Abstract
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.
MeSH terms
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Animals
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Autoradiography
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Clusterin
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Complement Membrane Attack Complex / metabolism
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Cross-Linking Reagents / pharmacology
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Extracellular Matrix Proteins / metabolism
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Glycoproteins / metabolism*
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Glycoproteins / pharmacology
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Humans
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In Vitro Techniques
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Iodine Radioisotopes
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Molecular Chaperones*
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Nerve Tissue Proteins / metabolism*
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Nerve Tissue Proteins / pharmacology
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Protein Binding
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Rats
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Receptors, Opioid / drug effects
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Receptors, Opioid / metabolism
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Vitronectin
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beta-Endorphin / metabolism*
Substances
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CLU protein, human
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Clusterin
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Complement Membrane Attack Complex
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Cross-Linking Reagents
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Extracellular Matrix Proteins
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Glycoproteins
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Iodine Radioisotopes
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Molecular Chaperones
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Nerve Tissue Proteins
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Receptors, Opioid
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Vitronectin
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beta-Endorphin