Binding of a tritiated thyrotropin-releasing factor to a prolactin secreting clonal cell line (GH3)

Gourdji, D.; Tixier‐Vidal, A.; Morin, Annie; Pradelles, Philippe; Morgat, Jean‐Louis; Fromageot, P.; Kerdelhué, B.

doi:10.1016/0014-4827(73)90242-5

Cited by 83 publications

(35 citation statements)

References 17 publications

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“…Moreover, autoradiographic study of GH3 cells previously incubated for 30 min with 3 H-labelled TRF revealed the presence of radioactive material within the cells but no concentration on the plasma membrane [7,8]. A similar localization has been found by dry mount autoradiography in pituitary cells of rat sacrified 1 hr after the injection of 3H-labelled TRF [10].…”

Section: Introductionmentioning

confidence: 58%

“…As it is generally admitted that peptide hormone receptors are localized on plasma membrane, it could be objected that the present results might correspond to a displacement of TRF during the homogenization and fractionation procedures. This possibility however may be ruled out since: 1) as previously shown, cells incubated with 3H-labelled TRF and extensively washed at 4°C retain at this temperature their radioactivity for at least 6 hr [8]. By its stability the binding of 3H-labelled TRF by GH3 cells strongly contrasts with that previously observed for pituitary plasma membrane preparations which is rapidly dissociated at 4°C [ 11 ].…”

Section: Discussionmentioning

confidence: 93%

“…Previous analysis of the interaction of the 3H-labelled TRF [6] with the GH3 ceils [7,8] allowed establishing several characteristics of the HG3 cells binding sites for TRF. The binding is time dependent, increasing linearly in the first 15 rain and thereafter reaching a plateau.…”

Section: Introductionmentioning

confidence: 99%

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Chemical evidence for associated TRF with subcellular fractions after incubation of intact rat prolactin cells (GH3) with ³H‐labelled TRF

et al. 1974

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Section: Introductionmentioning

confidence: 58%

Section: Discussionmentioning

confidence: 93%

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Chemical evidence for associated TRF with subcellular fractions after incubation of intact rat prolactin cells (GH3) with ³H‐labelled TRF

et al. 1974

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“…Such a phenomenon might correspond to the internalization of a fraction of the radioactive material escaping from the two-dimensional space of the membrane surface. The entry of 3H-labeled thyrotropin-releasing factor in a prolactin secreting clonal cell line [12], of '251-labeled insulin in human cultured lymphocytes [13], and of '251-labeled low density lipoproteins in fibroblasts [14] is well documented.…”

Section: Dissociution Of Bound [ 3h]cueruleinmentioning

confidence: 99%

The Interaction of Caerulein with the Rat Pancreas. 2. Specific Binding of [3H]Caerulein on Dispersed Acinar Cells

Christophe

Deschodt-Lanckman

et al. 1978

Eur J Biochem

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[3H]Caerulein was bound to dispersed acinar cells from rat pancreas in a rapid, reversible, specific, saturable, and temperature-dependent manner. Binding decreased above pH 6.5. lein within 1 min at 37 "C. The dissociation of remainder followed much slower kinetics. .The results suggested that intact rat pancreatic acinar cells have one class of caerulein binding sites existing in two states: one with high affinity and another with low affinity, the proportion of sites in each state depending on the degree af site occupancy (negative cooperativity), and on the intracellular concentration of nucleotides.Caerulein, a decapeptide isolated from the skin of the Australian amphibian Hyla cacrulea, is similar in chemical structure and in biologic activity to cholecystokinin-pancreozymin [l -41. In general the potency of caerulein is approximately the same as that of the C-terminal octapeptide of cholecystokininpancreozymin.The interaction of monotritiated [3H]caeruleiii with rat pancreatic plasma membranes has been reported in the preceding paper [5]. A study with dispersed intact acinar cells was undertaken to observe the effect of extramembrane events on caerulein binding, e. with the ability to stimulate secretion, calcium outflux and adenylate cyclase activity. Some of the present data have been published in abstract form [7]. MATERIALS AND METHODS Preparation of Isolated Rat Pancreatic Acinar CellsMale Wistar albino rats (200-250 g) fed ad libitum were sacrificed by decapitation. Isolated pancreatic acinar cells were prepared following the procedure of Amsterdam and Jamieson [8] using crude collagenase and hyaluronidase, EDTA and mild shearing forces. The digestion of the rat pancreas and the isolation of acinar cells offered no more difficulty than that of the guinea pig. The final three washings of the cells were conducted in media containing 0.5 mM calcium concentration. Light microscopy revealed that 96 -98 % of the cells were zymogen-containing exocrine cells. Their viability was demonstrated by their ability to exclude trypan blue. Cell concentration was determined by counting an appropriately diluted suspension in a conventional Neubauer hemocytometer. Unless otherwise specified, the dispersed acinar cells

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“…Peptide hormones, including thyrotropin-releasing hormone and somatostatin (Gourdji, Tixier-Vidal, Morin, Pradelles, Morgat, Fromageot & Kerdelhue, 1973;Morel, 1994), were found to localize in the nucleus in lactotrophic cells.…”

Section: Endocrine Cells and Neurons)mentioning

confidence: 99%

Intracellular trafficking of prohormones and proneuropeptides: cell type‐specific sorting and targeting

Perone¹,

Windeatt²,

Castro³

1997

Experimental Physiology

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Binding of a tritiated thyrotropin-releasing factor to a prolactin secreting clonal cell line (GH3)

Cited by 83 publications

References 17 publications

Chemical evidence for associated TRF with subcellular fractions after incubation of intact rat prolactin cells (GH3) with ³H‐labelled TRF

Chemical evidence for associated TRF with subcellular fractions after incubation of intact rat prolactin cells (GH3) with ³H‐labelled TRF

The Interaction of Caerulein with the Rat Pancreas. 2. Specific Binding of [3H]Caerulein on Dispersed Acinar Cells

Intracellular trafficking of prohormones and proneuropeptides: cell type‐specific sorting and targeting

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Binding of a tritiated thyrotropin-releasing factor to a prolactin secreting clonal cell line (GH3)

Cited by 83 publications

References 17 publications

Chemical evidence for associated TRF with subcellular fractions after incubation of intact rat prolactin cells (GH3) with 3H‐labelled TRF

Chemical evidence for associated TRF with subcellular fractions after incubation of intact rat prolactin cells (GH3) with 3H‐labelled TRF

The Interaction of Caerulein with the Rat Pancreas. 2. Specific Binding of [3H]Caerulein on Dispersed Acinar Cells

Intracellular trafficking of prohormones and proneuropeptides: cell type‐specific sorting and targeting

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Chemical evidence for associated TRF with subcellular fractions after incubation of intact rat prolactin cells (GH3) with ³H‐labelled TRF

Chemical evidence for associated TRF with subcellular fractions after incubation of intact rat prolactin cells (GH3) with ³H‐labelled TRF