Maguelone G. Forest

TL;DR: The nucleotide sequence of the two highly homologous genes encoding 3β–HSD isoenzymes in three classic 3β-HSD deficient patients belonging to two apparently unrelated pedigrees is described, providing the first elucidation of the molecular basis of this disorder.

TL;DR: The finding of a normal type I 3 β-HSD gene explains the elevated Δ5-steroids and mild virilization of affected girls at birth and the consequences of the missense mutations on some domains of the 3β-enzyme, such as membrane-spanning domains, cofactor- binding site, and steroid-binding site were reviewed.

TL;DR: It is suggested that a very weak residual activity of the normal type II 3 beta HSD enzyme could prevent salt loss, but it was insufficient for normal male sex differentiation.

TL;DR: In vitro analysis of mutant enzymes expressed in heterologous COS-1 cells found that Vmax values for PREG and NAD+ were lower for both mutant enzymes; thus, the in vitro overall efficiency, relative to the normal enzyme, is approximate as 0.3% and 0.2% respectively.

TL;DR: A prenatal diagnosis in a partial form of AIS associated with a point mutation R840H of the AR gene is reported, and the polymorphic number of trinucleotide CAG repeats located in the exon 1 can be used for prenatal diagnosis, providing prior study of the nuclear family.