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Abstract
It is well established that GH-like proteins and mRNA are present in extrapituitary tissues, but it is not known whether this reflects ectopic transcription of the pituitary GH gene or the expression of a closely related gene. This possibility was, therefore, further investigated.
Immunoreactive (IR) GH-like proteins were readily measured by RIA and immunoblotting in hypothalamic and extrahypothalamic brain tissues of the domestic fowl, in which GH-IR was similar in size and antigenicity to pituitary GH. RT-PCR of mRNA from these brain tissues, with oligonucleotide primers spanning the coding region of pituitary GH cDNA, also generated cDNA fragments identical in size (689 bp) to pituitary GH cDNA. The amplified brain cDNA sequences contained BamH1 and Rsa1 cleavage sites similar to those located in pituitary GH cDNA. These cDNA sequences also hybridized with a cDNA probe for chicken GH cDNA, producing moieties of expected size that were identical to the hybridizing moieties in pituitary tissue. The nucleotide sequences of the PCR products generated from hypothalamic and extrahypothalamic brain tissues, determined by a modified cycle dideoxy chain termination method, were also identical to pituitary GH cDNA. This homology extended over 594 bp of the hypothalamic cDNA fragment (spanning nucleotides 65 to 659 of the pituitary GH cDNA and its coding region for amino acids 4 to 201) and 550 bp of the extrahypothalamic cDNA fragment (spanning nucleotides 76 to 626 of pituitary GH cDNA and its coding region for amino acids 8 to 190).
These results clearly establish that pituitary GH mRNA sequences are transcribed in hypothalamic and extrahypothalamic tissues of the chicken brain, in which GH-IR proteins are abundantly located. However, as GH mRNA could not be detected in the chicken brain by Northern blotting, its turnover may be more rapid than in pituitary tissue. The local production of GH within the brain nevertheless suggests that it has paracrine roles in modulating neural or neuroendocrine function.
Journal of Endocrinology (1995) 147, 413–422
Centro de Estudios Farmacológicos y Botánicos (CEFYBO), Dpto. de Química Biológica, Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET)-Facultad de Medicina, UBA, Paraguay 2155, 16° P, C1121ABG Buenos Aires, Argentina
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Centro de Estudios Farmacológicos y Botánicos (CEFYBO), Dpto. de Química Biológica, Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET)-Facultad de Medicina, UBA, Paraguay 2155, 16° P, C1121ABG Buenos Aires, Argentina
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pituitary and the gonads, which form the reproductive axis. The Ob-R has been found all along the hypothalamus–pituitary–gonads (HPG) axis and several groups have demonstrated the presence of Ob-R mRNA in endocrine tissue in the rat. In humans and rodents
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A fractionation procedure used for the purification of glycoprotein hormones from pituitary glands of the human being (Stockell Hartree, 1966), horse (Stockell Hartree, Mills, Welch & Thomas, 1968) and chicken (Stockell Hartree & Cunningham, 1969) was also applied to acetone-dried dog pituitaries. The pituitaries were removed from dogs generally within 60 h of death. The glands were washed in acetone and stored in 20 volumes of acetone at 4 °C for several weeks. An acetone powder was prepared by drying the pituitaries in air and grinding them in a glass mortar. The yield of powder from 980 pituitaries was 10·3 g. This material was extracted with 6% ammonium acetate at pH 5·1 in 40% ethanol and the soluble extract chromatographed on a column of CM-cellulose equilibrated with 4 mm-ammonium acetate buffer at pH 5·5 as described previously (Stockell Hartree, 1966; Stockell Hartree et al. 1968; Stockell Hartree &
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The pathogenesis of sporadic pituitary tumours remains elusive. Recently, a new candidate gene has been described which is able to induce pituitary cell transformation, and the expression of which appears to be strongly correlated with pituitary tumorigenesis. The so-called pituitary tumour transforming gene (PTTG) encodes a 23 kDa, 202 amino acid protein, and is located on chromosome 5q33, a locus previously associated with recurrent lung cancer and acute myelogenous leukaemias. Although the precise function of PTTG protein is unknown, in vitro experiments have demonstrated that it is capable of inducing fibroblast growth factor (FGF) expression. Mutation of the two proline-rich domains of the PTTG protein has also been shown to abolish subsequent FGF induction. Furthermore, in patients with pituitary adenomas, serum FGF concentrations fall post-operatively after successful excision of the tumour.
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Introduction Arginine vasopressin (AVP) is an important physiologic regulator of adrenocorticotropin (ACTH) secretion from the anterior pituitary ( Aguilera 1994 ). The effects of AVP on corticotroph cells of the anterior pituitary
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Introduction Acromegaly is caused by excessive growth hormone (GH) secretion from pituitary GH-secreting adenomas. Treatment of acromegaly patients often involves combining surgical, pharmacological, and radiotherapeutic approaches to control
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is certainly perturbed (if not quite guided) by those whose bold ideas gain currency. In the present essay, we trace the impact of the work of Geoffrey Harris on our understanding of the posterior pituitary gland, although whether our understanding
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ABSTRACT
Thyrotrophin in individual pituitaries obtained from fetal and prepubertal pigs was quantified by homologous radioimmunoassay (RIA) and heterologous radioreceptor assay (RRA). Relative evolution of pituitary TSH contents and concentrations with age were in good agreement as measured by both assay systems although the quantity of TSH detected by RRA appeared consistently lower than that measured by RIA. Thyrotrophin was first detected in pituitaries of fetal pigs at day 75 of gestation. Thereafter the pituitary content of TSH increased to approximately 45 μg/pituitary in the oldest group tested (6 weeks of age). The pituitary TSH concentration rose sharply until birth (114±1 day post coitum) and thereafter remained increased at a concentration of approximately 400 ng/mg wet weight.
J. Endocr. (1986) 111, 111–115
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Introduction Corticotropin-releasing factor (CRF) and arginine vasopressin (AVP) are the two major regulatory peptides in the hypothalamic–pituitary–adrenal (HPA) axis. CRF, produced in the hypothalamic paraventricular nucleus (PVN
