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)

To elucidate further the pathogenesis of steroid-induced ulceration, plasma gastrin levels, both basal and after a test meal, were studied in normal volunteers and patients treated with glucocorticoids or corticotropin. In normal subjects the acute intravenous administration of 100 mg prednisolone had no effect on plasma gastrin levels. After oral administration of prednisolone (40 mg daily, for four days) a significant increase of the basal, the reactive, and the over 90-min integrated gastrin release was observed. In this group, the glucocorticoid treatment had a slight, but significant influence on gastric acid and pepsin secretion, while acidity and pepsin output stimulated by pentagastrin was not affected. In patients treated with prednisolone for more than 24 weeks, the oral administration of this hormone failed to alter basal gastrin values but affected significantly secretion after the test meal. In patients with multiple sclerosis, after intramuscular administration of corticotropin (60 IU daily, for 12 days), an increase of the basal, the reactive, and the integrated gastrin release also was found. Glucocorticoid-induced hypergastrinemia provides information on the pathogenesis of steroid-induced ulceration.
 ...
PMID:Hypergastrinemia induced by glucocorticoid and corticotropin treatment in man. 18 Jul 97

The corticotropins from two species of whales, e. g. seiwhale (Balaenoptera borealis) and finwhale (Balaenoptera physalus) were subjected to hydrolysis by trypsin, chymotrypsin and pepsin. The peptide fragments were separated by gel-filtration through Sephadex and partition paper chromatography. The study of the amino acid sequence of the peptides obtained allowed to establish the primary structure of corticotropin from both species, which was found structurally identical to human corticotropin.
 ...
PMID:[Amino acid sequence of corticotropins from seiwhale (Balaenoptera borealis) and pinwhale (Balaenoptera physalus)]. 20 8

Ovine corticotropin (alpha s-ACTH) was enzymatically methylated with purified calf brain protein methylase II (protein O-methyltransferase; S-adenosyl-L-methionine: protein-carboxyl O-methyltransferase, EC 2.1.1.24) and S-adenosyl-L-[methyl-14C]methionine. After incubation for 60 min at 37 degrees C, 30 mol % of the hormone was methylated on the basis of the [14C]methyl incorporation. In order to assess the location of methylation, the modified peptide was digested with pepsin. Analytical results derived from studies on the peptic digest led to the suggestion that the alpha s-ACTH-(6--28) peptide fragment was esterified. Because there is only one available methylation site at Glu-28, these results indicate that Glu-28 of alpha s-ACTH was specifically methyl esterified to yield [Glu(OMe)28]-alpha s-ACTH.
 ...
PMID:Enzymatic methyl esterification of specific glutamyl residue in corticotropin. 22 92

Peptides with opioid activity are found in pepsin hydrolysates of wheat gluten and alpha-casein. The opioid activity of these peptides was demonstrated by use of the following bioassays: 1) naloxone-reversible inhibition of adenylate cyclase in homogenates of neuroblastoma X-glioma hybrid cells; 2) naloxone-reversible inhibition of electrically stimulated contractions of the mouse vas deferens; 3) displacement of [3H]dihydromorphine and [3H-Tyr, dAla2]met-enkephalin amide from rat brain membranes. Substances which stimulate adenylate cyclase and increase the contractions of the mouse vas deferens but do not bind to opiate receptors are also isolated from gluten hydrolysates. It is suggested that peptides derived from some food proteins may be of physiological importance.
 ...
PMID:Opioid peptides derived from food proteins. The exorphins. 37 81

The influence of proteinase inhibitors on the lipolytic effect of the pituitary polypeptide hormones and epinephrine in an isolated adipose tissue of rabbits and rats has been studied. Neither of proteinase inhibitors changed the basal rate of lipolysis. Trasylol, a serine proteinase inhibitor, suppressed completely growth hormone (GH) effect and partially reduced the effect of adrenocorticotropin (ACTH) and beta-lipotropin (beta-LPH) but did not change the effect of epinephrine. Bacitracin proved ineffective with regard to the effect of polypeptide hormones. Pepstatin, an acid proteinase inhibitor, partially blocked the stimulation of lipolysis by ACTH without affecting the effect of GH and beta-LPH. The influence of proteinase inhibitors on the ACTH effect in rat adipose tissue was similar to that found in rabbit tissue. The Trasylol-induced inhibition of the hormone-stimulated lipolysis decreased to a considerable extent after GH or ACTH incubation with rabbit plasma or partial GH digestion with pepsin. This decrease was not observed when plasma serine proteinases were blocked during GH incubation with plasma. The results demonstrate an involvement of some proteolytic enzymes in the realization of the polypeptide hormone lipolytic effect and permit to suppose the requirement of preliminary activation of the hormones by means of proteolytic modification.
 ...
PMID:Involvement of proteolytic enzymes in the lipotropic effect of the pituitary polypeptide hormones. 242 65

Two analogues of alpha-MSH (Ac-Ser-Tyr-Ser-Met-Glu-His-Phe-Arg-Trp-Gly-Lys-Pro-Val-NH2), Ac-[Nle4, Asp5, D-Phe7, Lys10]alpha-MSH4-10NH2 and Ac-[Nle4, Asp5, D-Phe7, Lys10] alpha-MSH4-10-NH2, were synthesized, and the melanotropic activities of the peptides were compared in several bioassays. Potencies were determined in the in vitro frog and lizard skin bioassays and in the S91 melanoma cell tyrosinase assay. Both analogues were equipotent or more potent than alpha-MSH in all bioassays, and the activities of the analogues were prolonged compared to alpha-MSH. The two analogues were very resistant to inactivation by purified proteolytic enzymes (alpha-chymotrypsin, trypsin, and pepsin). The two peptides could be topically applied and transdermally delivered across the skin of mice in vivo, resulting in a shift from pheomelanogenesis to eumelanogenesis within follicular melanocytes. The cyclic analogue exhibited greater potency, prolonged activity, and stability against enzyme inactivation than did the linear peptide. The significance of the findings for the further design of melanotropin analogues is discussed, as in the possible relevance of these melanotropin analogues for use in biomedical studies.
 ...
PMID:Linear and cyclic alpha-melanotropin [4-10]-fragment analogues that exhibit superpotency and residual activity. 255 3

Anti-alpha-corticotropin [anti-ACTH alpha (1-13)](also alpha-melanotropin) and anti-gamma-endorphin antisera neutralized human leukocyte interferon activity but not fibroblast interferon activity. Human leukocyte interferon was not neutralized by anti-human lutenizing hormone (lutropin) or follicle-stimulating hormone (follitropin) antisra. Conversely, antisera to human leukocyte interferon neutralized ACTH activity. The neturalization of human leukocyte interferon by anti-human leukocyte interferon serum was partially blocked by ACTH. These studies show strong antigenic relatedness among human leukocyte interferon, ACTH, and endorphins, implying that there are underlying structural similarities. Structural relatedness is shown by pepsin cleavage of ACTH activity from human leukocyte interferon. The implication for the natural functions of human leukocyte interferon are discussed.
 ...
PMID:Human leukocyte interferon: structural and biological relatedness to adrenocorticotropic hormone and endorphins. 616 May 89

Human leukocyte interferon (hIFN-alpha) preparations contain immunologically and biologically recognizable endorphin and corticotropin-like (ACTH-like) activities. The ACTH bioactivity was demonstrable only after pepsin or acid treatment. Highly purified hIFN-alpha was composed of two molecular species of interferon (18,500 and 23,000 daltons). Endorphin activity was associated with both of these molecules. Pepsin treatment of the 23,000-dalton but not the 18,500-dalton hIFN-alpha generated ACTH activity. In acid, the 23,000-dalton hIFN-alpha broke down into the 18,500-dalton form and ACTH (4500 daltons). The ACTH derived from hIFN-alpha by pepsin digestion comigrated with a purified ACTH standard in NaDodSO4/polyacrylamide gel electrophoresis. hIFN-alpha-producing lymphocytes showed positive immunofluorescence after staining with highly specific antisera to ACTH alpha-(1-13) and gamma-endorphin. Essentially 100% of the human peripheral lymphocytes were capable of producing both ACTH and gamma-endorphin-related substances, presumably associated with hIFN-alpha. These results strongly suggest a circuit between the immune and neuroendocrine systems which involves neuroendocrine hormone-like substances, some of which are associated with hIFN-alpha
 ...
PMID:Human lymphocyte production of corticotropin and endorphin-like substances: association with leukocyte interferon. 617 75

Sequential similarities between the tryptophan peptide of myelin basic protein (residues 111-121), luteinizing hormone releasing hormone, melanotropin, adrenocorticotropin (residues 1-13), human leukocyte interferon (residues 28-40), and various segments of human and bovine serum albumin and hen ovalbumin are presented. It is suggested that these structural similarities may explain observations concerning common functional characteristics such as serotonin modulation, immunological activity with the adjuvant muramyl dipeptide, immunological cross-reactivity, and the possible MSH-ACTH-like activity of a pepsin-derived peptide of interferon.
 ...
PMID:'Molecular sandwiches' as a basis for structural and functional similarities for interferons, MSH, ACTH, LHRH, myelin basic protein, and albumins. 620 49

The effects of met-enkephalin and morphine on gastric acid and pepsin secretion and gastric mucosal and total blood flow were studied in anaesthetized dogs with an in vivo chambered secretion stomach preparation. It was found that both agents infused intraarterially caused an increase in histamine-induced acid and pepsin secretion and mucosal and total blood flow. The above responses were significantly blocked by naloxone and nalorphine. In the resting stomach both opiates did not induce secretory changes but they increased mucosal and total blood flow. Met-enkephalin and morphine were also effective after intravenous administration. Met-enkephalin but not morphine fails to stimulate acid secretion if given into the portal vein. The likely mechanism of action of opiates on gastric secretion is discussed and a hypothesis of existence of opiate receptors in the gastric wall is presented.
 ...
PMID:Effect of met-enkephalin and morphine on gastric secretion and blood flow. 627 49


1 2 Next >>