scholarly journals TGFBR3L—An Uncharacterised Pituitary Specific Membrane Protein Detected in the Gonadotroph Cells in Non-Neoplastic and Tumour Tissue

Cancers ◽  
2020 ◽  
Vol 13 (1) ◽  
pp. 114
Author(s):  
Evelina Sjöstedt ◽  
Anders J. Kolnes ◽  
Nicoleta C. Olarescu ◽  
Nicholas Mitsios ◽  
Feria Hikmet ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Pituitary Gland ◽  
Anterior Pituitary ◽  
Neuroendocrine Tumours ◽  
Transforming Growth Factor ◽  
Somatostatin Receptors ◽  
Cell Lineage ◽  
Anterior Pituitary Gland ◽  
Specific Membrane ◽  
E Cadherin

Here, we report the investigation of transforming growth factor beta-receptor 3 like (TGFBR3L), an uncharacterised pituitary specific membrane protein, in non-neoplastic anterior pituitary gland and pituitary neuroendocrine tumours. A polyclonal antibody produced within the Human Protein Atlas project (HPA074356) was used for TGFBR3L staining and combined with SF1 and FSH for a 3-plex fluorescent protocol, providing more details about the cell lineage specificity of TGFBR3L expression. A cohort of 230 pituitary neuroendocrine tumours were analysed. In a subgroup of previously characterised gonadotroph tumours, correlation with expression of FSH/LH, E-cadherin, oestrogen (ER) and somatostatin receptors (SSTR) was explored. TGFBR3L showed membranous immunolabeling and was found to be gonadotroph cell lineage-specific, verified by co-expression with SF1 and FSH/LH staining in both tumour and non-neoplastic anterior pituitary tissues. TGFBR3L immunoreactivity was observed in gonadotroph tumours only and demonstrated intra-tumour heterogeneity with a perivascular location. TGFBR3L immunostaining correlated positively to both FSH (R = 0.290) and LH (R = 0.390) immunostaining, and SSTR3 (R = 0.315). TGFBR3L correlated inversely to membranous E-cadherin staining (R = −0.351) and oestrogen receptor β mRNA (R = −0.274). In conclusion, TGFBR3L is a novel pituitary gland specific protein, located in the membrane of gonadotroph cells in non-neoplastic anterior pituitary gland and in a subset of gonadotroph pituitary tumours.

Human pituitary somatotropes express transforming growth factor-α and its receptor

1994 ◽  
Vol 141 (3) ◽  
pp. 547-554 ◽  
Author(s):  
E L Finley ◽  
J S King ◽  
J S Ramsdell
Keyword(s):  
Growth Factor ◽  
Pituitary Gland ◽  
Anterior Pituitary ◽  
Transforming Growth Factor ◽  
Anterior Pituitary Gland ◽  
Human Pituitary ◽  
Transforming Growth Factor Α ◽  
Human Pituitary Gland ◽  
Pituitary Glands ◽  
Factor Α

Abstract Transforming growth factor-α (TGF-α) is a growth-regulatory peptide produced by a variety of transformed and non-transformed cells. Among non-transformed cells, TGF-α has been identified in the prolactin (PRL)- and GH-secreting cells of the bovine anterior pituitary gland. In this report, we have examined the expression of TGF-α in human anterior pituitary glands by Western analysis and immunohistochemistry. For the Western analysis, human pituitary glands were extracted in acid/ethanol, an acetic acid-soluble fraction was ether-precipitated and dialysed, and TGF-α was partially purified by C18 chromatography. TGF-α was then identified by immunostaining of Western transfers. Anterior pituitary extracts exhibited a major band(s) migrating at 19 kDa that was immunoreactive with a monoclonal antibody directed against the mature TGF-α. However, no evidence of the fully processed 6 kDa TGF-α was observed. We next identified TGF-α by immunohistochemistry. Using both monoclonal and polyclonal antibodies, specific immunoreactivity was identified in a population of secretory cells in the anterior pituitary gland. Using antibodies specific for the COOH and NH3 terminals of the TGF-α precursor, a comparable number of TGF-α-positive cells were found to contain TGF-α precursor sequences. These results indicate that the 19 kDa form of TGF-α expressed in the human pituitary gland may exist as the transmembrane form. We next sought to determine which cells express TGF-α in a human male pituitary gland. On frontal sections, TGF-α-immunopositive cells were evenly distributed in a manner and number indistinguishable from GH-immunopositive cells. By contrast, PRL-immunopositive cells in midfrontal sections were largely restricted to the lateral wings and extended dorsally to the neural lobe. TGF-α was positively co-localized to GH-immunopositive cells but not in PRL-immunopositive cells by immunostaining of consecutive sections. TGF-α-immunopositive cells were also immunopositive for the epidermal growth factor receptor, indicating that TGF-α has the capacity for autocrine action in the human pituitary gland. These results indicate that TGF-α is expressed in the human anterior pituitary gland and it is not proteolytically processed into the mature 6 kDa form. In addition, immunohistochemistry of an adult male human pituitary gland indicates that TGF-α is expressed in somatotropes and has the capacity for autocrine action. Journal of Endocrinology (1994) 141, 547–554

Effects of estrogens on the characteristics of [3H]spiroperidol and [3H]RU24213 binding in rat anterior pituitary gland and brain

1979 ◽  
Vol 16 (2) ◽  
pp. 99-112 ◽  
Author(s):  
Thérèse Di Paolo ◽  
Réjean Carmichael ◽  
Fernand Labrie ◽  
Jean-Pierre Raynaud
Keyword(s):  
Pituitary Gland ◽  
Anterior Pituitary ◽  
Anterior Pituitary Gland

Effect of hypothalamic neuropeptides on corticotrophin release from quarters of rat anterior pituitary gland in vitro

1984 ◽  
Vol 100 (2) ◽  
pp. 219-226 ◽  
Author(s):  
S. A. Nicholson ◽  
T. E. Adrian ◽  
B. Gillham ◽  
M. T. Jones ◽  
S. R. Bloom
Keyword(s):  
Pituitary Gland ◽  
Anterior Pituitary ◽  
Low Dose ◽  
Physiological Role ◽  
Anterior Pituitary Gland ◽  
High Concentration ◽  
Response Curves ◽  
Corticotrophin Releasing Factor ◽  
Basal Release

ABSTRACT The effect of six hypothalamic peptides on the basal release of ACTH and that induced by arginine vasopressin (AVP) or by ovine corticotrophin releasing factor (oCRF) from fragments of the rat anterior pituitary gland incubated in vitro was investigated. Dose–response curves to AVP and to oCRF were obtained, and the response to a low dose of oCRF was potentiated by a low dose of AVP. Basal release of ACTH was not affected by any of the peptides in concentrations in the range 10−12 to 10−6 mol/l, and only substance P (SP) and somatostatin (SRIF) inhibited significantly the response to oCRF in a dose-related manner. The responses to a range of doses of oCRF or AVP were reduced by 10−8 and 10 − 6 mol SP or SRIF/1, and to a greater extent by the higher dose. Except in the case of 10−6 mol SRIF/1 on the response to AVP, the response was not further diminished by preincubation of the tissue with the peptide before the stimulating agent was added. The inhibition of the responses to AVP or oCRF by 10−9 mol SP/1 was not potentiated by its combination with either 5 × 10−10 or 10−8 mol SRIF/1; the inhibitory effects were merely additive. The results suggest that although SRIF and SP are able to modulate the release of ACTH from the anterior pituitary gland, they do so only at a high concentration. In the case of SRIF these concentrations are several orders of magnitude higher than those reported to be present in the hypophysial portal blood and therefore a physiological role for this peptide in the control of ACTH secretion is unlikely. J. Endocr. (1984) 100, 219–226

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