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PubMedDate not supplied

"Joining peptide" of pro-opiomelanocortin. I. Radioimmunoassay and extraction of related peptides from pituitary glands.

In order to immunoassay the specific region of bovine pituitary pro-opiomelanocortin (POMC) between ACTH and gamma-MSH, referred to as "joining peptide," antisera were prepared against the synthetic amidated decapeptide Val-Ala-Val-Gly-Glu-Gly-Pro-Gly-Pro-Arg-NH2. The non-amidated peptide represents residues -23 to -14 of bovine POMC. An NH2-terminal tyrosine analog of the decapeptide was used as the radioligand. Under optimal conditions, immunoassay with selected antisera exhibited a sensitivity (50% displacement of the radioligand) toward the decapeptide in the range of 31-55 pg. Immunoreactivity found in extracts of fresh or lyophilized bovine pituitary glands displaced the iodinated Tyr-decapeptide in the RIA in a parallel manner. The amount of immunoreactive (ir)-material was dependent upon the state of preservation of the tissue, the method of extraction, and the particular antiserum used. Extractable immunoreactivity was separated into low (Mr 1,500) and high (Mr 17,000) molecular weight peptides using gel chromatography (G-75). Additional ir-material appeared in the void volume (Mr greater than 22,500). Thus, these antisera have the capacity to interact not only with a region of the joining peptide but also with its larger, and apparent precursor forms. The immunoassay developed should be valuable in understanding the disposition and processing in this specific region of POMC.

Animals↗
PubMed1998

Specific receptors for synthetic GH secretagogues in the human brain and pituitary gland.

In vitro studies have been performed to demonstrate and characterize specific binding sites for synthetic GH secretagogues (sGHS) on membranes from pituitary gland and different human brain regions. A binding assay for sGHS was established using a peptidyl sGHS (Tyr-Ala-hexarelin) which had been radioiodinated to high specific activity at the Tyr residue. Specific binding sites for 125I-labelled Tyr-Ala-hexarelin were detected mainly in membranes isolated from pituitary gland and hypothalamus, but they were also present in other brain areas such as choroid plexus, cerebral cortex, hippocampus and medulla oblongata with no sex-related differences. In contrast, negligible binding was found in the thalamus, striatum, substantia nigra, cerebellum and corpus callosum. The binding of 125I-labelled Tyr-Ala-hexarelin to membrane-binding sites is a saturable and reversible process, depending on incubation time and pH of the buffer. Scatchard analysis of the binding revealed a finite number of binding sites in the hypothalamus and pituitary gland with a dissociation constant (Kd) of (1.5 +/- 0.3) x 10(-9) and (2.1 +/- 0.4) x 10(-9) mol/l respectively. Receptor activity is sensitive to trypsin and phospholipase C digestion, suggesting that protein and phospholipids are essential for the binding of 125I-labelled Tyr-Ala-hexarelin. The binding of 125I-labelled Tyr-Ala-hexarelin to pituitary and hypothalamic membranes was displaced in a dose-dependent manner by different unlabelled synthetic peptidyl (Tyr-Ala-hexarelin, GHRP2, hexarelin, GHRP6) and non-peptidyl (MK 0677) sGHS. An inhibition of the specific binding was also observed when binding was performed in the presence of [D-Arg1-D-Phe5-D-Trp7,9-Leu11]-substance P, a substance P antagonist that has been found to inhibit GH release in response to sGHS. In contrast, no competition was observed in the presence of other neuropeptides (GHRH, somatostatin, galanin or Met-enkephalin) which have a known influence on GH release. In conclusion, the present data demonstrate that sGHS have specific receptors in human brain and pituitary gland and reinforce the hypothesis that these compounds could be the synthetic counterpart of an endogenous GH secretagogue involved in the neuroendocrine control of GH secretion and possibly in other central activities.

Adult↗
PubMed2003

The effects of frequency-encoding gradient upon detectability of the margins and height measurements of normal adult pituitary glands.

We investigated the effects of frequency-encoding gradient (FEG) upon detectability and height measurements of the normal adult pituitary gland. We obtained two sets of T1-weighted sagittal images of the pituitary gland from 70 adult subjects without known pituitary dysfunction using 1.5 tesla imagers; one with an inferior-superior FEG, and one with an anterior-posterior FEG. We classified the subjects into three types according to the distribution of fatty marrow in the clivus. Each set of images was assessed for pituitary height on midline sagittal images, and detectability of pituitary margins. Height measurements and detectability scores were evaluated for significant difference between the two FEGs. In subjects with fatty marrow in the clivus, there was significant difference between pituitary height measurements (P < 0.005) and pituitary margin detectability (P < 0.001). Care should be taken to image the pituitary gland using an anterior-posterior FEG.

Adult↗
PubMed1982

The presence of glial fibrillary acidic protein in the human pituitary gland.

The presence of glial fibrillary acidic protein (GFAP) was studied in human pituitary glands with the peroxidase-antiperoxidase (PAP) method. Positive reaction was observed in cells and processes of the neurohypophysis, in occasional cells lining the Rathke's cysts of the pars intermedia, and in scattered star-shaped cells and small follicles of the pars distalis. GFAP immunoreactivity was sparse and variable in amount from case to case. An increase in GFAP-immunoreactivity was observed as a reaction to injury. GFAP-positive cells were seen within and around pituitary adenomas regardless of their secretory cell type. Evidence is presented to indicate that these cells do not contain conventional pituitary hormones. It is postulated that the GFAP-positive cells of the pars distalis are nonsecretory elements, identical to the folliculostellate cells. They may become visible by immunostaining following increased synthesis of GFAP. The latter may be a response to cell injury or metabolic changes in adjacent secretory elements. A similar reaction in pituicytes may explain the appearance of immunoreactive GFAP in the neural lobe. The presence of GFAP in the adenohypophysis suggests that some of their cells are neuroectodermal in origin.

Adenoma↗
PubMed1995

Further studies on the regulation, localization and function of the TRH-like peptide pyroglutamyl-glutamyl-prolineamide in the rat anterior pituitary gland.

Recent evidence shows that thyrotrophin-releasing hormone (TRH) immunoreactivity in the rat anterior pituitary gland is accounted for by the TRH-like tripeptide pyroglutamyl-glutamyl-prolineamide (pGlu-Glu-ProNH2, < EEP-NH2). The present study was undertaken to investigate further the regulation, localization and possible intrapituitary function of < EEP-NH2. Anterior pituitary levels of < EEP-NH2 were determined between days 5 and 35 of life, during the oestrous cycle and after treatment with the luteinizing hormone-releasing hormone (LHRH) antagonist Org 30276. Treatment of adult males with the LHRH antagonist either for 1 day (500 micrograms/100 g body weight) or for 5 days (50 micrograms/100 g body weight) reduced anterior pituitary < EEP-NH2 levels by 25-30% (P < 0.05 versus saline-treated controls). Anterior pituitary < EEP-NH2 increased between days 5 and 35 of life. In females, these levels were 2- to 3-fold higher (P < 0.05) than in males between days 15 and 25 after birth; these changes corresponded with the higher plasma follicle-stimulating hormone (FSH) levels in the female rats. After day 25, < EEP-NH2 levels in female rats decreased in parallel with a decrease in plasma FSH. Injections with the LHRH antagonist (500 micrograms/100 g body weight), starting on day 22 of life, led to reduced contents of < EEP-NH2 in the anterior pituitary gland of female rats on days 26 and 30 (55 and 35% decrease respectively). Levels of < EEP-NH2 in the anterior pituitary gland did not change significantly during the oestrous cycle.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1981

Effects of dopamine on prolactin secretion and cyclic AMP accumulation in the rat anterior pituitary gland.

The effects of dopamine on pituitary prolactin secretion and pituitary cyclic AMP accumulation were studied by using anterior pituitary glands from adult female rats, incubated in vitro. During 2h incubations, significant inhibition of prolactin secretion was achieved at concentrations between 1 and 10nm-dopamine. However, 0.1-1mum-dopamine was required before a significant decrease in pituitary cyclic AMP content was observed. In the presence of 1mum-dopamine, pituitary cyclic AMP content decreased rapidly to reach about 75% of the control value within 20min and there was no further decrease for at least 2h. Incubation with the phosphodiesterase inhibitors theophylline (8mm) or isobutylmethylxanthine (2mm) increased pituitary cyclic AMP concentrations 3- and 6-fold respectively. Dopamine (1mum) had no effect on the cyclic AMP accumulation measured in the presence of theophylline, but inhibited the isobutylmethylxanthine-induced increase by 50%. The dopamine inhibition of prolactin secretion was not affected by either inhibitor. Two derivatives of cyclic AMP (dibutyryl cyclic AMP and 8-bromo cyclic AMP) were unable to block the dopamine (1mum) inhibition of prolactin secretion, although 8-bromo cyclic AMP (2mm) significantly stimulated prolactin secretion and both compounds increased somatotropin (growth hormone) release. Cholera toxin (3mug/ml for 4h) increased pituitary cyclic AMP concentrations 4-5-fold, but had no effect on prolactin secretion. The inhibition of prolactin secretion by dopamine was unaffected by cholera toxin, despite the fact that dopamine had no effect on the raised pituitary cyclic AMP concentration caused by this factor. Dopamine had no significant effect on either basal or stimulated somatotropin secretion under any of the conditions tested. We conclude that the inhibitory effects of dopamine on prolactin secretion are probably not mediated by lowering of cyclic AMP concentration, although modulation of the concentration of this nucleotide in some other circumstances may alter the secretion of the hormone.

1-Methyl-3-isobutylxanthine↗
PubMed2002

MRI of the liver and the pituitary gland in patients with beta-thalassemia major: does hepatic siderosis predict pituitary iron deposition?

Our objective was to study, in thalassemic patients, if hepatic siderosis evaluated by MRI could predict the pituitary iron overload. In 36 thalassemic patients (age range 6-44 years, mean age 21.7 years) the liver/fat ratio (L/F), the pituitary/fat ratio (P/F), the liver and pituitary T2 relaxation times were evaluated, by using a multiecho spin-echo sequence. Serum ferritin levels were measured and an extensive endocrine evaluation was performed. The L/F, the P/F and pituitary T2 showed a good correlation with serum ferritin ( r=-0.55, r=-0.55 and r=-0.53, respectively; p<0.01). Liver T2 did not show significant correlation with serum ferritin. The variability of L/F explained only the 10.8% of the variability of pituitary T2 and of the P/F. When ferritin was added to the model it predicted only the 26.85% and the 30.8% of the variability of pituitary T2 and of the P/F, respectively. The P/F and pituitary T2 were lower in patients with hypogonadotropic hypogonadism (group 1) compared with those without pituitary dysfunction (group 2). No significant differences of L/F were found between the two groups. Hepatic iron overload evaluated by MR is a poor predictor of pituitary siderosis. The MR studies of the pituitary gland might be necessary to evaluate the pituitary iron overload.

Adolescent↗
PubMed1986

Synthesis and storage of prolactin in the pituitary gland of bullfrog tadpoles during metamorphosis.

Changes in prolactin (PRL) levels and PRL-producing activities in the pituitary gland of tadpoles during metamorphosis were studied. PRL concentration in the pituitary gland as measured by a homologous radioimmunoassay was relatively low during pre- and prometamorphosis and early climax (2.5-3.5 micrograms/100 micrograms protein). PRL levels increased thereafter and reached maximum (7.3 micrograms/100 micrograms protein) at late climax (stage 24). It was also demonstrated that the pituitary cells which immunologically reacted with the antiserum to bullfrog PRL increased in number as metamorphosis proceeded. Measurement of incorporation of [3H]leucine into pituitary PRL in vitro revealed that elevation of PRL synthesis took place in the tadpoles which had reached climax. Radioimmunoassay and bioassay of PRL in the pituitary glands of adult frogs and tadpoles indicated that there was no difference in immunological and biological properties between adults and larvae.

Animals↗
PubMed1995

Cloning and expression of a myc family member from the pituitary gland of the Rainbow trout, Oncorhynchus mykiss.

A myc gene cloned from a Rainbow trout pituitary gland cDNA library is described. This clone (Tmyc2) shows extensive homology to Rainbow trout C-myc, which is expressed in the liver. Tmyc2 does not appear in the liver but is expressed in the pituitary gland (1.9 kb transcript), brain (2.0 kb transcript) and, at very low levels, in the heart (2.0 kb transcript). Tmyc2 contains three highly modified areas within the coding sequence, one of which shows an extensive loss of acidic residues that is uncommon in C-myc family members and may be important in determining the function of Tmyc2 in the pituitary gland and brain.

Amino Acid Sequence↗
PubMed1993

Isolation and characterization of two distinct gonadotropins, GTHI and GTHII, from bonito (Katsuwonus plelamis) pituitary glands.

Two distinct glycoproteins homologous to chum salmon GTHI and GTHII were isolated from the pituitary glands of a marine fish, the bonito (Katsuwonus plelamis), and characterized by amino acid sequence analysis in order to obtain additional evidence for duality of teleost GTHs. Glycoproteins were extracted from the pituitary glands, and intact GTHI and GTHII, consisting of two distinct subunits, were purified by ion-exchange chromatography on DEAE-cellulose, rpHPLC on Asahipak C4P-50 in alkaline buffer, and gel filtration on Superdex 75. The association of the subunits was stable in GTHI (39 kD) and unstable in GTHII (30 kD) in acidic conditions. Immunoblotting revealed that antisera against beta subunits of chum salmon GTHs reacted with GTHII, but not with GTHI. In addition, none of the GTHs was stained with antiserum against human TSH beta. Sequence analysis demonstrated that bonito GTHI beta is homologous to salmon GTHI beta with 43% sequence identity, and bonito GTHII beta is homologous to salmon GTHII beta with 67% identity. Sequence identity between bonito GTHI beta and GTHII beta was only 28%. Thus, it is evident that the bonito pituitary gland produces two chemically distinct gonadotropins homologous to chum salmon GTHs.

Amino Acid Sequence↗
PubMed1988

Dome formation of keratin-containing agranular cells from rat anterior pituitary gland in vitro.

A certain kind of cell in the pituitary gland exhibited immunoreactive keratin and dome formations in vitro. We obtained epithelial cells, which were able to subculture, from the outgrowth of anterior pituitary organ cultures. These cells lacked hormone secretory granules and exhibited immunoreactive keratin. Furthermore, they produced dome formations or cystic structures in monolayer culture and under three-dimensional culture condition using type I collagen gel. Dome formation was stimulated by dibutyryl cyclic AMP (dbcAMP, 10(-3) to 10(-5) M). Their responsiveness to dbcAMP is similar to that of several other epithelial cells that possess transport functions in vivo and in vitro. Although the origin of our cultured cells is unknown, these cells formed dome formations that possessed transport function and were related to cystic structures in the pituitary gland in vivo.

Animals↗
PubMed1999

In vitro release of isoforms of prolactin from pituitary glands of turkey hens at different physiological stages.

To study the in vitro release of PRL isoforms, anterior pituitary glands from medium white turkeys at various physiological stages were stimulated by cVIP in a perifusion system. Pituitaries were cut into hemi-pituitaries after collection and placed into separate perifusion chambers. Medium (M199) was continuously perifused through the system and pituitaries were stimulated with cVIP (10(-7) M). Total PRL content was monitored by RIA and, the ratio of immunoreactive PRL isoforms in the perifusate was estimated by Western blotting. After exposure to X-ray film for autoradiography, the relative intensity of the bands was analyzed by densitometry. All the perifused pituitaries responded to cVIP stimulation by increasing the release of PRL. Two immunoreactive bands with relative molecular weights of 24 and 27 kDa were detected by Western blotting. The immunoreactive band corresponding to the glycosylated isoforms of PRL (27 kDa) was predominant in samples from egg-laying and incubating hens and the band corresponding to the nonglycosylated isoform (24 kDa) was predominant in samples from out-of-lay and molting stages. No changes in the ratio of isoform released were detected during cVIP stimulation. Our data clearly show that glycosylated and nonglycosylated PRL isoforms are released by the pituitary gland in vitro in the same relative proportion that was previously observed in pituitary extracts and thus are likely to reflect the secreted forms of PRL in the blood during various physiological stages. In addition, the PRL-releasing activity of VIP does not affect the ratio of isoforms secreted by the pituitary gland in vitro.

Animals↗
PubMed1992

Expression of c-myc and c-fos protooncogenes in the anterior pituitary gland of the rat. Effect of estrogen.

Thymidine incorporation into the DNA of the anterior pituitary gland is stimulated by estrogen. We studied the relationship between this effect and expression of the protooncogenes c-myc and c-fos. Within one hour after estrogen administration, the level of c-myc and c-fos mRNA increased in the anterior pituitary gland and remained high throughout the experimental period (16 to 22 hrs). Transcription of the prolactin gene, one of the targets of estrogen action, was stimulated at the same time intervals. There were no modifications in the growth hormone mRNA level. Thus, estrogen induced the expression of c-myc and c-fos in the anterior pituitary gland in an early period.

Animals↗
PubMed2006

Gene expression profiling during cellular differentiation in the embryonic pituitary gland using cDNA microarrays.

The anterior pituitary is comprised of five major hormone-secreting cell types that differentiate during embryonic development in a temporally distinct manner. Microarrays containing 5,128 unique cDNAs expressed in the chicken neuroendocrine system were produced and used to identify genes with potential involvement in the onset of thyroid-stimulating hormone beta-subunit (TSHbeta), growth hormone (GH), and prolactin (PRL) mRNA during embryonic development. We identified 352 cDNAs that were differentially expressed (P < or = 0.05) on embryonic day 10 (e10), e12, e14, or e17, the period of thyrotroph, somatotroph, and lactotroph differentiation. Self-organizing maps were used to identify genes that may function to initiate hormone gene transcription. Consistent with cellular ontogeny, TSHbeta mRNA increased steadily between e10 and e17, GH mRNA increased between e12 and e17, and PRL mRNA did not increase until e17. Expression of 141 genes increased in a manner similar to TSHbeta mRNA, and 64 genes decreased between e10 and e17. Although genes with these expression profiles are likely involved in development of the pituitary gland as a whole, some of these could be specifically associated with thyrotroph differentiation. Similarly, the expression profiles of 69 and 61 genes indicate a potential involvement in the induction of GH and PRL mRNA, respectively. Quantitative real-time RT-PCR was used to confirm microarray results for 31 genes. This is the first study to evaluate changes in anterior pituitary gene expression during embryonic development of any species using microarrays, and numerous transcription factors and signaling molecules not previously implicated in pituitary development were identified.

Animals↗
PubMed1983

Calmodulin and Ca2+- and calmodulin-dependent protein kinase in rat anterior pituitary gland.

Calmodulin and Ca2+- and calmodulin-dependent protein kinase were identified in the rat anterior pituitary gland. The concentration of calmodulin was 1.18 +/- 0.11 microgram/mg protein (n = 7) in the cytosol fraction. The calmodulin of the anterior pituitary gland co-migrated with brain calmodulin on sodium dodecyl sulfate polyacrylamide gel electrophoresis. The Ka value of the partially purified enzyme for Ca2+ was 3.3 microM in the presence of 0.30 microM calmodulin. Trifluoperazine and chlorpromazine, calmodulin-interacting agents, inhibited enzyme activity, with Ki values of 1.3 and 2.6 X 10(-5) M, respectively. The enzyme was resolved into two peaks of activity, with sedimentation coefficients of 5.5 S and 16.5 S, by sucrose density gradient centrifugation. At least nine proteins were phosphorylated by the enzyme in a Ca2+- and calmodulin-dependent manner. In light of these results, the possibility that calmodulin and the calmodulin-activatable protein kinase system are involved in the mediation of the Ca2+ effect on hormone release from the anterior pituitary gland must be given consideration.

Animals↗
PubMed1995

Cytochrome P450 CYP3A5 in the human anterior pituitary gland.

The cytochromes P450 are a key group of enzymes involved in the metabolism of xenobiotics and several biologically active endogenous compounds. The expression of CYP3A5 has been identified by reverse transcriptase-polymerase chain reaction in human pituitary gland and shown by immunohistochemistry to be localized to growth hormone containing cells of the anterior pituitary gland. This is the first direct identification of an individual P450 subfamily in the pituitary gland and the presence of CYP3A in the pituitary gland may play a role in regulating growth hormone secretion.

Aged↗