Reversibility of the inhibitory effect of atrazine and lindane on cytosol 5α-Dihydrotestosterone receptor complex formation in rat prostate

1991 ◽  
Vol 46 (1) ◽  
pp. 92-99 ◽  
Author(s):  
Branimir Šimić ◽  
Zlatko Kniewald ◽  
John E. Davies ◽  
Jasna Kniewald
Keyword(s):  
Complex Formation ◽  
Inhibitory Effect ◽  
Receptor Complex ◽  
Rat Prostate

THE BINDING OF [1,2-3H]TESTOSTERONE WITHIN NUCLEI OF THE RAT PROSTATE

1969 ◽  
Vol 44 (3) ◽  
pp. 323-333 ◽  
Author(s):  
W. I. P. MAINWARING
Keyword(s):  
Molecular Weight ◽  
Equilibrium Dialysis ◽  
Prostate Gland ◽  
Ventral Prostate ◽  
Rat Tissues ◽  
Receptor Complex ◽  
Rat Prostate ◽  
Binding Component

SUMMARY The specificity of the binding of [1,2-3H]testosterone to nuclei of various rat tissues in vivo has been studied. A significant amount of radioactivity was retained in the nuclei of androgen-dependent tissues only, particularly the ventral prostate gland. The bound radioactivity was only partially recovered as [1,2-3H]testosterone; the remainder was identified as [3H]5α-dihydrotestosterone. Efforts were made to characterize the binding component, or 'receptor', in prostatic nuclei. On digestion of nuclei labelled in vivo with [1,2-3H]testosterone, with enzymes of narrow substrate specificity, only trypsin released tritium, suggesting that the receptor is a protein. On the basis of subfractionation studies of labelled nuclei, the receptor is an acidic protein. The androgen—receptor complex could be effectively extracted from the prostatic nuclei in 1 m-NaCl and from the results of fractionations on a calibrated agarose column, the complex has a molecular weight 100,000–120,000. The specificity of the binding of steroids to such 1 m-NaCl extracts in vitro was investigated by the equilibrium dialysis procedure. Under these conditions, the specificity of the binding of [1,2-3H]testosterone demonstrated in vivo could not be simulated. The receptor is probably part of the chromatin complex but its precise intranuclear localization cannot be determined by biochemical procedures alone.

Homodimeric Murine Interleukin-3 Agonists Indicate that Ligand Dimerization is Important for High-Affinity Receptor Complex Formation

1994 ◽  
Vol 10 (1) ◽  
pp. 17-27 ◽  
Author(s):  
Horst Müther ◽  
Klaus Kühlcke ◽  
André Gessner ◽  
Said Abdallah ◽  
Heinz Lother
Keyword(s):  
Complex Formation ◽  
Receptor Complex ◽  
Interleukin 3 ◽  
High Affinity ◽  
High Affinity Receptor ◽  
Affinity Receptor

Participation of the upstream region of the fibroin gene in the formation of transcription complex in vitro

1986 ◽  
Vol 6 (11) ◽  
pp. 3928-3933
Author(s):  
M Tsuda ◽  
S Hirose ◽  
Y Suzuki
Keyword(s):  
Complex Formation ◽  
Specific Interaction ◽  
Inhibitory Effect ◽  
Silk Gland ◽  
Upstream Region ◽  
Fibroin Gene ◽  
Transcription Complexes ◽  
Posterior Silk Gland

The addition of exogenous histones has an inhibitory effect on fibroin gene transcription in posterior silk gland extracts. The histones probably disturb a process in complex formation, because when transcription complexes were constructed by preincubation of the templates with the extracts, the inhibitory effect of histones was greatly reduced. Transcription of a fibroin gene construct, pFb5' delta-238, having the upstream region beyond the TATA box was relatively less inhibited than that of pFb5' delta-44 lacking the upstream region. This tendency toward differential inhibition was observed in the silk gland extracts but not in a HeLa cell extract and persisted even after complex formation in the silk gland extracts, suggesting a specific interaction of the upstream region with some factors in the extracts. The complexes formed on pFb5' delta-44 are probably more susceptible to the inhibitory effect of histones. On the basis of these results we propose a participation of the upstream region of the fibroin gene in the formation of stable transcription complexes at the promoter through an interaction with specific factors in the silk gland. Since the transcription-enhancing effect via the upstream region is augmented at a high histone/DNA ratio, it may mimic the in vivo situation in which the fibroin gene can be transcribed in the posterior silk gland even in the presence of excess suppressive materials.

Single chain TNF derivatives with individually mutated receptor binding sites reveal differential stoichiometry of ligand receptor complex formation for TNFR1 and TNFR2

2010 ◽  
Vol 22 (7) ◽  
pp. 1088-1096 ◽  
Author(s):  
Verena Boschert ◽  
Anja Krippner-Heidenreich ◽  
Marcus Branschädel ◽  
Jessica Tepperink ◽  
Andrew Aird ◽  
...  
Keyword(s):  
Complex Formation ◽  
Receptor Binding ◽  
Binding Sites ◽  
Receptor Complex ◽  
Single Chain

scholarly journals Time-dependence of biological activity induced by covalent insulin-receptor complexes in rat adipocytes

1985 ◽  
Vol 232 (1) ◽  
pp. 49-53 ◽  
Author(s):  
A Schüttler ◽  
C Diaconescu ◽  
D J Saunders ◽  
D Brandenburg
Keyword(s):  
Insulin Receptor ◽  
Inhibitory Effect ◽  
Receptor Complex ◽  
Half Time ◽  
Simple Method ◽  
Receptor Complexes ◽  
Maximal Stimulation ◽  
Monocomponent Insulin ◽  
Specific Receptors ◽  
Stimulation Of

Lipogenesis in isolated adipocyte preparations is stimulated when photosensitive insulin derivatives are attached covalently to specific receptors. This response was compared quantitatively with that to reversibly associated insulin, and it was shown that both covalent and reversible insulin-receptor complexes behave very similarly. The extent of stimulation of lipogenesis was studied as a function of time. Cells were incubated in buffer for various times before addition to vials containing 0 (basal) or 10 ng of monocomponent insulin/ml (maximal) and [U-3H]glucose. After 60 min, the toluene-soluble [3H]lipids were measured. The maximal stimulation induced by reversibly bound insulin was virtually constant over a period of 4 h. In contrast, adipocytes to which N alpha B2-(2-nitro-4-azidophenylacetyl)-des-PheB1-insulin had been covalently attached at the start of the experiment showed a loss of stimulation with time when incubated at 37 degrees C. This loss was decreased in the presence of lysosomotropic agents such as chloroquine at concentrations (approx. 200 microM) that had very little or no effect on the basal and maximal lipogenesis rates. A simple method was used to transform the measured rate of loss of stimulation into a rate of loss of effective units. A half-time of 80 min was calculated for the effective covalent insulin-receptor units in adipocytes at 37 degrees C at pH 7.4. This is very close to values reported by others for the internalization of covalent complexes in these cells, suggesting that this may be the causative event for the deactivation of the insulin-receptor unit. The inhibitory effect of chloroquine on the deactivation may indicate that the insulin-receptor complex can function even after internalization.

Real-time dynamics of peptide ligand–dependent receptor complex formation in planta

2015 ◽  
Vol 8 (388) ◽  
pp. ra76-ra76 ◽  
Author(s):  
Marc Somssich ◽  
Qijun Ma ◽  
Stefanie Weidtkamp-Peters ◽  
Yvonne Stahl ◽  
Suren Felekyan ◽  
...  
Keyword(s):  
Complex Formation ◽  
Real Time ◽  
Peptide Ligand ◽  
Receptor Complex ◽  
In Planta ◽  
Time Dynamics

Roles of 3,5,3'-triiodothyronine and deoxyribonucleic acid binding on thyroid hormone receptor complex formation.

Endocrinology ◽  
1994 ◽  
Vol 134 (3) ◽  
pp. 1075-1081 ◽  
Author(s):  
P M Yen ◽  
J H Brubaker ◽  
J W Apriletti ◽  
J D Baxter ◽  
W W Chin
Keyword(s):  
Thyroid Hormone ◽  
Complex Formation ◽  
Hormone Receptor ◽  
Deoxyribonucleic Acid ◽  
Thyroid Hormone Receptor ◽  
Receptor Complex
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