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)

The nucleotide sequence of a 1,091-base pair cloned cDNA insert encoding bovine corticotropin-beta-lipotropin precursor mRNA is reported. The corresponding amino acid sequence indicates that the precursor protein consists of repetitive units and includes a third melanotropin sequence in its cryptic portion. Pairs of lysine and arginine residues separate the component peptides of the precursor.
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PMID:Nucleotide sequence of cloned cDNA for bovine corticotropin-beta-lipotropin precursor. 22 18

Beta-Endorphin has been reported to specifically interact with SC5b-9 complement complexes via non-opioid binding sites. Covalent cross-linking of [125I]beta H-endorphin to SC5b-9 and analysis of the cross-linking products by gel electrophoresis and subsequent autoradiography revealed a single specifically labelled species which was identical with the S protein subunit of the complement complex. In contrast to SC5b-9, no cross-linking of labelled beta-endorphin to subunits of C5b-9(m) could be observed, indicating that beta-endorphin binding to SC5b-9 was mediated exclusively via S protein. Beta-Endorphin binding to SC5b-9 was compared with binding to purified S protein. Whereas beta-endorphin binding to purified S protein was only modest, complex formation of S protein with complement proteins led to a strong increase in beta-endorphin-binding site concentration, compatible with the exposure of primarily cryptic beta-endorphin-binding sites on S protein.
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PMID:Identification of the beta-endorphin-binding subunit of the SC5b-9 complement complex: S protein exhibits specific beta-endorphin-binding sites upon complex formation with complement proteins. 246 72

Several reports indicate that enkephalins participate in lymphocyte proliferation and several events of the immune response. It has been proposed that peptides involved in these processes may originate in the nervous system or endocrine glands. We have found that human peripheral blood lymphocytes (PBL) activated with a mitogenic agent contain and release proenkephalin derived peptides. The kinetics of met-enkephalin and cryptic products of proenkephalin in PBL activated with phytohemaglutinin (PHA) were studied. Peptides were released to the supernatant of stimulated PBL, reaching the highest values after 18 to 24 hours. The material secreted corresponds to high, intermediate and low molecular weight peptides derived from proenkephalin, displaying met-enkephalin and synenkephalin (proenkephalin 1-70) immunoreactivity. Therefore, an intrinsic lymphocytic proenkephalin system is induced by PHA and may play an important role in the regulation of the immune response.
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PMID:Mitogenic activation of the human lymphocytes induce the release of proenkephalin derived peptides. 259 69

MTC is characterized by multiple humoral and hormonal manifestations. Although calcitonin is the specific marker of the disease, somatostatin, the pro-opiomelanocortin derived peptides and bombesin--among hormones produced by the tumor--can represent an exacerbation of normal C cells potentialities through genome derepression induced by the cancer. In this paper, the functional polymorphism of princeps tumoral markers and the endocrinological aspects of this neoplasia are reviewed. Molecular biology has been instrumental in discovering new tumoral peptides ("ancestral" CT forms, cryptic peptide and CGRP) and methods of CT detection; therefore, the role of CT could be better evaluated. In addition to its calciotropic role, CT acts also as a neuromodulator on some hypophyseal hormones. Conversely, CT secretion is also regulated by amines and neuropeptides, providing the basis of potential hormonal treatment.
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PMID:[Tumor markers of medullary cancer of the thyroid body. Basic and endocrine aspects]. 290 Jun 20

Region-specific antisera to three enkephalins: met-enkephalin, met-enkephalin-Arg6-Phe7 and met-enkephalin-Arg6-Gly7-Leu8, together with four region specific antisera to progastrin: C-terminal G17 specific, N-terminal G34 specific, cryptic peptides A- and B-specific, were used in immunohistochemical studies of hog antral mucosa. A sub-population (6-10%) of the gastrin-containing endocrine cells (G-cells) was found to react with antisera to met-enkephalin, met-enkephalin-Arg6-Phe7 and met-enkephalin-Arg6-Gly7-Leu8. About 30% of all the enkephalin-containing cells were identified as G-cells. The results indicate that a fraction of G-cells produces both enkephalin-like peptides and gastrin.
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PMID:Occurrence of met-enkephalin, met-enkephalin-Arg6-Phe7 and met-enkephalin-Arg6-Gly7-Leu8 in gastrin cells of hog antral mucosa. 399 57

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.
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PMID:Pituitary immunoreactive gamma-melanotropins are glycosylated oligopeptides. 610 Dec 29

Using a specific radioimmunoassay for gamma-MSH, a predicted peptide in the cryptic N-terminal portion of the adrenocorticotropin-beta-lipotropin precursor, gamma-MSH-like immunoreactivity (gamma-MLI) was detected in two ectopic ACTH producing tumors. Gel chromatographic studies on Bio-Gel P-60 revealed one or two peaks of gamma-MLI; one was eluted near th elution position of beta-LPH, compatible with gamma-MLI in human pituitary and the other emerged near the position of beta-endorphin. These results indicate that ectopic ACTH-producing tumors eleborate not only ACTH, beta-endorphin but also gamma-MLI.
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PMID:Evidence for gamma-MSH-like immunoreactivity in ectopic ACTH-producing tumors. 624 46

gamma-Melanotropin (gamma-MSH), a putative peptide residing in the cryptic N-terminal portion of ACTH-beta-LPH precursor, shares several amino acid residues with alpha-MSH or beta-MSH. The present study revealed that gamma-MSH and structurally related peptides had as potent an affinity for rat brain opiate receptors as did ACTH1-24 when 3H-naloxone was used as a ligand. Thus, gamma-MSH and structurally related peptides may have physiological significance in the activities of the CNS.
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PMID:'gamma-MSH' fragments from ACTH-beta-LPH precursor have an affinity for opiate receptors. 624 15

The most obvious function of the pars intermedia in lower vertebrates is the secretion of melanocyte-stimulating hormone (MSH) for the purpose of pigmentary control. In some amphibia, elasmobranchs and teleosts, the histological study of the pars intermedia, the radioimmunoassay of pituitary and plasma MSH and the effects of hypophysectomy and of MSH injection suggest that the activity of the pars intermedia is regulated to satisfy the needs of cryptic colour change. MSH secretion is associated with dispersion of melanin granules and with melanogenesis. However, in other teleost species, both the evidence from pituitary cytology and the failure to respond to MSH injection suggest that pigmentary change is not regulated by changes in the plasma titres of MSH. Results discussed here indicate that MSH alone may be inadequate for pigmentary control. Evidence for non-pigmentary functions of the pars intermedia is circumstantial and fragmentary. It is based on cytological observations of altered pars intermedia activity under certain conditions, and on observations of physiological changes that accompany increased melanotropic activity. Such function include effects of plasmas titres of cortisol in teleosts, resistance to adrenaline-induced hyperglycaemia in toads, and effects on neural activity in fish and amphibia. Evidence for pars intermedia involvement in osmoregulation is briefly discussed.
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PMID:Biological role of the pars intermedia in lower vertebrates. 691 95

It is well established that ACTH and beta-lipotropin (LPH) originate from a common precursor molecule. Recently the complete complementary DNA sequence of the bovine precursor was reported, and within the cryptic sequence of this molecule is a third melanocyte stimulating hormone (MSH) region tentatively named gamma-MSH. The signal peptide of this molecule consists of 26 amino acids in both the rat and mouse. Pulse-chase experiments using both rat and mouse pituitary cells, showed the gradual maturation of this common precursor to proceed via the initial cleavage of the carboxy terminal beta-LPH, followed by release of ACTH, leaving an NH2-terminal extension of about 105 amino acids, which does not seem to undergo appreciably further maturation. It is within the sequence of this NH2-terminal extension that gamma-MSH is located. It is not yet clear what the biological role of this molecule is and whether gamma-MSH itself is released. Recently, it was shown that a synthetic 12 amino acid bovine gamma-MSH fragment possessed very little melanophore-stimulating activity as compared to alphs-MSH. We report here the successful purification of the human NH2 terminal cryptic peptide, its amino acid composition and present some of its tryptic fragments. The data show that human and bovine gamma-MSH have indentical amino acid composition.
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PMID:A novel human pituitary peptide containing the gamma-MSH sequence. 718 26


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