J. Closset

Cellular localization of IGF-I and IGF-II mRNAs in immature hypophysectomized rat testis and epididymis after in vivo hormonal treatment.

IGF-I and II genes expression has been localized by in situ hybridization in testis and epididymis of immature hypophysectomized rats treated in vivo with either pFSH, hLH, bGH, hPRL or with saline. IGF-I mRNA expression was found in both Sertoli and Leydig cells after treatment with either FSH or LH. IGF-I mRNA was highly expressed in germ cells after FSH stimulation and to a lesser extent after GH or LH treatments. However, its expression was very low in hypophysectomized control or PRL treated rats. IGF-I mRNA was also expressed in stromal cells of epididymis after LH treatment and to a lesser extent after GH stimulation. In contrast, IGF-II mRNA expression was detected in all testicular cell types whatever the hormonal treatment (FSH, LH, GH, PRL). For each hormonal treatment testicular sections were examined after immunohistochemical staining with specific antisera against IGF-I and IGF-II. Both in situ hybridization and immunohistochemical data were examined in order to determine the testicular sites of synthesis of IGF-I and IGF-II.

Selective Radioimmunoassays for Human Luteinizing Hormone (hLH) and Human Chorionic Gonadotropin (hCG)

Highly specific radioimmunoassay systems were developed for measurement of hLH and hCG using antisera purified by affinity chromarography or simple adsorption to select the antibodies reacting specifically with either gonadotropin. Such systems permit specific measurement of lLH and hCG in samples containing both. These assays are suitable for various clinical and physiological studies, particularly, study of pituitary functions in the presence of chorionic or trophoblastic secretion.

Human thyrotropin and its α and β subunits

AbstractA new procedure is described for the isolation of human thyrotropin using ion exchange chromatography and gel nitration onlyThyroid stimulating activity of the final preparation of our human thyrotropin amounted to 0.5 IU/mg by bioassayThe α and β subunit of the hormone were also obtained by a new procedure. In this method the native hormone was incubated in an acidified 8 m urea solution and the chains were then separated by ion exchange chromatography and gel filtrationThe amino-terminal residues of the α and β chains were valine and phenylalanine respectivelyThe β chain appears shorter at its carboxy-terminal end by one methionine residue than its bovine counterpartCross-contamination of the subunit preparations were measured by radioimmunoassay. The β chain exhibited a contamination of about 3 percent of the α subunit by weight. The α subunit is contaminated by about one percent of the β chain by weight