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)

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

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

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