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Biomedical subjects

N Josso

Publications and source records attributed to N Josso.

138 records · Page 8Linked to original sources
PubMedDate not supplied

Hermaphroditism pathology.

Hermaphroditism is a more general term for the discrepancy between the phenotype and the genotype of sex development than sexual ambiguity, which refers mainly to external genitalia anomalies. Hermaphroditism is studied on an historical and pathogenetical perspective. Short embryological summaries are integrated. The defects of sexual differentiation due to a hormonal deficiency are first studied: androgen insensitivity, steroid 5 alpha-reductase 2 deficiency, defects of testosterone synthesis, persistent mullerian ducts syndrome. Sexual determinism deficiencies come after: Turner syndrome, XX males, pure gonadal dysgenesis, and true hermaphroditism, mixed gonadal dysgenesis, Drash and Frasier syndrome. Tumors of dysgenetic gonads followed. Mixed tumors developed in dysgenetic gonads are gonadoblastoma and dysgerminoma. Sex cord tumors are androgen insensitivity associated tumors, Leydig cells tumors and adrenal cell inclusion tumors. New perspectives open by sex reversion genes are open.

Androgens↗
PubMedDate not supplied

[Anti-mullerian hormone : a new glycoprotein (author's transl)].

The hypothesis that anti-müllerian hormone might be a glycoprotein was suggested by the discrepancy between various methods of evaluation of the molecular weight of the substance responsible for anti-müllerian activity. Incorporation of radioactive fucose to the proteins synthesised by the fetal calf testis in vitro resulted in specific labelling of bioactive molecules, once labelled contaminants had been removed by prior partial purification.

Aging↗
PubMedDate not supplied

[Anti-müllerian hormone and lectins. New perspectives (author's transl)].

Anti-müllerian hormone (AMH), responsible for the regression of müllerian ducts in male fetuses in a glycoprotein. Its affinity towards 7 different lectins has been tested in a density gradient sedimentation system. AMH binds with low affinity to the E subunit of the Phaseolus vulgaris lectin. On the opposite, high affinity binding was observed with wheat germ agglutinin (WGA) and confirmed by affinity chromatography on immobilized WGA. Anti-müllerian activity was totally bound by the column and eluted by N-acetyl-glucosamine. These data confirm the glycoprotein nature of AMH and offer great promise for its purification.

Anti-Mullerian Hormone↗