recovery rate of oocytes when ultrasound was used and above all when LH-RH analogues were used in the process of stimulation.

Simultaneous evaluation of mRNAs of dopamine ?-hydroxylase, tyrosine hydroxylase and proenkephalin a from three human pheochromocytomas.

Using the rabbit reticulocyte cell-free translation system, the relative proportions of in vitro translatable mRNAs of three proteins in three human pheochromocytomas: tyrosine hydroxylase (TH), dopamine ?-hydroxylase (DBH) and proenkephalin A have been compared. TH expression appeared rather constant in the three tumors. In contrast, those of DBH and proenkephalin A were more variable.

In vitro translation of human pheochromocytoma messenger RNAs: characterization of tyrosine-hydroxylase and dopamine-beta-hydroxylase.

mRNAs extracted from human pheochromocytoma were translated in vitro in a lysate of a rabbit reticulocytes. Two enzymes of the biosynthetic pathway of the catecholamines, tyrosine-hydroxylase (TH) and dopamine-beta-hydroxylase (DBH), were characterized as translation products after immunoprecipitation by specific antisera and electrophoretic analysis. The precursor of TH is a polypeptide having a molecular mass of 62,000 identical to that found for the mature protein.