scholarly journals Glucocorticoid receptors in lung. Comparison between nonactivated and activated forms of the cytoplasmic glucocorticoid binding protein and their relationship to the nuclear binding protein of fetal rabbit lung.

1975 ◽  
Vol 250 (8) ◽  
pp. 2904-2910
Author(s):  
G Giannopoulos
Keyword(s):  
Glucocorticoid Receptors ◽  
Binding Protein ◽  
Rabbit Lung ◽  
Nuclear Binding

scholarly journals Alteration of hepatic glucocorticoid receptor stability and nuclear binding in vitro by citrate

1983 ◽  
Vol 210 (1) ◽  
pp. 259-263 ◽  
Author(s):  
J Hubbard ◽  
M Kalimi
Keyword(s):  
Glucocorticoid Receptor ◽  
Glucocorticoid Receptors ◽  
Density Gradient Centrifugation ◽  
Gradient Centrifugation ◽  
Deae Cellulose ◽  
Sucrose Density Gradient ◽  
Sucrose Density Gradient Centrifugation ◽  
Nuclear Binding ◽  
Wide Range

Citrate greatly stabilized rat hepatic unbound glucocorticoid receptors in cell-free conditions at 4 degrees C with optimal effectiveness at 5-15 mM. Control receptors were inactivated at 4 degrees C with a half-life of less than 12 h. However, in the presence of 10 mM-citrate, unbound receptors were almost completely stabilized for 48 h at 4 degrees C. Citrate at a concentration of 1-2 mM yielded half-maximal stabilization. The stabilizing effect of citrate was rather specific, as succinate, alpha-oxoglutarate, oxaloacetate, malate and pyruvate had no apparent stabilizing action. Citrate stabilized receptors over a wide range of H+ concentrations, with complete protection between pH 6.5 and 8.5. In addition, citrate appeared to have a significant effect on glucocorticoid-receptor complex activation into a nuclear binding form. Thus 5-10 mM-citrate enhanced nuclear binding, with optimal activation achieved at 10 mM concentration. As analysed by sucrose-density-gradient centrifugation and DEAE-cellulose chromatography, no apparent change was observed in the physical characteristics of the glucocorticoid receptor in the presence of citrate.

511 INVOLVEMENT OF NUCLEAR BINDING PROTEIN C/EBP?? IN THE ACTIVATION OF PEPCK GENE EXPRESSION DURING EXERCISE

1994 ◽  
Vol 26 (Supplement) ◽  
pp. S91
Author(s):  
J. E. Friedman ◽  
S. E. Niezielski ◽  
C Arizmendi ◽  
A. R. Shteyngarts ◽  
C. J. Farrell
Keyword(s):  
Gene Expression ◽  
Protein C ◽  
Binding Protein ◽  
Nuclear Binding

IDENTIFICATION OF A NOVEL REPRESSOR ELEMENT IN THE CYCLO-OXYGENASE-2 PROMOTER AND ITS NUCLEAR BINDING PROTEIN

2008 ◽  
Vol 35 (10) ◽  
pp. 1204-1208 ◽  
Author(s):  
Xiaomin Yang ◽  
Ling Lin ◽  
Xiongfei Zhang ◽  
Yong Ji ◽  
Jinghuan Lv ◽  
...  
Keyword(s):  
Binding Protein ◽  
Nuclear Binding ◽  
Repressor Element

Triiodothyronine Nuclear Binding in Fetal and Adult Rabbit Lung and Cultured Lung Cells*

Endocrinology ◽  
1978 ◽  
Vol 103 (5) ◽  
pp. 1725-1731 ◽  
Author(s):  
JEFFREY A. LINDENBERG ◽  
ARLETTE BREHIER ◽  
PHILIP L. BALLARD
Keyword(s):  
Adult Rabbit ◽  
Lung Cells ◽  
Rabbit Lung ◽  
Nuclear Binding

scholarly journals A urokinase receptor mRNA binding protein from rabbit lung fibroblasts and mesothelial cells

1998 ◽  
Vol 274 (6) ◽  
pp. L871-L882 ◽  
Author(s):  
Sreerama Shetty ◽  
Steven Idell
Keyword(s):  
Malignant Mesothelioma ◽  
Binding Protein ◽  
Mesothelial Cells ◽  
Urokinase Receptor ◽  
Lung Fibroblasts ◽  
Cross Linking ◽  
Coding Region ◽  
Rabbit Lung ◽  
Mrna Binding Protein ◽  
Mrna Binding

The urokinase receptor (uPAR) influences several biological functions relevant to lung injury and repair, including proteolysis, cell migration, and adhesion. In malignant mesothelioma cells, we recently found that a posttranscriptional mechanism involving a cis- transinteraction between a uPAR mRNA sequence and a cytoplasmic uPAR mRNA binding protein (mRNABP) regulates uPAR gene expression (S. Shetty, A. Kumar, and S. Idell. Mol. Cell Biol. 17: 1075–1083, 1997). In this study, we sought to determine if uPAR expression in lung and pleural cells involves a similar posttranscriptional pathway. We first identified and characterized the uPAR mRNABP in rabbit tissues using gel mobility shift, ultraviolet (UV) cross-linking, and RNase protection assays and detected it in liver, heart, brain, spleen, colon, and lung. Phorbol 12-myristate 13-acetate, lipopolysaccharide, transforming growth factor-β, tumor necrosis factor-α, or cycloheximide induced uPAR and uPAR mRNA expression in cultured rabbit pleural mesothelial cells and lung fibroblasts and concurrently reduced the uPAR mRNA-uPAR mRNABP interaction. Using conventional and affinity chromatography, we purified a 50-kDa uPAR mRNABP that selectively binds to a 51-nucleotide fragment of the uPAR coding region. This protein migrates as a monomer when analyzed by SDS-PAGE and UV cross-linking and does not possess intrinsic RNase activity in vitro. A uPAR mRNABP physicochemically and functionally similar to that of human malignant mesothelioma is constitutively expressed in the rabbit lung and other nonneoplastic tissues. In rabbit lung fibroblasts and mesothelial cells, expression of uPAR involves posttranscriptional regulation whereby the uPAR mRNABP appears to interact with a specific coding region cis-element to decrease the stability of uPAR mRNA.

Glucocorticoid receptors in rat kidney cortical tubules enriched in proximal and distal segments

1981 ◽  
Vol 240 (1) ◽  
pp. F38-F45 ◽  
Author(s):  
T. Mishina ◽  
D. W. Scholer ◽  
I. S. Edelman
Keyword(s):  
Triamcinolone Acetonide ◽  
Glucocorticoid Receptors ◽  
Rat Kidney ◽  
Affinity Binding ◽  
High Affinity ◽  
Nuclear Binding ◽  
Fitting Method ◽  
Least Squares Curve Fitting ◽  
Distal Tubules ◽  
Curve Fitting Method

Cytoplasmic and nuclear binding of [3H]triamcinolone acetonide was assessed in isolated rat kidney cortical tubules, enriched in distal (fraction A) or in proximal segments (fraction B). The concentration dependence of specific [3H]triamcinolone acetonide binding in cytoplasm was determined (range = 4.4 X 10(-10) to 2.1 X 10(-7) M) and analyzed by a least-squares curve-fitting method. A single, high-affinity binding class with a dissociation constant of 1 X 10(-8) M (25 degrees C) was obtained in both fractions A and B. Based on competition for the [3H]triamcinolone acetonide sites, the following sequence of affinities was obtained: triamcinolone acetonide = dexamethasone > progesterone = corticosterone > d-aldosterone > 17 beta-estradiol. These specificities imply that these sites are glucocorticoid receptors. Fraction B contained 1.6 times more cytosol sites for [3H]triamcinolone acetonide than fraction A (5.0 +/- 0.5 X 10(-13) vs. 3.0 +/- 0.5 X 10(-13) mol/mg protein). In the presence of a onefold excess of d-aldosterone specific cytoplasmic binding of [3H]triamcinolone acetonide was 1.4-fold greater in fraction B than in fraction A, and specific nuclear binding was 1.3-fold greater in fraction B than in fraction A (5.1 +/- 0.6 X 10(-13) vs 4.0 +/- 0.5 X 10(-13) mol/mg DNA). These results and the measured lengths of proximal and distal tubules yielded estimates of a higher proximal content (three- to sixfold) compared to distal content of glucocorticoid receptors.

scholarly journals Distribution of actin-binding protein and myosin in macrophages during spreading and phagocytosis.

1980 ◽  
Vol 84 (2) ◽  
pp. 215-224 ◽  
Author(s):  
O I Stendahl ◽  
J H Hartwig ◽  
E A Brotschi ◽  
T P Stossel
Keyword(s):  
Actin Filaments ◽  
Structural Unit ◽  
Binding Protein ◽  
Actin Binding ◽  
Rabbit Lung ◽  
Actin Binding Protein ◽  
Lung Macrophages ◽  
In Cells

Actin-binding protein (ABP) and myosin are proteins that influence the rigidity and movement, respectively, of actin filaments in vitro. We examined the distribution of ABP and myosin molecules in acetone-fixed rabbit lung macrophages by means of immunofluorescence. The staining for both of these proteins in unspread cells was quite uniform, but was reduced in the nucleus and concentrated slightly in the periphery. The peripheral accumulation of staining attenuated in uniformly spread cells, although filopodia and hyaline veils definitely stained. In cells fixed during ingestion of yeast particles, the brightest staining correlated with the disposition of organelle-excluding pseudopodia initially surrounding the yeast. After phagocytosis was complete and the yeasts resided in intracellular vacuoles, no concentration of staining around the ingested yeasts was detectable. We conclude that ABP and myosin molecules are components of the structural unit of the cell responsible for spreading and phagocytosis, the hyaline cortex, a region known to be rich in actin filaments. The findings are consistent with the theory that these molecules control the rigidity and movement of filaments in the periphery of the living macrophage.

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