Pituitary Disorders

Author(s):  
Pankaj Shah

Hypopituitarism usually results from a deficiency of anterior pituitary hormones or, rarely, from tissue resistance to these hormones. Deficiency may be from primary pituitary disease, pituitary stalk disorders, hypothalamic disease, or an extrasellar disorder impinging on, or infiltrating, the hypothalamic-pituitary unit. Primary pituitary disease results from the loss of anterior pituitary cells and may be congenital or acquired. Common causes are pituitary tumors and their surgical or radiotherapeutic ablation. Infrequent causes include pituitary infarction (eg, postpartum pituitary necrosis, also known as Sheehan syndrome), pituitary apoplexy, lymphocytic hypophysitis, infiltrative diseases (eg, hemochromatosis), and metastatic disease (eg, from breast or lung).

2006 ◽  
Vol 188 (3) ◽  
pp. 417-423 ◽  
Author(s):  
Masafumi Amano ◽  
Shunsuke Moriyama ◽  
Masayuki Iigo ◽  
Shoji Kitamura ◽  
Noriko Amiya ◽  
...  

We recently identified a cDNA encoding three novel fish hypothalamic neuropeptides, having LPXRF-NH2 from the goldfish brain. In this study, to clarify the physiological functions of these three LPXRFamide peptides (gfLPXRFa-1, -2, and -3), we analysed the localisation and hypophysiotrophic activity of these peptides using sockeye salmon, Oncorhynchus nerka, in which immunoassay systems for several anterior pituitary hormones have been developed. gfLPXRFa-immunoreactive cell bodies were detected in the nucleus posterioris periventricularis of the hypothalamus and immunoreactive fibres were distributed in various brain regions and the pituitary. We also detected gfLPXRFa-immunoreactivity in the pituitary by competitive enzyme-linked immunosorbent assay combined with reversed-phase HPLC. These three gfLPXRFamide peptides stimulated the release of FSH, LH and GH, but did not affect the release of prolactin (PRL) and somatolactin (SL) from cultured pituitary cells. These results suggest that novel fish hypothalamic LPXR-Famide peptides exist in the brain and pituitary of sockeye salmon and stimulate the release of gonadotrophins and GH from the pituitary.


Endocrinology ◽  
2003 ◽  
Vol 144 (2) ◽  
pp. 732-740 ◽  
Author(s):  
Louise M. Bilezikjian ◽  
Angela M. O. Leal ◽  
Amy L. Blount ◽  
Anne Z. Corrigan ◽  
Andrew V. Turnbull ◽  
...  

Folliculostellate cells of the anterior pituitary are postulated to be an important source of factors, such as follistatin, that regulate pituitary function by intercellular communication. To gain further insight into the function of this cell type, folliculostellate cells were enriched from cultured rat anterior pituitary cells, and an immortalized cell line designated FS/D1h was established and characterized. These FS/D1h cells express S100 immunoreactivity and produce IL-6 but not pituitary hormones such as GH, ACTH, FSH, and LH. Importantly, FS/D1h cells express large amounts of follistatin mRNA and secrete the protein, as quantified indirectly by the amount of [125I]activin A immunoprecipitated with a follistatin antiserum. The FS/D1h cells also express α, βA, and βB inhibin/activin subunit mRNAs, but whether they produce the corresponding activins and inhibins has not been determined. The response of FS/D1h cells to agents thought to modulate folliculostellate cell function was evaluated. IL-1β (0.005–5 nm) stimulated the secretion of follistatin and increased mRNA expression. In parallel, IL-6 secretion was stimulated. Dexamethasone, pituitary adenylate cyclase-activating polypeptide(1–27), and lipopolysaccharide but not testosterone, 12-O-tetradecanoylphorbol-13-acetate, or forskolin also increased follistatin secretion. Surprisingly, activin had no effect on follistatin mRNA levels, despite the fact that FS/D1h cells express ActRII, ActRIIB, and ALK-4 (ActRIB). Activin, on the other hand, induced Smad7 mRNA accumulation and exerted an antiproliferative effect on FS/D1h cells. Altogether, these observations support the possibility that follistatin originating from folliculostellate cells participates in mediating the effects of IL-1β, glucocorticoids, and other agents on the response of pituitary cells to activins.


1996 ◽  
Vol 148 (1) ◽  
pp. 33-41 ◽  
Author(s):  
H Ikawa ◽  
K Yamamoto ◽  
Y Takahashi ◽  
N Ueda ◽  
Y Hayashi ◽  
...  

Abstract Arachidonate 12-lipoxygenase, which oxygenates positions 12 and 13 of arachidonic and linoleic acids, is present in porcine anterior pituitary cells. Colocalization of the 12-lipoxygenase with various pituitary hormones was examined by immunohistochemical double-staining using antibodies against 12-lipoxygenase and various anterior pituitary hormones. Under light microscopy, approximately 7% of the cells producing luteinizing hormone (LH) and follicle-stimulating hormone (FSH) were positive for 12-lipoxygenase, whereas the enzyme was detected in less than 2% of the cells producing thyrotrophin, prolactin, growth hormone (GH), and adrenocorticotrophin. In an attempt to examine the participation of 12-lipoxygenase metabolites in pituitary hormone release, we incubated the primary culture of porcine anterior pituitary cells with 12-hydroperoxy-arachidonic acid or 13-hydroperoxy-linoleic acid. Significant stimulation of LH and FSH release by these hydroperoxides was observed at 10 μm in a time-dependent manner. At doses around 10 μm these compounds produced responses of similar magnitude to 1 nm gonadotrophin-releasing hormone (GnRH), but higher concentrations (30 μm) of the compounds were required for GH release. In contrast, 12-hydroxy-arachidonic and 13-hydroxy-linoleic acids were almost ineffective. Furthermore, the gonadotrophin release by 1 nm GnRH was inhibited by nordihydroguaiaretic acid (a lipoxygenase inhibitor) with an IC50 of about 5 μm. Thus, the hydroperoxy (but not hydroxy) products of 12-lipoxygenase may be involved in the release of pituitary hormones especially LH and FSH. Journal of Endocrinology (1996) 148, 33–41


Endocrinology ◽  
2012 ◽  
Vol 153 (11) ◽  
pp. 5452-5466 ◽  
Author(s):  
Alex Reichenbach ◽  
Frederik J. Steyn ◽  
Mark W. Sleeman ◽  
Zane B. Andrews

Abstract Ghrelin is the endogenous ligand for the GH secretagogue receptor (GHSR) and robustly stimulates GH release from the anterior pituitary gland. Ghrelin also regulates the secretion of anterior pituitary hormones including TSH, LH, prolactin (PRL), and ACTH. However, the relative contribution of a direct action at the GHSR in the anterior pituitary gland vs. an indirect action at the GHSR in the hypothalamus remains undefined. We used a novel GHSR-enhanced green fluorescent protein (eGFP) reporter mouse to quantify GHSR coexpression with GH, TSH, LH, PRL, and ACTH anterior pituitary cells in males vs. females and in chow-fed or calorie-restricted (CR) mice. GHSR-eGFP-expressing cells were only observed in anterior pituitary. The number of GHSR-eGFP-expressing cells was higher in male compared with females, and CR did not affect the GHSR-eGFP cell number. Double staining revealed 77% of somatotrophs expressed GHSR-eGFP in both males and females. Nineteen percent and 12.6% of corticotrophs, 21% and 9% of lactotrophs, 18% and 19% of gonadotrophs, and 3% and 9% of males and females, respectively, expressed GHSR-eGFP. CR increased the number of TSH cells, but suppressed the number of lactotrophs and gonadotrophs, expressing GHSR-eGFP compared with controls. These studies support a robust stimulatory action of ghrelin via the GHSR on GH secretion and identify a previously unknown sexual dimorphism in the GHSR expression in the anterior pituitary. CR affects GHSR-eGFP expression on lactotrophs, gonadotrophs, and thyrotrophs, which may mediate reproductive function and energy metabolism during periods of negative energy balance. The low to moderate expression of GHSR-eGFP suggests that ghrelin plays a minor direct role on remaining anterior pituitary cells.


2008 ◽  
Vol 42 (2) ◽  
pp. 171-183 ◽  
Author(s):  
Laura E Ellestad ◽  
Stefanie A Malkiewicz ◽  
H David Guthrie ◽  
Glenn R Welch ◽  
Tom E Porter

The expression profile of glucocorticoid-induced leucine zipper (GILZ) in the anterior pituitary during the second half of embryonic development in the chick is consistent with in vivo regulation by circulating corticosteroids. However, nothing else has been reported about the presence of GILZ in the neuroendocrine system. We sought to characterize expression and regulation of GILZ in the chicken embryonic pituitary gland and determine the effect of GILZ overexpression on anterior pituitary hormone levels. Pituitary GILZ mRNA levels increased during embryogenesis to a maximum on the day of hatch, and decreased through the first week after hatch. GILZ expression was rapidly upregulated by corticosterone in embryonic pituitary cells. To determine whether GILZ regulates hormone gene expression in the developing anterior pituitary, we overexpressed GILZ in embryonic pituitary cells and measured mRNA for the major pituitary hormones. Exogenous GILZ increased prolactin mRNA above basal levels, but not as high as that in corticosterone-treated cells, indicating that GILZ may play a small role in lactotroph differentiation. The largest effect we observed was a twofold increase in FSH β subunit in cells transfected with GILZ but not treated with corticosterone, suggesting that GILZ may positively regulate gonadotroph development in a manner not involving glucocorticoids. In conclusion, this is the first report to characterize avian GILZ and examine its regulation in the developing neuroendocrine system. We have shown that GILZ is upregulated by glucocorticoids in the embryonic pituitary gland and may regulate expression of several pituitary hormones.


1995 ◽  
Vol 43 (7) ◽  
pp. 657-664 ◽  
Author(s):  
D Tilemans ◽  
V V Vijver ◽  
G Verhoeven ◽  
C Denef

Using a specific anti-rat transferrin (Tf) antiserum, Tf-like immunoreactivity (Tf-lir) was detected by immunostaining in intact rat pituitaries and in reaggregated pituitary cells cultured in serum-free medium. Tf-lir cells were present in the anterior pituitary (AP), and in the intermediate (IL) and neural lobes (NL). In the AP, Tf-lir cells were oval or polygonal. An unusual topographical distribution was found. Tf-lir cells mainly occurred as dense clusters in the lateral wings. In the central part of the AP, Tf-lir was found in flattened perisinusoidal cells. Double immunostaining for Tf and the different pituitary hormones showed that Tf-lir co-localized with some gonadotrophs and somatotrophs (7% and 3% of Tf-lir cells, respectively, in typical sections). No co-localization was seen with PRL, ACTH, TSH, or alpha-MSH. The distribution of Tf-lir cells and their cell shape completely differed from that of S-100-positive cells in the AP. In the IL, clusters of large stellate Tf-lir cells were found. Again, their distribution completely differed from S-100-positive cells. In the NL, diffuse staining was found. Double immunostaining of paraffin-embedded sections of reaggregate cell cultures of the AP did not reveal any co-localization of Tf-lir with ACTH, alpha-MSH, LH, FSH, TSH, GH, or PRL. In aggregates consisting of NL + IL cells, Tf-lir was located in clusters: no co-localization with ACTH or alpha-MSH could be demonstrated. Reaggregate cell cultures of AP and NL + IL secreted Tf-lir as measured by radioimmunoassay, at least during 21 days of culture. After metabolic labeling with [35S]-methionine and immunoprecipitation of [35S]-methionine-labeled material present in the culture medium of both AP and NL + IL aggregates with anti-Tf antiserum, a 35S-labeled substance was found, which on SDS-PAGE showed an apparent M(r) of approximately 78 KD, corresponding to the M(r) of rat Tf. The present data show that a specific population of cells of rat anterior pituitary is capable of synthesizing, storing, and secreting transferrin or a substance closely related to it. Cells different from melanotrophs and S-100 cells in the IL, as well as pituicytes in the NL, also appear to produce this material. We suggest that transferrin or a transferrin-like substance may have a local role in the transport of iron or other metals or may play a role as growth factor in the three lobes of the pituitary gland.


1995 ◽  
Vol 145 (2) ◽  
pp. 333-341 ◽  
Author(s):  
K O Akinsanya ◽  
H Jamal ◽  
M A Ghatei ◽  
S R Bloom

Abstract The novel peptide, pyroglutamyl-glutamyl-proline amide (pGlu-Glu-ProNH2; EEP), which has structural and immunological similarities to TRH (pGlu-His-ProNH2) has recently been shown to contribute to total TRH-like immunoreactivity (t-TRH-LI) detected in the rabbit prostate and rat and porcine anterior pituitary. In this study, the effects of dexamethasone (DEX) on rat pituitary TRH-like peptide levels in the rat were determined. TRH-like immunoreactivity (TRH-LI) was separated by ion exchange chromatography and detected by TRH RIA. Anion exchange chromatographic analysis suggested that EEP-like immunoreactivity (EEP-LI) accounted for 15·0 ± 1·2 pmol t-TRH-LI/g (70·4 ± 3·9%) in the control anterior pituitary with the remaining t-TRH-LI being due to TRH-LI. Following DEX treatment pituitary EEP-LI and TRH-LI increased by 200% and 400% (P<0·001) respectively, constituting a 2·5-fold increase in t-TRH-LI in the pituitary. TRH-LI now accounted for 45·7±5·3% of t-TRH-LI compared with 29·6 ±4·1% in the controls. TRH-LI, but not EEP-LI, was detected in the hypothalamus and posterior pituitary, suggesting that EEP-LI is synthesised within the anterior pituitary. DEX also caused a 2·6-fold rise (P<0·001) in t-TRH-LI in dispersed, cultured anterior pituitary cells. Chromatographic analysis of cultured pituitary cell extracts revealed that the majority of t-TRH-LI (>98%) was due to TRH-LI. A possible explanation for the change in EEP-LI and TRH-LI levels in the in vivo and in vitro pituitary samples is that hypothalamic influences are necessary for the continued production of EEP-LI and are not present in vitro. Alternatively, the dissociation of the cell–cell interactions and/or the accumulation of cell products, particularly pituitary hormones in vitro, may result in a loss of the in vivo paracrine influences or the introduction of factors which inhibit EEP-LI and stimulate TRH-LI. Journal of Endocrinology (1995) 145, 333–341


Author(s):  
S. Jalalah ◽  
K. Kovacs ◽  
E. Horvath

Lactotrophs, as many other endocrine cells, change their morphology in response to factors influencing their secretory activity. Secretion of prolactin (PRL) from lactotrophs, like that of other anterior pituitary hormones, is under the control of the hypothalamus. Unlike most anterior pituitary hormones, PRL has no apparent target gland which could modulate the endocrine activity of lactotrophs. It is generally agreed that PRL regulates its own release from lactotrophs via the short loop negative feedback mechanism exerted at the level of the hypothalamus or the pituitary. Accordingly, ultrastructural morphology of lactotrophs is not constant; it is changing in response to high PRL levels showing signs of suppressed hormone synthesis and secretion.By transmission electron microscopy and morphometry, we have studied the morphology of lactotrophs in nontumorous (NT) portions of 7 human pituitaries containing PRL-secreting adenoma; these lactotrophs were exposed to abnormally high PRL levels.


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