Growth hormone-releasing hormone and somatostatin in normal and tumoral human pituitaries

Benlot, C.; Pagésy, Patrick; Peillon, F; Joubert-Bression, D.

doi:10.1016/0196-9781(91)90042-n

Cited by 12 publications

(5 citation statements)

References 17 publications

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“…Recently, the silent corticotroph adenoma has been reported also to contain a large amount of POMC mRNA without secreting biologically active ACTH (Lloyd et al, 1990). An altered processing of prosomatostatin has been proposed in GH producing adenomas (Benlot et al, 1991;Levy et al, 1993). Thus, we have investigated the expression of PC2 and PC3 mRNA in ACTH and GH producing adenomas in the present study.…”

Section: Discussionmentioning

confidence: 94%

Expression patterns of messenger ribonucleic acids encoding prohormone convertases (PC2 and PC3) in human pituitary adenomas

Hashimoto

Koga

Kouhara

et al. 1994

Clinical Endocrinology

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Section: Discussionmentioning

confidence: 94%

Expression patterns of messenger ribonucleic acids encoding prohormone convertases (PC2 and PC3) in human pituitary adenomas

Hashimoto

Koga

Kouhara

et al. 1994

Clinical Endocrinology

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“…GHRH and its mRNA have been found in GHsecreting adenomas (Joubert et al, 1989;Levy and Lightman, 1992;Wakabayashi et al, 1992) and high levels appear to correlate with high circulating GH, suggesting a paracrine role in release of GH by the tumour (Benlot et al, 1991). Since GHRH has been shown to be mitogenic for somatotrophs (Billestrup et al, 1986) it could also effect autocrine growth control.…”

Section: Novel Peptidesmentioning

confidence: 94%

“…However, studies on the human gland also indicate such complexity, although species differences may occur in the cell-specific expression of particular peptides. Hypothalamic peptides have been identified, including growth hormone-releasing hormone (GHRH) and somatostatin (Benlot et al, 1991;Joubert [Bression] et al, 1989;, TRH (Le Dafniet et al, 1990) and gonadotrophin-releasing hormone (GnRH) (Miller et al, 1996). These may act locally in the fine tuning of GH, TSH, and gonadotrophin release.…”

Section: Novel Peptidesmentioning

confidence: 98%

Gene expression in pituitary adenomas: New insights

McNicol

1997

Microsc. Res. Tech.

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“…Studies by Hashimoto et al (1994) have demonstrated altered or insufficient prohormone processing in some human pituitary adenomas. Altered processing of the growth-inhibitory prosomatostatin has been observed in GH-producing adenomas (Benlot et al 1991). Lloyd et al (1990) have shown that some silent ACTHsecreting adenomas contain abundant POMC mRNA without secreting biologically active ACTH.…”

mentioning

confidence: 99%

Immunohistochemical Localization of Carboxypeptidases D, E, and Z in Pituitary Adenomas and Normal Human Pituitary

Fan

Olson

Blevins

et al. 2002

J Histochem Cytochem.

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S U M M A R YCarboxypeptidases may play important role(s) in prohormone processing in normal and neoplastic adenohypophyseal cells of the pituitary. We have recently demonstrated carboxypeptidase E (CPE) and carboxypeptidase Z (CPZ) in the majority of adenohypophyseal cells with carboxypeptidase D (CPD) immunoreactivity largely confined to adrenocorticotrophs. This study evaluated the expression patterns of CPE, CPD, and CPZ immunoreactivity in 48 pituitary adenomas. Our immunohistochemistry demonstrated extensive intracytoplasmic immunoreactivity for CPE, CPD, and CPZ in adrenocorticotrophic hormone (ACTH)-producing adrenocorticotroph cells, prolactin-producing lactotroph cells, and growth hormone (GH)-producing somatotroph cell adenomas, all of which require carboxypeptide processing of prohormones to produce active endocrine hormones. In contrast to the restricted expression in the normal adenohypophysis, CPD appeared to be widespread in the majority of adenomas, suggesting that CPD levels are increased in adenomas. In luteinizing hormone/follicle-stimulating hormone (LH/FSH)-producing gonadotroph adenomas, which do not require carboxypeptidases to produce gonadotropins, only CPZ immunostaining was demonstrated. In null-cell adenomas, CPE immunoreactivity was detected in the majority of tumors, but CPD and CPZ were identified only in a minority of cases. CPE in these cells may process other peptides critical for pituitary cell function, such as chromogranin A or B. These findings suggest that CPs participate in the functioning of pituitary adenomas.

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Growth hormone-releasing hormone and somatostatin in normal and tumoral human pituitaries

Cited by 12 publications

References 17 publications

Expression patterns of messenger ribonucleic acids encoding prohormone convertases (PC2 and PC3) in human pituitary adenomas

Expression patterns of messenger ribonucleic acids encoding prohormone convertases (PC2 and PC3) in human pituitary adenomas

Gene expression in pituitary adenomas: New insights

Immunohistochemical Localization of Carboxypeptidases D, E, and Z in Pituitary Adenomas and Normal Human Pituitary

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