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

We have characterized a precursor protein which gives rise to the neuropeptide Phe-Met-Arg-Phe-amide (FMRFamide) by determining the nucleotide sequence of a genomic and five cDNA clones. The 597-amino-acid protein contains 28 copies of the tetrapeptide FMRFamide, a single Phe-Leu-Arg-Phe-amide (FLRFamide), and other sequences flanked by paired basic residues, some of which have homologies to mammalian brain peptides. The data presented suggest the genes encoding pro-opiomelanocortin, pre-pro-enkephalin, and the hypothalamic releasing factor, cortico-releasing factor (CRF), arose from a common ancestral gene.
 ...
PMID:The Aplysia FMRFamide gene encodes sequences related to mammalian brain peptides. 381 95

The function of alpha-melanocyte-stimulating hormone (alpha-MSH) is not known in mammals. It is well-established in the amphibian Xenopus laevis in which alpha-MSH mediates the process of adaptation to a dark background. The amino acid sequence of this hormone is, however, not known in amphibians. In order to determine the primary structure of the precursor protein for alpha-MSH, which in mammals has been called pro-opiomelancortin (POMC), we constructed a cDNA library from Xenopus pituitary mRNA. A pool of synthetic oligodeoxyribonucleotide tetradecamers corresponding to part of the mammalian alpha-MSH sequence was used to screen the library. The nucleotide sequence of a 1050-base pair hybridization-positive cDNA clone was determined and the deduced amino acid sequence of Xenopus POMC revealed the sequences of Xenopus gamma-MSH, alpha-MSH, corticotropin-like intermediate lobe peptide, beta-MSH, and beta-endorphin. Interestingly, the N-terminal amino acid of Xenopus alpha-MSH, which is N alpha-acetylated in the biologically active form of the hormone, is different from that of mammalian alpha-MSH. The distribution of the bioactive domains within Xenopus POMC is remarkably similar to that in other known POMC molecules and as in mammals the domains in the amphibian prohormone are flanked on both sides by pairs of basic amino acids.
 ...
PMID:Nucleotide sequence of cloned cDNA for pro-opiomelanocortin in the amphibian Xenopus laevis. 384 Apr 81

beta-endorphin and adrenocorticotropic hormone (ACTH) are derived from the same precursor protein, and the plasma levels of beta-endorphin and ACTH are thought to be representative of the pituitary secretion of these peptides. Simultaneous measurements of immunoreactive beta-endorphin and ACTH were done on plasma samples from pregnant women at term and found to be normal, but a significant increase was observed during the stress of labor. Simultaneous measurement of immunoreactive beta-endorphin and ACTH in the umbilical vein at time of vaginal delivery demonstrated elevated levels of both peptides. The newborn also demonstrated an increased ratio of beta-endorphin to ACTH, of which the role is uncertain at present.
 ...
PMID:Plasma levels of immunoreactive beta-endorphin and adrenocorticotropic hormone during labor and delivery. 608 29

Nakanishi et al. have recently characterised the complete sequence of the mRNA isolated from the intermediate lobe of bovine pituitary which codes for the 31,000 molecular weight (31K) precursor protein of corticotropin/beta-lipotropin (ACTH/beta-LPH). The corresponding amino acid sequence translated from this mRNA revealed in the cryptic region of the precursor protein a fragment sharing a common amino acid sequence with the alpha- beta-melanotropins (alpha-MSH, beta-MSH) and thus named gamma-MSH. To study whether this gamma-MSH fragment is also processed and released as a biologically active substance and to ascertain its location in the pituitary and possibly in the brain, we have raised antibodies to the synthetic replicate of gamma 3-MSH (ref. 2). We report here the detection of at least two gamma-MSH-like peptides in the pituitary using these antibodies in a radioimmunoassay (RLA) and, furthermore, evidence that these two peptides are glycosylated.
 ...
PMID:Pituitary immunoreactive gamma-melanotropins are glycosylated oligopeptides. 610 Dec 29

The primary structure of a precursor protein that contains beta-neo-endorphin, dynorphin and a third leucine-enkephalin sequence with a carboxyl extension has been deduced from the nucleotide sequence of cloned DNA complementary to the porcine hypothalamic mRNA encoding it. The three peptides are each bounded by Lys-Arg. This precursor protein, like adrenal preproenkephalin and the corticotropin/beta-lipotropin precursor, comprises multiple repetitive units and a cysteine-containing amino-terminal sequence preceded by a signal peptide.
 ...
PMID:Cloning and sequence analysis of cDNA for porcine beta-neo-endorphin/dynorphin precursor. 612 53

The pituitary hormones corticotropin (ACTH) and beta-lipotropin (beta-LPH) are formed from a large common precursor. Recently, we have elucidated the whole primary structure of the bovine ACTH-beta-LPH precursor (designated alternatively as preproopiocortin) by determining the nucleotide sequence of cloned DNA complementary to the mRNA coding for the precursor protein. The amino acid sequence assigned has disclosed a characteristic repetitive structure of the ACTH-beta-LPH precursor. The repetitive units of the precursor protein each contain a melanotropin (MSH) sequence (alpha-, beta- or gamma-MSH) as well as other peptide components such as beta-endorphin and corticotropin-like intermediate lobe peptide (CLIP). The repetitive units as well as their peptide components are each bounded by paired basic amino acid residues, which apparently represent the sites of proteolytic processing. Several studies have confirmed the translational initiation site and protein structure assigned (see also ref. 11 and refs therein). In view of the recent knowledge about the organization of eukaryotic genes (see refs 12, 13 for reviews), it would be of particular interest to investigate the relationship between the repetitive structure of the ACTH-beta-LPH precursor containing different functional components and the arrangement of the protein-coding sequence in its gene. We have now isolated and characterized bovine genomic DNA fragments encoding this precursor protein and have demonstrated that the protein sequence is encoded by two non-consecutive DNA segments. An intron (intervening sequence) of approximately 2.2 kilobase pairs separates the smaller exon (mRNA-coding sequence), which contains the gene sequence encoding the signal peptide, from the larger exon, which contains the gene sequence for most of the protein structure, including the known biologically active component peptides.
 ...
PMID:The protein-coding sequence of the bovine ACTH-beta-LPH precursor gene is split near the signal peptide region. 625 15

Regulation of secretion of ACTH-, beta-endorphin-, and gamma-melanotropin-like immunoreactivities (ACTH-LI, beta-EP-LI, and gamma-MSH-LI, respectively) was studied by using a perfused Sephadex column containing dispersed pituitary tumor cells obtained from three patients with Cushing's disease. Serial dilution of the perfusion medium gave lines parallel to the standard curve in each RIA for ACTH, beta-EP and gamma-MSH, suggesting that immunoreactive materials in the medium are immunologically indistinguishable from the authentic peptides. Gel exclusion chromatography of the medium revealed the existence of ACTH, beta-lipotropin (beta-LPH), beta-EP, and their possible precursor protein. gamma-MSH-LI consists of a major peak of big gamma-MSH eluted near the elution position of beta-LPH, suggesting the entire or nearly entire N-terminal portion of the precursor molecule. The addition of lysine vasopressin and rat median eminence extracts (MEE) to the perfusion system concomitantly enhanced the release of ACTH-LI, beta-EP-LI, and gamma-MSH-LI, although the dose-response relationship was clear-cut only in the case of MEE. TRH and LRH also elicited the concomitant release of these peptides in one patient, in whom combined administration of TRH and LRH significantly augmented plasma cortisol levels when studied preoperatively. The molar ratio of ACTH-LI to beta-EP-LI was approximately 1.0, whereas gamma-MSH-LI was about one fourth of ACTH-LI when compared on a weight basis. These results indicate that 1) ACTH-producing human pituitary adenomas concomitantly secrete ACTH, beta-LPH, beta-EP, and big gamma-MSH, and 2) lysine vasopressin, MEE, TRH, and LRH act directly on pituitary cells to stimulate the release of these peptides.
 ...
PMID:Concomitant secretion of adrenocorticotropin, beta-endorphin, and gamma-melanotropin from perfused pituitary tumor cells of Cushing's disease: effects of lysine vasopressin, rat median eminence extracts, thyrotropin-releasing hormone, and luteinizing hormone-releasing hormone. 625 4

The focus of research in our laboratory over the past few years has been the regulation of synthesis, processing and release of the ACTH/LPH family of peptides. These peptides are derived from a common precursor protein that is found in both the anterior and intermediate lobes of the pituitary (Roberts et al. 1978) and in the hypothalamus (Liotta et al. 1979). In the anterior lobe this protein gives rise to alpha (1-39)ACTH, beta-lipotropin and an N-terminal fragment of undefined function. In addition, a variety of intermediate lobe pituitary peptides can be derived from the precursor by further processing of ACTH and beta-LPH. In this paper we compare the structure of the precursor in the anterior and intermediate lobes of mouse and rat pituitary. Processing of the precursor to its constituent hormones is then contrasted in primary cultures of anterior and intermediate lobe cells using pulse label and pulse chase techniques with radioactive amino acids and sugars. Finally, we discuss the difference in behaviour of anterior and intermediate lobe cells in culture with regard to their rates of secretion and intracellular turnover of hormones and regulation of these processes by hypothalamic factors, glucocorticoids and catecholamines.
 ...
PMID:A cellular basis for the differences in regulation of synthesis and secretion of ACTH/endorphin peptides in anterior and intermediate lobes of the pituitary. 625 70

The peptide hormones of the intermediate lobe are derived from a common precursor protein and are therefore biogenetically and structurally related. They represent a group of linear, flexible peptides which elicit a variety of physiological response. Structure-activity studies have shown that different segments of adjacent amino acid residues have a specific function (e.g. address, message, potentiation) in the interaction of each of these hormones with its receptor(s). This kind of organization of hormonal information is called sychnologic; it is the basic for the pleiotropic action of the opiomelanocortin peptides, i.e. the ability of related peptides to interact with different types of receptors in different target cells. Labelled peptide hormones with radioactive, fluorescent, or photolabile groups at defined sites are a prerequisite for studying hormone-receptor interaction. Multi-labelled derivatives of alpha-MSH are suitable for degradation and intracellular incorporation studies. Photoaffinity labelling of melanophore receptors with azidophenyl-containing analogues of alpha-MSH produces an irreversible stimulation of pigment cells. Covalent conjugates between peptide hormone receptors. These conjugates exhibit remarkable properties such as superpotency, strongly enhanced receptor affinity and prolonged action.
 ...
PMID:Structure and chemistry of the peptide hormones of the intermediate lobe. 626 75

Extracts of human term placenta were fractionated by Sephadex G-75 gel filtration and assayed for immunoreactive ACTH. Both high and low molecular weight protein fractions were detected to be immunologically reactive toward anti-human ACTH (1--39 alpha) antibody. For the extraction of low molecular weight ACTH from human term placenta (pl. -ACTH), a glacial acetic acid-acetone mixture was employed, while a pH 3.0-HCl solution was used for high molecular weight immunoreactive ACTH. The high molecular weight immunoreactive ACTH fraction (F-I), co-eluted with horse hemoglobin from a Sephadex G-75.column in 0.1M acetic acid, was essentially devoid of low molecular weight materials as revealed by polyacrylamide gel disc electrophoresis at pHs 9.5 and 4.3. Tryptic digestion of F-1 at pH 8.1 and 37 degrees C for 4 hr with E/S of 1/100, followed by fractionation with a Sephadex G-75, resulted in the formation of lower molecular weight fragments. One fragment was eluted at the same position as that of porcine ACTH with a recovery of 86% of immunoreactivity of F-I. Another fragment which was eluted last exhibited positive beta-endorphin receptor binding activity. These results suggest the presence of a common precursor protein to ACTH and beta-endorphin in human term placenta.
 ...
PMID:[Studies on immunoreactive ACTH from human term placenta. (I) Detection of a high molecular weight-immunoreactive ACTH in term placenta (author's transl)]. 626 17


<< Previous 1 2 3 4 5 6 7 Next >>