Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:2.7.7.48 (transcriptase)
 9,479 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Recently, overlapping molecular phenotypes of hematopoietic and neuropoietic cells were described in mice. Here, we examined primary human CD34(+) hematopoietic stem and progenitor cells applying specialized cDNA arrays, real-time reverse-transcriptase-polymerase chain reaction (RT-PCR), and fluorescent-activated cell sorter (FACS) analysis focusing on genes involved in neurobiologic functions. We found expression of vesicle fusion and motility genes, ligand- and voltage-gated ion channels, receptor kinases and phosphatases, and, most interestingly, mRNA as well as protein expression of G protein-coupled receptors of neuromediators (corticotropin-releasing hormone 1 [CRH 1] and CRH 2 receptors, orexin/hypocretin 1 and 2 receptors, GABAB receptor, adenosine A(2)B receptor, opioid kappa 1 and mu 1 receptors, and 5-HT 1F receptor). As shown by 2-color immunofluorescence, the protein expression of these receptors was higher in the more immature CD38(dim) than in the CD38(bright) subset within the CD34(+) population, and completely absent in fully differentiated blood cells, suggesting that those receptors play a role in developmentally early CD34(+) stem and progenitor cells. The intracellular concentration of cyclic adenosine monophosphate (cAMP) in CD34(+) cells was diminished significantly upon stimulation of either CRH or orexin receptors, indicating that those are functionally active and coupled to inhibitory G proteins in human hematopoietic cells. In conclusion, these findings suggest a molecular interrelation of neuronal and hematopoietic signaling mechanisms in humans.
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PMID:Primary human CD34+ hematopoietic stem and progenitor cells express functionally active receptors of neuromediators. 1501 51

The purpose of this study was to investigate whether orexin expression in the rat brain was changed during pregnancy. Brain samples were obtained from 5 nonpregnant rats and 10 pregnant rats (5; day 10 of gestation, and 5; day 20 of gestation). Reverse transcriptase-polymerase chain reaction (RT-PCR) analysis was performed to investigate the expression of prepro-orexin mRNA and the housekeeping gene in the rat brain. The signals were quantified by the densitometric analysis. The distribution and expression of orexin-A and orexin-B were determined using immunohistochemistry. The ratio of the prepro-orexin mRNA expressions to the housekeeping gene expression in pregnant rat brain were significantly higher than that in nonpregnant control. There was no significant difference between prepro-orexin mRNA levels of day 10 and day 20 of gestation. Immunohistochemical staining for orexin-A and orexin-B was present in neurons within and around the lateral and posterior hypothalamic areas in both nonpregnant and pregnant rats. These results suggest that increased prepro-orexin mRNA levels at early gestational age in the maternal rat has a role on energy metabolism during pregnancy.
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PMID:Prepro-orexin mRNA expression in the rat brain is increased during pregnancy. 1534 37

We report that mice with a targeted null mutation in the interferon type I receptor (IFN-RI), which cannot respond to such IFNs as IFNalpha and IFNbeta, have a 30% reduction in time spent in spontaneous rapid eye movement sleep (REMS) as a consequence of a reduced number of REMS episodes. Time spent in nonrapid eye movement sleep (NREMS) was essentially unaltered in IFN-RI knockouts (KOs) compared to 129 SvEv controls. Body temperature and locomotor activity were similar in both strains of mice. Hypothalamic expression of mRNAs for molecules previously linked to sleep-wake regulation and an IFN-inducible antiviral gene, 2',5'-oligoadenylate synthetase 1a (OAS), were determined by real-time reverse-transcriptase polymerase chain reaction (RT2-PCR). The level of hypocretin A mRNA was elevated in IFN-RI KO mice compared to 129 SvEv mice, while prolactin mRNA and OAS mRNA levels were suppressed. Vasoactive intestinal peptide (VIP) and corticotropin-releasing hormone (CRH) mRNA levels were unchanged relative to controls. Serum prolactin levels were similar in both strains. Results are consistent with the hypothesis that increased hypocretin and reduced prolactin in the hypothalamus of IFN-RI KO mice are responsible for their reduced REMS. In addition, the reduced OAS expression may result in modulation of prolactin receptor signaling and thus contribute to suppression of REMS.
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PMID:Mice deficient in the interferon type I receptor have reduced REM sleep and altered hypothalamic hypocretin, prolactin and 2',5'-oligoadenylate synthetase expression. 1549 63

Orexin-A (hypocretin-1), a neuropeptide with stimulatory actions on arousal and appetite, was originally shown to be specifically expressed in the hypothalamus. We studied expression of orexin-A and orexin receptors in the kidney and the presence of orexin-A-like immunoreactivity in human urine. Immunocytochemistry showed that orexin-A-like immunoreactivity and two types of orexin receptors (types 1 and 2) were localized in the tubules of the human kidney obtained at autopsy. Orexin-A-like immunoreactivity was detected in human kidneys (21.3 +/- 6.2 fmol/g wet weight, mean +/- S.E.M., n = 4) and rat kidneys (16.2 +/- 1.6 fmol/g wet weight, n = 5) by radioimmunoassay, although the levels were much lower than the levels in the brain. Orexin-A-like immunoreactivity was present in the urine obtained from male healthy volunteers (67.8 +/- 4.5 pmol/l, n = 5). Reverse phase high-performance liquid chromatography showed that most of orexin-A-like immunoreactivity of the urine extract was eluted earlier than authentic orexin-A, suggesting that orexin-A-like immunoreactivity in urine was modified to hydrophilic forms. Reverse transcriptase polymerase chain reaction showed expression of orexin receptors 1 and 2 mRNAs in the human kidney. These findings suggest that orexin-A is produced by the renal tubular cells and secreted into urine. Orexin-A may act on the kidney in the autocrine or paracrine fashion, or via the urine (urocrine fashion).
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PMID:Expression of orexin-A and orexin receptors in the kidney and the presence of orexin-A-like immunoreactivity in human urine. 1620 75

Transforming growth factor-betas are expressed in the brain, have neuroprotective functions, and may be involved in the pathogenesis of neurodegenerative disorders. Their intracellular processing, secretion, and extracellular activation requires latent transforming growth factor-beta binding proteins (LTBPs) as demonstrated in peripheral organs. Here, we first report that the four types of LTBPs are expressed in the rat brain based on reverse-transcriptase polymerase chain reaction (RT-PCR) and that the subtypes have different topographical distributions based on in situ hybridization histochemistry. LTBP-1 has a high expression level in several brain regions including choroid plexus, cerebral cortex, medial amygdaloid nucleus, anteromedial and midline thalamic nuclei, medial preoptic area, arcuate and dorsomedial hypothalamic nuclei, superior olive, and area postrema. LTBP-3 and -4 are the most widely distributed LTBPs. Both are abundant in the cerebral cortex, cerebellum, hypothalamus, amygdala, brainstem motor nuclei, and area postrema. In addition, LTBP-3 mRNA is also abundant in the choroid plexus, globus pallidus, anterior and reticular thalamic nuclei, mamillary body, substantia nigra, red nucleus, pontine nuclei, some brainstem sensory nuclei, and reticular formation, while LTBP-4 is more abundant in the hippocampus and the parabrachial nuclei. In contrast, the expression of LTBP-2 is restricted to cerebral cortex, CA1 neurons of the hippocampus, and perifornical/lateral hypothalamic areas. The hypothalamic cells were identified by double in situ hybridization histochemistry as orexin-synthesizing neurons, demonstrating that LTBP expression can be very specifically regulated. Our data demonstrate that each type of LTBPs have highly distinct distributional patterns suggesting that the expression of LTBPs are specifically regulated in the brain.
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PMID:Expression of latent transforming growth factor beta binding proteins in the rat brain. 1819 29

Orexin A (oxA) and orexin B are recently discovered peptides derived from the proteolytic cleavage of the common precursor prepro-orexin. They bind two G protein-coupled receptors, defined orexin 1 (ox1R) and orexin 2 receptor. Both peptides are highly expressed in the lateral hypothalamic area of the brain and are involved in the regulation of many functions of the body, the best investigated of which is food intake. Recent data described the presence of orexins in peripheral organs such as the adrenal glands, stomach, bowel, pancreas, and testis. Here, we report the detection of oxA and ox1R in the exocrine and endocrine cytotypes of the cattle urethroprostatic complex by using immunohistochemistry. The expression of prepro-orexin and ox1R mRNA transcripts in the prostatic tissue was assessed by reverse-transcriptase polymerase chain reaction, while the presence of both the proteins in the tissue was confirmed by Western blotting analysis. Our findings provide the first evidence for the presence of oxA and ox1R in the urethroprostatic complex of the cattle and demonstrate that both proteins are locally synthesized, thus suggesting a role for oxA on both physiological and pathological functioning of the complex.
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PMID:Expression of orexin A and its receptor 1 in the bovine urethroprostatic complex. 1821 4

The hypothalamic peptide orexin A (oxA) derives from the proteolytic cleavage of the precursor molecule prepro-orexin. It binds with the high affinity G-protein-coupled orexin receptor 1 (OX1R). Here, we report the detection of oxA and OX1R in the principal cells of the rat caudal epididymis by immunohistochemistry. Both oxA and OX1R immunolabelling showed cytoplasmic supranuclear localization, filling the apical portion of the cells. The expression of prepro-orexin and OX1R mRNA transcripts in the rat epididymis was assessed by reverse-transcriptase polymerase chain reaction, while the presence of both these proteins in the tissue was confirmed by Western blotting analysis. Our findings provide the evidence for the presence of oxA and OX1R in the rat epididymis, and demonstrate that both proteins are locally synthesised, thus suggesting a role for oxA in governing the fertilizing capability of the immature male gamete.
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PMID:Expression of orexin A and its receptor 1 in the rat epididymis. 1932 27

The aim of this paper is to explore the effect of intestinal ischemia/reperfusion (I/R) injury on leptin and orexin-A levels in peripheral blood and central secretory tissues, and to examine the roles of leptin and orexin-A in acute inflammatory responses. An intestinal I/R injury model of rats was made; the rats were grouped according to the time of after 60 min ischemia. Radioimmunoassay was employed to detect the levels of leptin in serum and adipose tissue and orexin-A levels in plasma and hypothalamus. Reverse transcriptase-polymerase chain reaction was used to detect mRNA expressions of adipose leptin and hypothalamus orexin-A. Compared with the levels before the injury, serum leptin in 60 min ischemia/30 min reperfusion (I60'R30') group decreased and that of I60'R360' group increased. Compared with sham-operation group (sham group) after injury, serum leptin level of I60'R360' group increased, adipose leptin levels of I60'R30' and I60'R90' decreased, and adipose leptin in I60'R360' group increased. After the injury, adipose leptin mRNA expressions of I60'R30', I60'R240' and I60'R360' increased, whereas that of I60'R150' group decreased as compared with the sham group. There was no significant difference in the protein levels of orexin-A, either between plasma and hypothalamus or between pre-and post-I/R injury. Compared with sham group, hypothalamus orexin-A mRNA expressions of I60'R30' and I60'R90' decreased gradually after the injury, with that of I60'R150' group reaching the lowest, and those of I60'R240' and I60'R360' recovering gradually, although they were still significantly lower than that of sham group. Leptin and orexin-A respond to intestinal I/R injury in a time-dependent manner, with leptin responding more quickly than orexin-A does, and both of them may contribute to the metabolic disorders in acute inflammation.
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PMID:Effect of intestinal ischemia/reperfusion injury on leptin and orexin-A levels. 2455 24