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pregnenolone by cytochrome P 450 scc ( Payne & Hales 2004 ). We have previously demonstrated that the steroidogenic enzymes, such as P 450 scc, 3β-hydroxysteroid dehydrogenase (HSD), and 17β-HSD activities, are diminished in PCB-exposed adult rat Leydig cells
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in adult rat offspring ( Oliveira et al . 2009 ). Adipose tissue has a crucial role in metabolic disorders associated with obesity ( Rasouli & Kern 2008 ). Beyond secreting free fatty acids, the adipocytes release several proteins and hormones, such
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Department of Ophthalmology and Visual Sciences, University of Alberta, Edmonton, Alberta, Canada
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Department of Physiology, University of Alberta, Edmonton, Alberta, Canada
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of human T2D ( Cefalu 2006 , Srinivasan & Ramarao 2007 , King 2012 ). Therefore, it can be problematic when translating those results to humans. The Nile grass rat has the potential to be a highly suitable model for T2D in humans for two main
Department of Medicine-Gastroenterology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA
Department of Physiology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA
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Department of Medicine-Gastroenterology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA
Department of Physiology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA
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Department of Medicine-Gastroenterology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA
Department of Physiology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA
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Department of Medicine-Gastroenterology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA
Department of Physiology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA
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Department of Medicine-Gastroenterology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA
Department of Physiology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA
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Department of Medicine-Gastroenterology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA
Department of Physiology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA
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Department of Medicine-Gastroenterology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA
Department of Physiology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA
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Department of Medicine-Gastroenterology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA
Department of Physiology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA
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tissues using Trizol ® reagent (Gibco BRL). Isolation of total RNA Total RNA was extracted from CaCo-2 cell cultures and rat proximal colon tissues using Trizol ® reagent, following the protocol suggested by the
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SUMMARY
Rat prolactin (11 i.u./mg) was continuously infused into the circulation of urethaneanaesthetized lactating rats for 35 min at doses of either 200 or 472 ng/min. The immunoreactive prolactin in both milk and plasma rose quickly during the first 20–25 min of infusion, then stabilized at similar levels over baseline (68 and 98 ng/ml for milk and plasma, respectively, with the 200 ng/min dose and 250 and 230 ng/ml, respectively, with the 472 ng/min dose). The concentration of prolactin in plasma fell after the infusion was stopped, whereas that in the milk either did not fall at all or fell slightly to a new stabilized level. There was a rapid and extensive loss in the immunoreactivity of prolactin added to milk when rat milk was incubated in vitro (37 °C for 1–120 min) with either 600 ng/ml of extracted pituitary prolactin (NIAMDD RP-1) or unit equivalent amounts of prolactin obtained from pituitary culture media (secreted prolactin, supplied by C. S. Nicoll). Significantly greater amounts of added RP-1 prolactin were lost when it was incubated with milk obtained after 4 h than after 18 h of non-suckling. There was, however, no drop in endogenous immunoreactive milk prolactin levels (350–400 ng/ml) when rat milk was incubated with saline for 30 min. This suggests that milk prolactin obtained as a result of plasma transfer is different chemically from the milk prolactin resulting from the addition of either RP-1 or secreted prolactin to milk in vitro.
Approximately 90% of 131I-labelled rat prolactin appeared in the trichloroacetic acid precipitable fraction after incubation (37 °C for 120 min) with milk obtained after 4 h of non-suckling in either the presence or absence of thiouracil (added to prevent binding of 131I or 131I-labelled fragments to milk protein). The recovery was slightly less when 131I-labelled prolactin was incubated with milk obtained after 18 h of non-suckling.
These data suggest that prolactin is quickly transferred from plasma into milk in direct relation to the plasma concentration. Once there, much of it appears to be retained by the milk perhaps chemically or physically bound; there is little, if any, degradation of the hormone. We conclude that the lactating rat mammary gland may function normally as an excretory organ for prolactin.
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and summative changes in overall pituitary trophic (i.e. mitotic and apoptotic) activity, in the present study we have carefully examined the responses of the rat anterior pituitary to surgical gonadectomy and various sex hormone treatments over a
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SUMMARY
The pattern of proteins in the soluble fraction of the cytoplasm of the rat epididymis was studied by acrylamide gel electrophoresis. The components of five distinct bands, labelled A, B, C, D and E, were found to be sensitive to changes in androgen in the blood. Castration for 14 days produced a sharp decrease in the colour intensity of bands B–E when stained with Amido black. After 21 days of castration, bands D and E were undetectable, bands B and C were severely diminished and band A was more intense. Seven days of replacement with testosterone (1 mg/day) induced a return towards a normal pattern. The degree of restoration was inversely proportional to the duration of castration. Quantitation by densitometry showed that the relative contributions of bands B–E to the region A–E were 61% in the control rat, only 27% after 21 days of castration and 35% when testosterone was given between days 14 and 21 of castration. The components of bands A–E are presumed to be proteins since the electrophoretic pattern was altered by digestion with pronase but not by ribonuclease, phospholipase C or neuraminidase. Epididymides from castrated and androgen-treated castrated rats were incubated with 14C- and 3H-labelled mixed amino acids respectively. After co-electrophoresis the ratio 3H: 14C rose from a baseline of 2–5 in band B, 32 in band C and 7 in bands D and E. Molecular weights were estimated as 27900 for B, 23100 for C and 34400 for D. Band A had the same electrophoretic mobility as serum albumin. Bands B and C were also present in testicular cytosol. Bands D and E were only found in the epididymis, localized mainly within the lumen of the tubules. Bands B–E increased with age during sexual maturation, bands D and E became detectable in the 20-day-old rats. Preliminary evidence indicates that the proteins in bands C, D and E can be removed from caput spermatozoa by washing.
Department of Biochemistry and Molecular Biology,
Department of Anatomy and Cell Biology, The University of Melbourne, Victoria 3010, Australia
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Department of Biochemistry and Molecular Biology,
Department of Anatomy and Cell Biology, The University of Melbourne, Victoria 3010, Australia
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Department of Biochemistry and Molecular Biology,
Department of Anatomy and Cell Biology, The University of Melbourne, Victoria 3010, Australia
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Department of Biochemistry and Molecular Biology,
Department of Anatomy and Cell Biology, The University of Melbourne, Victoria 3010, Australia
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Department of Biochemistry and Molecular Biology,
Department of Anatomy and Cell Biology, The University of Melbourne, Victoria 3010, Australia
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Department of Biochemistry and Molecular Biology,
Department of Anatomy and Cell Biology, The University of Melbourne, Victoria 3010, Australia
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Department of Biochemistry and Molecular Biology,
Department of Anatomy and Cell Biology, The University of Melbourne, Victoria 3010, Australia
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Department of Biochemistry and Molecular Biology,
Department of Anatomy and Cell Biology, The University of Melbourne, Victoria 3010, Australia
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Department of Biochemistry and Molecular Biology,
Department of Anatomy and Cell Biology, The University of Melbourne, Victoria 3010, Australia
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species ( Kawamura et al. 2004 ). In an attempt to further elucidate the biology of the INSL3–LGR8 system in the rat, we cloned and sequenced rat Lgr8 cDNA and screened various tissues for Lgr8 mRNA expression using RT-PCR ( Scott et al. 2005
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of transcription factors in vitro and a reduction in body weight in vivo ( Murakami et al . 1997 , Grasso et al . 1999 ). The a and b isoforms are expressed in the rat placenta, showing an increment in their expression at term gestation
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ABSTRACT
Previous studies utilizing steroid-binding assays have suggested that corticosteroid-binding globulin (CBG)-like glucocorticoid binding sites are present in various tissues of the rat. It is not known, however, whether such binding reflects the intracellular presence of CBG derived from serum or a special class (type III) of receptors. In order to elucidate this problem, immunocytochemical localization of rat CBG was carried out using a specific antiserum prepared against rat serum CBG and the peroxidase-antiperoxidase technique. Positive staining was found in certain cells of the liver, the distal and/or convoluted tubules of the kidney, the uterus, the follicular cells of the thyroid, and some cells of the anterior pituitary. Other tissues including heart, muscle, thymus, hypothalamus, supraoptic and paraventricular nuclei, and diaphragm were negative. The presence of immunoreactive CBG in specific cells of some glucocorticoid-responsive tissues and not others raises interesting questions concerning the transport of glucocorticoids and their mechanism of action.
J. Endocr. (1986) 108, 31–36