Somatostatin-28- and somatostatin- 14-like immunoreactivities in the rat pituitary gland

Mesguich, Patrick; Benoit, Robert; Dubois, Paul; Morel, Gérard

doi:10.1007/bf00214385

Cited by 19 publications

(6 citation statements)

References 47 publications

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“…These results, which clearly show the restricted pres ence of rGH-RBP expression in discrete adult rat pitu itary cells, were obtained using nonradioactive in situ hybridization and immunocytology performed on ultrathin frozen sections; these methods have been shown to be highly sensitive [21,23,24,26,27], The controls carried out in our study indicated the specificity of the in situ hybridization for the detection of GH-RBP mRNA trans cripts and of immunocytology for the detection of the GH-RBP protein. In addition, visualization of the intense signal produced by the rGH-RBP mRNAs and rGH-RBP immunoreactivity in the hepatocytes, where the presence GH PRl LH-FSH NS Fig.…”

Section: Discussionmentioning

confidence: 99%

“…The concentration of gold particles in each pituicyte after in situ hybridization and immunocytological reactions was determined for 3 animals as previously described [27], Each cell type (n > 60) was photographed in order to count the gold particles per unit area of cell sections through the nucleus. All data were expressed as a mean ± SEM.…”

Section: Immunocytologymentioning

confidence: 99%

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Growth Hormone Receptor Binding Protein in Rat Anterior Pituitary

et al. 1994

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GH is synthesized by the somatotrophs in the pituitary, where it may have paracrine actions. In order to identify the GH target cells in rat pituitary, the cellular distributions of rat GH receptor binding protein messenger ribonucleic acid (rGH-RBP mRNA) and protein were investigated at the electron-microscopic level, using in situ hybridization and immunocytology, respectively, on ultrathin frozen sections of rat pituitary. Ultrastructural distribution of ¹²⁵I-bGH, 30 min after intracardiac administration was also performed in order to determine the pituitary cell types that bind the labeled hormone. In situ hybridization was performed using digoxigenin-labeled oligonucleotide probe revealed by indirect immunogold reaction. rGH-RBP mRNA was readily identified in the cytoplasmic matrix, associated with the endoplasmic reticulum and the nucleus of the somatotrophs, the lactotrophs and the gonadotrophs. No significant signal was detected in the corticotrophs or thyrotrophs. The number of gold particles in each pituitary cell type was estimated by direct counting, and was compared to the results of hybridization performed on rat liver sections as a control. The results showed that the level of rGH-RBP mRNA was higher in hepatocytes than in the pituitary cells, and was higher in the somatotrophs and lactotrophs than in the gonadotrophs. Immunocytological dectection of rGH-RBP was performed using two monoclonal antibodies (mAbs 43 and 263) directed against independent epitopes of the extracellular domain of the rGH-R. Indirect immunocytological detection showed regionalization of rGH-RBP; it was present in the cytoplasmic matrix and the nucleus of the hepatocytes and in discrete pituitary cells: somatotrophs, lactotrophs and gonadotrophs, but not in thyrotrophs or corticotrophs. Gold particle number was also higher in somatotrophs and lactotrophs than in gonadotrophs and higher in the nucleus compared to the cytoplasmic matrix. Radioiodinated GH was uptaken 30 min after injection by the same three pituitary cell types, showing evidence for the functional role of the GH receptor. In conclusion, we find that the cellular localization of rGH-RBP mRNA and protein is similar in discrete cell subpopulations of the pituitary, suggesting a direct effect of GH on somatotrophs, lactotrophs and gonadotrophs, through paracrine, autocrine or intracrine mechanisms.

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Section: Discussionmentioning

confidence: 99%

Section: Immunocytologymentioning

confidence: 99%

Growth Hormone Receptor Binding Protein in Rat Anterior Pituitary

et al. 1994

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“…1 for review). In particular, the occurrence of vasoactive intestinal polypeptide (2,3), GnRH (4), somatostatin (5), TRH (4,6), as well as their corresponding mRNAs (7)(8)(9)(10)(11) has been demonstrated in the rat anterior pituitary. In contrast, the biosynthesis of hypothalamic neuropeptides in the intermediate lobe of the pituitary has received little attention (12,13).…”

Section: The Biosynthesis Of Various Hypothalamic Neuropeptides Has Bmentioning

confidence: 99%

Expression and Processing of the [Pro²,Met¹³]Somatostatin-14 Precursor in the Intermediate Lobe of the Frog Pituitary

Tostivint¹,

Vieau²,

Chartrel³

et al. 2002

Endocrinology

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The biosynthesis of various hypothalamic neuropeptides has been previously reported in anterior pituitary cells but not in intermediate lobe cells. We have recently demonstrated the occurrence of two somatostatin isoforms in the frog brain, namely somatostatin-14 (SS1) and [Pro(2),Met(13)]somatostatin-14 (SS2). In the present study, we demonstrate that the gene encoding the SS2 precursor (PSS2) is actively expressed in the intermediate lobe of the frog pituitary. High concentrations of PSS2 mRNA have been detected by Northern blot analysis and in situ hybridization in the frog pars intermedia but not in the pars distalis or pars nervosa. The distribution of PSS1- and PSS2-derived peptides has been investigated by immunohistochemistry using two antisera directed against SS1 and the sequence 54-66 of PSS2 (PSS2(54-66)), respectively. The SS1 antiserum stained only a network of fibers in the neural lobe and a few nerve processes in the intermediate lobe. In contrast, the PSS2(54-66) antiserum produced intense labeling of melanotrope cells in the pars intermedia. Biochemical characterization of the immunoreactive materials present in pituitary extracts was performed by combining high-performance liquid chromatography analysis and RIA detection. The SS1 RIA revealed the existence of two major immunoreactive peaks that exhibited the same retention times as synthetic SS1 and SS2. The PSS2(54-66) RIA detected a single peak that likely corresponds to the N-flanking peptide of SS2 (PSS2(1-66)). The present study reveals that melanotrope cells of the frog pituitary selectively express the PSS2 gene and fully process PSS2 to generate the mature somatostatin variant SS2. Taken together, these data provide the first evidence that the gene encoding a hypophysiotropic neuropeptide is intensely expressed in the intermediate lobe of the pituitary.

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“…The concentration of gold particles in each cell type (N>30) after immunocytological reaction was determined for three animals as previously described (Breton et al 1995;Mesguich et al 1988). Each cell type was photographed in order to count the gold particles per unit area of cell sections.…”

Section: Quantificationmentioning

confidence: 99%

Intrauterine oxytocin system

Morel

Péchoux

Raccurt

et al. 2001

Cell and Tissue Research

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At term, uterine epithelial cells express oxytocin (OT) as well as the OT receptor (OTR). Like other epithelial cells, uterine epithelial cells are polarized and sort secretory and membrane components to the apical or the basolateral cell surface. We have studied the subcellular localization of OT-like immunoreactivity (OT-IR) and OTR-IR in rat uterine epithelium by immuno-gold labelling of ultrathin frozen sections. Our observations indicate that OT and OTR are both distributed preferentially to the apical surface of rat uterine epithelial cells. OT-IR showed a 6-fold apical versus basolateral preference and was localized in apical secretory vesicles, suggesting that uterine OT is released by apical exocytosis. OTR-IR was localized to the apical surface with a 9-fold apical versus basolateral preference and was found specifically in association with apical microvilli. The present findings represent the first example of a G protein-coupled receptor that is preferentially localized on the microvillar compartment and support the concept of an autocrine uterine OT system at the apical side of the uterine epithelium.

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Somatostatin-28- and somatostatin- 14-like immunoreactivities in the rat pituitary gland

Cited by 19 publications

References 47 publications

Growth Hormone Receptor Binding Protein in Rat Anterior Pituitary

Growth Hormone Receptor Binding Protein in Rat Anterior Pituitary

Expression and Processing of the [Pro²,Met¹³]Somatostatin-14 Precursor in the Intermediate Lobe of the Frog Pituitary

Intrauterine oxytocin system

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Somatostatin-28- and somatostatin- 14-like immunoreactivities in the rat pituitary gland

Cited by 19 publications

References 47 publications

Growth Hormone Receptor Binding Protein in Rat Anterior Pituitary

Growth Hormone Receptor Binding Protein in Rat Anterior Pituitary

Expression and Processing of the [Pro2,Met13]Somatostatin-14 Precursor in the Intermediate Lobe of the Frog Pituitary

Intrauterine oxytocin system

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Expression and Processing of the [Pro²,Met¹³]Somatostatin-14 Precursor in the Intermediate Lobe of the Frog Pituitary