A prolactin-inhibiting factor within the precursor for human gonadotropin-releasing hormone

  title={A prolactin-inhibiting factor within the precursor for human gonadotropin-releasing hormone},
  author={K{\'a}roly Nikolics and Anthony John Mason and {\'E}va Szőnyi and Janakiraman Ramachandran and P. H. Seeburg},
The cloned complementary DNA sequence encoding the human gonadotropin-releasing hormone (GnRH) precursor protein was used to construct an expression vector for the bacterial synthesis of the 56-amino acid GnRH-associated peptide (GAP). GAP was found to be a potent inhibitor of prolactin secretion and to stimulate the release of gonadotropins in rat pituitary cell cultures. Active immunization with peptides corresponding to GAP sequences led to greatly increased prolactin secretion in rabbits. 
The Biosynthetic Precursor of Gonadotropin-Releasing Hormone: A Multifunctional Prohormone
Mammalian reproduction is regulated by the pituitary hormones luteinizing hormone (LH), follicle stimulating hormone (FSH), and prolactin, which stimulates ovulation and corpus luteum formation in females and androgen secretion in males.
Evolution of gonadotropin-releasing hormones
Gonadotropin-Releasing Hormone-associated Peptide Immunoreactivity in Bovine Colostrum
The presence of GAP immunoreactivity in bovine colostrum suggests that the GnRH precursor is synthesized and processed in mammary tissue itself, and is of low molecular weight and a high hydrophobic character.
The gonadotropin-releasing hormone associated peptide reduces calcium entry in prolactin-secreting cells.
It is shown that GAP reduces intracellular Ca++ levels, [Ca++]i, and inhibits Ca++ transients in these cells and may explain the inhibitory effect of GAP on hormonal secretion by PRL-secreting cells.
Partial purification of a hypothalamic factor that inhibits gonadotropin-releasing hormone-stimulated luteinizing hormone release.
A protein that suppresses GnRH-stimulated LH release from dispersed rat anterior pituitary cells was purified from rat hypothalami by chromatography on Sephadex G-25, carboxymethyl cellulose, and
Biological Activity of Non-GnRH Synthetic Peptide Sequences of the GnRH Precursor
The demonstration of GnRH biosynthesis by tryptic and carboxypeptidase B cleavage of a higher molecular precursor in sheep, pig and rat hypothalamus, and the postulate that pGlu1 is derived from
The GnRH family of peptides


Gonadotropin-Releasing Hormone: One Polypeptide Regulates Secretion of Luteinizing and Follicle-Stimulating Hormones
It appears that this peptide represents the hypothalamic hormone regulating the secretion of both luteinizing hormone and follicle-stimulating hormone from the pituitaries of several species.
Characterization of cDNA for precursor of human luteinizing hormone releasing hormone
Cloned genomic and cDNA sequences encoding the precursor form of LHRH, the existence of which had been suggested from Chromatographic studies of hypothalamic8,13 and placental8 extracts, are isolated.
Immunocytochemical localization in rat brain of a prolactin release-inhibiting sequence of gonadotropin-releasing hormone prohormone
It is reported here that a substance recognized by this antibody is present in GnRH-containing neurones of the rat brain and appears to coexist with GnRH in secretory granules of nerve terminals in the median eminence, indicating homology between hypothalamic and placental prohormones for GnRH.
Gonadotropin-releasing hormone in milk.
The hypothalamic hormone gonadotropin-releasing hormone (GnRH) has been found in milk of man, cow, and rat and may influence the secretion of the gonadotropic hormones in neonates.
Expression in Escherichia coli of a chemically synthesized gene for the hormone somatostatin.
This work has reported the first synthesis of a functional polypeptide product from a gene of chemically synthesized origin, including the sequence of amino acids corresponding to somatostatin, in vitro.
Gonadocrinins: Peptides in Ovarian Follicular Fluid Stimulating the Secretion of Pituitary Gonadotropins*
A newly discovered small peptide purified from rat follicular fluid stimulates the pituitary to release FSH and LH in vitro as well as in vivo, and is named gonadocrinin for operational facility.
Placental luteinizing hormone-releasing factor and its synthesis.
The synthesis of a placental luteinizing hormone-releasing factor (pLRF), which is immunologically, physiochemically, and biologically indistinguishable from synthetic LRF, was demonstrated and data indicate that the pLRF that was released initially was endogenous, whereas that released subsequently reflected synthesis.
Vasoactive intestinal peptide is a physiological mediator of prolactin release in the rat.
It is concluded that VIP mediates the acute PRL response to suckling and is required for maintenance of PRL levels in continuously suckling animals but is not the only factor causing PRL elevation.
Characterization of a growth hormone-releasing factor from a human pancreatic islet tumour
A synthetic replicate of this peptide, termed human pancreatic tumour GRF [hpGRF(1–40)]-OH, co-elutes on HPLC with the native peptide and is highly potent in stimulating GH secretion in vitro and in vivo.