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We first cloned porcine GDF-9 complementary DNA and then injected its gene fragments into the ovary in gilts to investigate the ovarian function of GDF-9 in pigs. The ovaries of 2-month-old prepubertal gilts were injected with GDF-9 gene fragments to investigate the role of GDF-9 in early folliculogenesis. These results showed that exogenous GDF-9 can promote early folliculogenesis in the porcine ovary, as well as a novel therapy for prevention and treatment of fertility problems associated with ovarian dysfunction.
Source link: https://doi.org/10.1530/rep.1.00224
Another cDNA clone with a 533 bp insert was isolated, using a subclone of L12 in pUC19 as the hybridization probe. According to adenohypophysial RNA, chicken and Japanese quail adenohypophyses contained RNA species of approximately 0b78 and 1 kb respectively, according to the pL12 cDNA insert to adenohypophysial RNA. The number of this RNA species was ten times higher in adult male quails kept at room temperature for longer days than those kept under shorter days at 7 u00b0C. The chicken's cDNA sequence in the LH-u03b2 cDNA sequence to that of mammals is lower than that found in mammals. The chicken LH-u03b2 subunit's deduced amino acid sequence supports the belief that the number of proline residues rises in the LH-u03b2 subunit, the closer phylogenetically the vertebrate is to mammals.
Source link: https://doi.org/10.1677/jme.0.0030129
ABSTRACT A cDNA library was created from mRNA extracted from anterior pituitary glands of incubating bantam hens, in which prolactin mRNA levels were expected to be high. The shorter clone was found to be a truncated cDNA sample, but otherwise identical to the longer clone. The protein was expected to have a 30 amino acid signal sequence, but it was later cleaved off to produce a mature protein with 199 amino acids. This similarity has led to the conclusion that PRL101 is a chicken prolactin cDNA clone. An abundant mRNA of about 880 b was discovered in poly + RNA from pituitary glands probed with PRL101. According to an analysis of chicken genomic DNA, there is only one copy of the prolactin gene in the genome. The PRL101 hybridized well to genomic DNA from closely related galliforms and less strongly to DNA from more distantly related species compared to PRL101.
Source link: https://doi.org/10.1677/jme.0.0020021
At the silver stage, the ABSTRACT Oestradiol therapy improves type-II gonadotrophin synthesis in the European eel. We cloned and characterized the cDNA encoding the eel GTH-II's u03b2 subunit of eel GTH-II, resulting in the first step in investigating the molecular mechanisms involved in this stimulation. The localization of the putative cleavage site of a 24 amino acid signal peptide was allowed by comparison with GTH-III from other teleost fish. The resulting 116 amino acid apopeptide had well-conserved cysteine positions and a putative N-linked glycosylation site, and homology was 70% with GTH-u2013II from other animals and birds, 58% with mammalian FSH, and just 35% with fish GTH-I. The putative GTH-III mRNA was found to have a significant positive effect of oestradiol treatment in the level of the putative GTH-II u03b2-subunit mRNA. This supports our argument that the European eel provides a good model for investigating gonadotrophin synthesis by gonadal steroids.
Source link: https://doi.org/10.1677/jme.0.0040257
ABSTRACT This research was conducted using antiserum against ovine prolactin from a cDNA library of porcine anterior pituitary, and their nucleotide sequences were determined by the chain-termination procedure. The mature prolactin molecule contained a signal sequence of 30 amino acids and a further 199 amino acids in the composite sequence of 957 nucleotides. The length of the porcine prolactin mRNA was about 1 kb, according to a Northern blot study, about 1 kb. The hydropathy and secondary structure of porcine prolactin were investigated and compared to those of porcine GH, which shares the same ancestral gene, according to the same ancestral gene. Both hormone-producing regions had similar hydrophilicity, and the predicted secondary structures showed that these regions in each hormone had altered structures, with differences in the extension of the hydrophilic residues outside the molecule.
Source link: https://doi.org/10.1677/jme.0.0040135
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