Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P01189 (beta-endorphin)
 21,003 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

While the present understanding of pituitary-adrenal function predicts attenuation of responses to a repeated stressor, experimental observations often show occurrence of potentiation rather than inhibition. The role of the CNS in this phenomenon was investigated in rats sustaining either a single (S-HEM) or a double episode (R-HEM) of hemorrhage. For S-HEM, blood was withdrawn over 3min and retransfused at 10min; for R-HEM, the stimulus was repeated at 90 min. S-HEM elicited 26- and 9-fold increases in circulating adrenocorticotropin (ACTH) and corticosterone, respectively. After R-HEM the plasma ACTH response was potentiated by 82%. Sixty min after S-HEM, Fos-like immunoreactivity (Fos-IR) was increased in medullary (solitary nucleus, NTS and ventrolateral medulla, VLM), pontine (locus coeruleus, LC and parabrachial nucleus, PBN), limbic (central amygdala, CNA and bed nucleus, BNST), and hypothalamic (supraoptic nucleus, SON and paraventricular nucleus, PVN) regions activated by hemodynamic stimuli. However after R-HEM, the Fos-IR response was significantly potentiated only in the VLM and PVN, while only a moderate increase was evident in the NTS. In other brain regions (LC, PBN, CNA, BNST, HPC and SON), Fos-IR either did not change or the increases were less than those observed after S-HEM. It is suggested that this plasticity in the pattern of neuronal activation following repetition of a stimulus may account for the maintenance of pituitary-adrenal secretory responses and its potentiation after R-HEM.
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PMID:Patterns of Fos-Immunoreactivity in the CNS Induced by Repeated Hemorrhage in Conscious Rats: Correlations with Pituitary-Adrenal Axis Activity. 978 63

Ovoinhibitor is a serine protease-inhibiting protein that was originally purified from egg whites. It is secreted by the oviduct under the control of estrogen and progesterone and it specifically inhibits serine proteinases such as trypsin and chymotrypsin. During recent attempts to raise monoclonal antibodies (Mabs) against chicken bursa of Fabricius proteins, one Mab was produced that specifically recognized chicken ovoinhibitor. This was the first demonstration of ovoinhibitor in an avian immune organ. We presently report on the expression of an ovoinhibitor-like molecule by the pituitary of the chicken as revealed by immunocytochemistry and RT-PCR. Immunofluorescent dual staining experiments using the mouse anti-ovoinhibitor Mab in conjunction with polyclonal antibodies against various hypophysial hormones revealed partial co-localization of an ovoinhibitor-like molecule with growth hormone (GH), luteinizing hormone (LH), and pro-opiomelanocortin (POMC), in a subset of the respective hormone producing cells. By contrast, no co-localization with prolactin (PRL) could be reliably demonstrated. RT-PCR of hypophysial mRNA using ovoinhibitor gene-specific primers yielded an amplicon that was 20% shorter than predicted on the basis of the published ovoinhibitor sequence. Sequencing revealed that of the represented exons only the central portion was expressed in the pituitary and that both 5' and 3' ends of each exon had been truncated. While expression of ovalbumin-like serine protease inhibitors (serpins) has been previously reported in the rat pituitary, to our knowledge, this is the first report of a Kazal-type serine protease inhibitor in the vertebrate neuroendocrine system.
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PMID:The chicken pituitary expresses an ovoinhibitor-like protein in subpopulations of some, but not all, hormone-producing cell types. 1465 38

Ectoine, a zwitterionic compatible solute (CS), acts as an effective stabilizer of protein function. Using molecular dynamics simulation, solvent spatial distributions around both met-enkephalin (M-Enk) and chymotrypsin inhibitor 2 (CI2) were investigated at the molecular level in ectoine aqueous solution. An unexpected finding was that ectoine exhibits preferential binding, as an overall tendency, around both peptides. However, with the aid of the surficial Kirkwood-Buff parameter, it was clearly shown that the preferential exclusion of ectoine from the peptide surface was weaker in the smaller M-Enk than in the larger CI2. It is concluded that a denser and more structured hydration layer, such as that developed on the surface of CI2, is an important factor in the exclusion of ectoine.
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PMID:Microscopic understanding of preferential exclusion of compatible solute ectoine: direct interaction and hydration alteration. 1767 87


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