109. Properties of the glucocorticoid receptor in rat tissues and in HTC cells

1978 ◽  
Vol 9 (9) ◽  
pp. 835-836
Author(s):  
D. Philibert ◽  
J.P. Raynaud
Keyword(s):  
Glucocorticoid Receptor ◽  
Rat Tissues ◽  
Htc Cells

scholarly journals Identification and tissue distribution of a novel rat glucocorticoid receptor splice variant.

2009 ◽  
Vol 56 (1) ◽  
Author(s):  
Huiming Ju ◽  
Xia Wang ◽  
Zongping Liu ◽  
Ping Liu ◽  
Yan Zhao ◽  
...  
Keyword(s):  
Glucocorticoid Receptor ◽  
Splice Variants ◽  
Blot Hybridization ◽  
Rat Tissues ◽  
Northern Blot Hybridization ◽  
Base Pairs ◽  
Physiological Processes ◽  
Sd Rat ◽  
Exon 1 ◽  
Nongenomic Effects

Glucocorticoid receptor (GR) is a steroid hormone receptor that has been shown to play important roles in diverse cellular and physiological processes. More and more evidence has revealed that the effects of glucocorticoids are mediated by the glucocorticoid receptor through genomic or nongenomic mechanisms. A growing number of glucocorticoid receptor splice variants have been identified in human tissues, but few are known in rat tissues. In this work, a novel rGR cDNA, called rGRbeta, was cloned from Sprague Dawlay (SD) rat liver. Sequence analysis revealed that the rGRbeta mRNA was 39 base pairs (bp) shorter than the rGR mRNA reported earlier. The deleted segment is located in exon 1 and encodes 13 repeated glutamine residues. Both the rGR and rGRbeta mRNAs were quantitated by Northern blot hybridization using non-homologous glucocorticoid cDNA probes. Results showed that the rGR and rGRbeta mRNAs were most abundant in the lung, the least abundant in the heart, and there were more rGR and rGRbeta mRNAs in the kidney than in the liver. The identification of rGRbeta may contribute to the understanding of the genomic or nongenomic effects of glucocorticoids.

Immunolocalization of the glucocorticoid receptor in rat tissues

1988 ◽  
Vol 117 (4_Suppl) ◽  
pp. S27
Author(s):  
U. RAUSCH ◽  
J. SEITZ ◽  
H. WESTPHAL ◽  
G. AUMÜLLER
Keyword(s):  
Glucocorticoid Receptor ◽  
Rat Tissues

High-resolution scanning electron microscopy (HRSEM) of mitochondria from various rat tissues

1988 ◽  
Vol 46 ◽  
pp. 14-15
Author(s):  
P.J. Lea ◽  
M.J. Hollenberg
Keyword(s):  
Electron Microscopy ◽  
Pigment Epithelium ◽  
Retinal Pigment ◽  
Rat Hepatocytes ◽  
Three Dimensions ◽  
Objective Lens ◽  
Rat Tissues ◽  
Thin Sections ◽  
Reconstruction Methods ◽  
Scanning Electron

Our current understanding of mitochondrial ultrastructure has been derived primarily from thin sections using transmission electron microscopy (TEM). This information has been extrapolated into three dimensions by artist's impressions (1) or serial sectioning techniques in combination with computer processing (2). The resolution of serial reconstruction methods is limited by section thickness whereas artist's impressions have obvious disadvantages.In contrast, the new techniques of HRSEM used in this study (3) offer the opportunity to view simultaneously both the internal and external structure of mitochondria directly in three dimensions and in detail.The tridimensional ultrastructure of mitochondria from rat hepatocytes, retinal (retinal pigment epithelium), renal (proximal convoluted tubule) and adrenal cortex cells were studied by HRSEM. The specimens were prepared by aldehyde-osmium fixation in combination with freeze cleavage followed by partial extraction of cytosol with a weak solution of osmium tetroxide (4). The specimens were examined with a Hitachi S-570 scanning electron microscope, resolution better than 30 nm, where the secondary electron detector is located in the column directly above the specimen inserted within the objective lens.

The Demonstration of Human Prostatic Acid Phosphatase (Pap) With Phosphorylcholine

1976 ◽  
Vol 34 ◽  
pp. 88-89
Author(s):  
José A. Serrano ◽  
Hannah L. Wasserkrug ◽  
Anna A. Serrano ◽  
Arnold M. Seligman
Keyword(s):  
Acid Phosphatase ◽  
Prostate Gland ◽  
Prostatic Acid Phosphatase ◽  
Human Prostate ◽  
Rat Tissues ◽  
Specific Substrate ◽  
Acid Phosphatases ◽  
Lysosomal Acid ◽  
Cacodylate Buffer

As previously reported (1, 2) phosphorylcholine (PC) is a specific substrate for prostatatic acid phosphatase (PAP) as opposed to other acid phosphatases, e.g., lysosomal acid phosphatase. The specificity of PC for PAP is due to the pentavalent nitrogen in PC, a feature that renders PC resistant to hydrolysis by all other acid phosphatases. Detailed comparative cytochemical results in rat tissues are in press. This report deals with ultracytochemical results applying the method to normal and pathological human prostate gland.Fresh human prostate was obtained from 7 patients having transurethral resections or radical prostatectomies. The tissue was fixed in 3% glutaraldehyde- 0.1 M cacodylate buffer (pH 7.4) for 15 min, sectioned at 50 μm on a Sorvall TC-2 tissue sectioner, refixed for a total of 2 hr, and rinsed overnight in 0.1 M cacodylate buffer (pH 7.4)-7.5% sucrose.

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