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)

Human beta-endorphin (1-31) (beta H-endorphin) was found to specifically interact with purified complement S protein from human plasma. As found by chemical cross-linking beta H-endorphin bound to both, the 65- and 75-kDa molecular mass forms of S protein. The interaction of S protein with heparin as well as the adsorption of S protein to surfaces led to an almost 10-fold increase of specific binding which was due to the exposure of further beta H-endorphin-binding sites. The interaction of beta H-endorphin with S protein bore characteristics of a ligand-receptor interaction, such as time dependence, reversibility, high affinity, saturability, and structural specificity and was mediated through the non-opioid COOH terminus of the beta H-endorphin molecule. beta H-Endorphin binding to S protein was observed at physiological pH or cation concentrations, indicating that the interaction may well occur in vivo. Our results provide conclusive evidence that interactions of S protein with very different effectors led to similar conformational changes which uniformly resulted in exposure of a highly specific beta H-endorphin binding domain on S protein. With S protein as major beta H-endorphin-binding protein in the periphery, the molecular basis of a widespread system of humoral target sites of the neuroendocrine effector appears to be established. In view of S protein involvement in processes of inflammation and wound repair and beta-endorphin effects on immunocompetent cells, the demonstrated S protein-beta H-endorphin interaction appears to be of considerable functional significance.
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PMID:A novel beta-endorphin binding protein. Complement S protein (= vitronectin) exhibits specific non-opioid binding sites for beta-endorphin upon interaction with heparin or surfaces. 247 99

We have characterized the specific binding of human beta-endorphin (1-31) to novel binding sites which are formed in human plasma or serum in the presence of heparin. The formation of the binding sites is temperature-dependent and does not occur in the presence of other anticoagulants, such as sodium-EDTA, sodium-oxalate, or sodium-citrate. The specific binding of 125I-beta H-endorphin to heparin-induced binding sites in human plasma is saturable and reversible. It is not inhibited by morphine or naloxone or by various opioid peptides which share their NH2-terminal opioid-active sequence with beta H-endorphin. In contrast, binding is inhibited by the COOH-terminal beta H-endorphin fragment Gly-Glu indicating that binding is to nonopioid sites. Electroimmunoprecipitation techniques revealed that these binding sites are identical with S protein/vitronectin or derivatives thereof. S protein is a plasma alpha 1-glycoprotein involved in attachment and spreading of cells and also in blood coagulation and complement activation. It is possible that the interaction of beta-endorphin with S protein is of physiological significance.
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PMID:Characterization and identification of heparin-induced nonopioid-binding sites for beta-endorphin in human plasma. 282 69

This study deals with the interaction of polypeptide hormones with their receptors. Specifically it involves the binding of synthetic ACTH analogs and fragments to a particulate fraction from beef adrenal cortical tissue. This fraction was found to bind synthetic [(14)C-Phe] [Gln(5)]beta-corticotropin(1-20) amide but failed to bind significant amounts of [(14)C-Phe] [Gln(5)]beta-corticotropin(1-10). The former peptide exhibits a high degree in vivo adrenocorticotropic activity in the rat; the latter is inactive. [(14)C-Phe] [Gln(5)]beta-corticotropin(1-20) amide exhibited little affinity for similarly prepared particulates from beef kidney, liver, or adrenal medulla. Using a series of synthetic homogeneous nonradioactive analogs or fragments of beta-corticotropin(1-20) amide to displace [(14)C-Phe] [Gln(5)]beta-corticotropin(1-20) amide from the particulate fraction a significant correlation between binding and in vivo adrenocorticotropic activity was established. Major "active" and "binding" sites were shown to reside in different sections of the ACTH molecule. Charged groups play a major role in the attachment of ACTH to the particulate fraction and the sequence Lys-Lys-Arg-Arg proved to be particularly significant. The high degree of binding specificity for ACTH peptides which is exhibited by the particulate suggests that it contains ACTH receptor(s). Moreover, the striking similarity between observations with the S-peptide-S-protein model system and the system described would seem to indicate that the ACTH receptor is a protein.
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PMID:Correlation of adrenocorticotropic activity of ACTH analogs with degree of binding to an adrenal cortical particulate preparation. 433 21

We have characterized the binding of 125I-labeled human beta-endorphin (125I-beta H-endorphin) to sites present on the terminal fluid-phase complex of human complement, consisting of complement components C5b, C6, C7, C8, C9, and the S-protein (SC5b-9 complex). Specific binding exhibited saturability, reversibility, structural specificity, temperature dependence, and absence of negative cooperative effects. Binding was maximal at 4 degrees C and pH 7.0; it was diminished by monovalent and divalent cations as well as by increasing concentrations of urea and Triton X-100 and apparently required intact disulfide groups. Binding was not inhibited by a number of opioid peptides sharing common sequences with the NH2 terminus of beta H-endorphin. In contrast, binding was inhibited by beta H-endorphin, N-acetyl-beta H-endorphin, and a series of COOH-terminal beta H-endorphin fragments, where of the COOH-terminal dipeptide Gly-Glu represented the minimal effective structure. Stepwise extension towards the NH2 terminus led to an increased binding affinity of the respective fragment. Computer resolution of competition curves yielded one binding component for several shorter COOH-terminal beta H-endorphin fragments and for beta H-endorphin (1-5) + (16-31), whereas two distinct binding components were obtained when beta H-endorphin (27-31), beta H-endorphin (6-31), N-acetyl-beta H-endorphin or beta H-endorphin were used as inhibitors. This study presents detailed data on the binding of COOH-terminal beta H-endorphin fragments to specific nonopiate binding sites present on the terminal SC5b-9 complex of human complement. We suggest that through this interaction, beta H-endorphin may modulate certain functions within the immune system.
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PMID:Interaction of human beta-endorphin with nonopiate binding sites on the terminal SC5b-9 complex of human complement. Significance of COOH-terminal beta H-endorphin fragments. 631 49

SP-40,40 bound to beta-endorphin via C-terminal non-opioid portion of beta-endorphin as well as S-protein (vitronectin) bound. Beta-endorphin bound mainly to SP-40,40, but not to S-protein, in the soluble membrane attack complex (SMAC, SC5b-9) of complement, because the results of autoradiography of the cross-linking experiment of SMAC with [125I] beta-endorphin revealed only a typical band of SP-40,40. The binding of SP-40,40 to beta-endorphin inhibited the binding of beta-endorphin to its receptor of rat brain; thus SP-40,40 might inhibit the biological action of beta-endorphin.
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PMID:Beta-endorphin binding activity of SP-40,40. 768 89

Vitronectin is a multifunctional plasma glycoprotein which may regulate the systems related to protease cascades such as the coagulation, fibrinolysis, and complement systems as well as cell adhesion. Solid-phase assays and affinity chromatography on immobilized glycolipids indicated that vitronectin purified under denaturing conditions bound to sulfatide (Gal(3-SO4)beta1-1ceramide), cholesterol 3-sulfate, and various phospholipids, but not gangliosides. Only the unfolded or multimeric form of vitronectin bound to sulfatide, suggesting a conformational dependency of the binding activity, while vitronectin bound to cholesterol 3-sulfate regardless of its conformational state. The recombinant domains of human vitronectin and mutants with certain domains deleted were separately expressed in E. coli as fusion proteins. Using the recombinants, sulfatide-, phosphatidylserine-, cholesterol 3-sulfate-, Type I collagen-, heparin-, and beta-endorphin-binding activities were found to be attributable to hemopexin domain 2 and hemopexin domain 1. The possibility was suggested that the presence of a somatomedin domain and/or connecting region flanking hemopexin domain 1 inactivated its heparin binding. De-N-glycosylation of plasma vitronectin significantly affected the cholesterol sulfate- and collagen-binding activities, although its effects were opposite. These findings suggest that diverse ligand-binding activities could be attributed to pexin family motifs but that the interdomain interactions and glycosylations modulate the ligand binding activities of vitronectin.
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PMID:Characterization of the ligand binding activities of vitronectin: interaction of vitronectin with lipids and identification of the binding domains for various ligands using recombinant domains. 957 50

This study was designed to examine the role of opioids on cell migration, chemotaxis, invasion, and adhesion, with an emphasis on whether the opioid growth factor (OGF, [Met(5)]-enkephalin) or the opioid antagonist naltrexone (NTX) impacts any or all of these processes. Drug concentrations of OGF and NTX known to depress or stimulate, respectively, cell proliferation and growth were analyzed. Three different human cancers (pancreatic, colon, and squamous cell carcinoma of the head and neck), represented by seven different cancer cell lines (PANC-1, MIA PaCa-2, BxPC-3, CAL-27, SCC-1, HCT-116, and HT-29), were evaluated. In addition, the influence of a variety of other natural and synthetic opioids on cell motility, invasion, and adhesion was assessed. Positive and negative controls were included for comparison. OGF and NTX at concentrations of 10(-4) to 10(-6)M, and dynorphin A1-8, beta-endorphin, endomorphin-1, endomorphin-2, leucine enkephalin, [D-Pen(2,5)]-enkephalin (DPDPE), [D-Ala(2), MePhe(4), Glycol(5)]-enkephalin (DAMGO), morphine, and U69,593 at concentrations of 10(-6)M, did not alter cell migration, chemotaxis, or invasion of any cancer cell line. OGF and NTX at a concentration of 10(-6)M, and incubation for 24 or 72h, did not change adhesion of these cancer cells to collagen I, collagen IV, fibronectin, laminin, or vitronectin. Moreover, all other opioids tested at 10(-6)M concentrations and for 24h had no effect on adhesion. These results indicate that the inhibitory or stimulatory actions of OGF and NTX, respectively, on cell replication and growth are independent of cell migration, chemotaxis, invasion, and adhesive properties. Moreover, a variety of other exogenous and endogenous opioids, many specific for the micro, delta, or kappa opioid receptors, also did not alter these biological processes, consonant with previous observations of a lack of effects of these compounds and their receptors on the biology of cancer cells.
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PMID:Opioids and migration, chemotaxis, invasion, and adhesion of human cancer cells. 1791 Aug 95