Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P20366 (substance P)
 21,176 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Antisera raised against porcine myelin basic protein (MBP) in Syrian hamsters were assayed by an ELISA method. The specificity of a high-titered antiserum was probed with synthetic peptides representing a hexapeptide and a decapeptide of the JC virus (JCV) large T-antigen C-terminus which is homologous to the MBP triproline region, a decapeptide from MBP which is encephalitogenic in guinea pigs, and peptides unrelated to MBP, i.e., substance P and poly-L-lysine. In an ELISA inhibition assay, preincubation of the hamster antiserum to MBP with either the JCV T-antigen C-terminal decapeptide or the encephalitogenic determinant inhibited binding activity in a dose-dependent manner. In contrast, the T-antigen C-terminal hexapeptide, substance P, and poly-L-lysine were not inhibitory. These results suggest that the triproline region of MBP can be immunogenic in hamsters, and support the concept that a conformation of the MBP triproline region is shared with certain of its viral homologues. In an effort to detect similar cross-reactive specificities in hamster antisera to JCV T-antigen, sera of 50 hamsters bearing subcutaneous tumors induced by JCV-transformed glial cells were tested for ability to bind to MBP in the ELISA assay. While significant increases in response compared to prebleed levels were observed in about one-fourth of the sera, some of them showed similar increases in binding to other basic proteins such as histones, and the binding to MBP was not inhibited by the triproline-containing decapeptide.
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PMID:Inhibition of binding of hamster antibody to myelin basic protein by a synthetic triproline-containing peptide from JC virus T-antigen. 243 49

In the present paper the effects of substance P (SP1-11, Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-MetNH2) and delta sleep inducing peptide (DSIP, Trp-Ala-Gly-Gly-Asp-Ala-Ser-Gly-Glu) to normalize the deprivation of sleep in chronically stressed rats with hyposomnia were investigated. The results indicated that SP1-11 is more potent than DSIP in rats with stress-induced hyposomnia. Different effects were found in the duration of sleep, the percentage of sleep phases compared to wake phases, the rhythm of sleep phases and the time periods of sleep-cycles. Based on the present results both the common and differences in the mode of action were discussed.
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PMID:[Comparison of the effects of DSIP and SP 1-11 on stress-induced chronic sleep disorders in rats]. 244 61

The substance Arg-Pro-Lys-Pro-(CH2)11CH3 [SP1-4C12] was synthesized by forming a peptide bond between Arg-Pro-Lys-Pro, the N-terminal sequence of substance P and dodecylamine. The aim was to examine the roles of the N- and C-terminal sequences of substance P in stimulating histamine release from mast cells of the rat peritoneal cavity. SP1-4 C12 induces concentration-dependent histamine release in the range 8 to 200 nM. SP1-4C12 was 50 times more potent than substance P and 300 times more potent than dodecylamine. Unlike dodecylamine itself, SP1-4C12 induced noncytolytic histamine release which was inhibited by benzalkonium chloride and by the substance P antagonist [D-Pro4,D-Trp7,9,10]SP4-11. Histamine release induced by SP1-4C12 was inhibited at temperatures below 16 degrees C and did not require the presence of extracellular calcium ions. It is suggested that substance P and some other basic histamine liberators initiate histamine secretion by a mechanism that involves the insertion of a hydrophobic region into the membrane lipid which is necessary to present positively charged moieties to a receptor site involved in activating the secretory mechanism.
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PMID:Histamine release induced by Arg-Pro-Lys-Pro(CH2)11CH3 from rat peritoneal mast cells. 244 99

We have compared the ability of anti-IgE, calcium ionophore A23187, substance P, compound 48/80, poly-L-lysine, and morphine to release histamine from mast cells of human skin, lung, adenoids, tonsils, and colon. Use of a single collagenase/hyaluronidase dispersion technique for all tissues has allowed comparisons of reactivity to be made that are free from methodological variations. Mast cells from all tissues examined secreted histamine in response to anti-IgE and calcium ionophore A23187. However, only skin mast cells were responsive to substance P, compound 48/80, poly-L-lysine, and morphine. Activation of human skin mast cells by these nonimmunologic stimuli clearly distinguishes them from the mast cells of human lung, adenoids, tonsils, and colon and is indicative of functional heterogeneity within the human mast cells population. We propose that the presence of functional receptor sites for neuropeptides and basic compounds on skin mast cells that are not present in mast cell populations from mucosal or lymphoid sources reflects a specialized role for these cells in vascular homeostasis.
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PMID:Human mast cell heterogeneity: histamine release from mast cells dispersed from skin, lung, adenoids, tonsils, and colon in response to IgE-dependent and nonimmunologic stimuli. 245 Jan 14

Using antisera specific for NH2-terminal and COOH-terminal regions of substance P and for the COOH-terminal region of neurokinin A, peptides with tachykinin-like immunoreactivity were isolated from extracts of chicken small intestine. The peptide Arg-Pro-Arg-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH2 differs from human substance P by substitution of the lysyl residue by an arginyl residue at position 3. Synthetic [Arg3]substance P showed identical chromatographic and immunochemical properties to chicken substance P and was equipotent with substance P in contracting the guinea pig ileum. A second peptide His-Lys-Thr-Asp-Ser-Phe-Val-Gly-Leu-Met-NH2 isolated from the extracts is identical to human neurokinin A. A third peptide was immunoreactive towards the COOH-terminally directed anti-serum to substance P only but was not characterized structurally in this study.
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PMID:[Arg3]substance P and neurokinin A from chicken small intestine. 245 61

The inflammatory neuropeptide substance P acted as a costimulant for macrophage CSF-1-induced clonal proliferation of murine marrow-derived two signal-dependent mononuclear phagocyte progenitors. Substance P had no effect on clonal proliferation by progenitors responding solely to CSF-1. Substance P fragment 2-11 had no costimulatory activity; however, SP fragment 1-4 retained the full activity of the parent undecapeptide. Fragment 1-4 (ARG-PRO-LYS-PRO), a peptide containing a PRO residue between two positive charges, is a tuftsin-like (THR-LYS-PRO-ARG) tetrapeptide, and tuftsin exerted an identical costimulatory effect. Substance P, SP:1-4, and tuftsin were optimally effective as costimulants at 10(-7) to 10(-6) M. (ALA1)-tuftsin, an inhibitory analog of tuftsin, was a potent negative regulator of two signal-dependent colony formation. (ALA1)-tuftsin at concentrations less than or equal to 10(-9) M exerted dose-dependent inhibition of the positive effects of optimal concentrations of all of the co-stimulants tested, including bacterial LPS. The inhibitory tetrapeptide was equivalent in activity to ferritin, an established inhibitor of two signal-dependent colony formation. The results indicated that SP may influence myelopoiesis in addition to its other inflammatory and immunopotentiating properties. In addition, a potentially valuable modulator of SP and LPS responses in this system, (ALA1)-tuftsin, was identified.
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PMID:Substance P augmentation of CSF-1-stimulated in vitro myelopoiesis. A two-signal progenitor restricted, tuftsin-like effect. 245 23

The N-terminal hexa- or pentapeptide sequences of the three mammalian tachykinins substance P, neurokinin A, and neurokinin B have been synthesized by the conventional solid-phase procedure with 6-aminocaproyl-S-(acetamidomethyl)cysteine as a C-terminal spacer and attachment function. A fourth sequence, with an additional N-terminal 6-aminocaproyl residue on the substance P-hapten sequence, was cyclized N- to C-terminally. For this purpose, a four-level protection scheme has been applied: BOC-TFA for N-terminal protection and cleavage; TFA-stable but HF-labile anchoring function and side-chain protection; S-acetamidomethyl for semipermanent thiol protection. The side chain amino function of Lys was protected with NO2Z, stable against HF but readily cleaved with hydrogenation. The hapten sequences were coupled to maleimidated BSA, after the Acm group was removed by mercury/hydrogen sulfide treatment. Mice immunized with the three linear hapten sequences produced sera that were specific in enzyme-linked immunosorbant assay for the presented hapten and the respective tachykinin but displayed no crossreactivity at all toward the other haptens nor to one of the other tachykinins. It is concluded that this approach produced antisera, specific and selective for its respective mammalian tachykinins.
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PMID:Synthesis and immunological evaluation of N-terminal, noncrossreactive tachykinin antigens. 245 85

Substance P was found to be an effective acyl donor substrate of transglutaminase in vitro, the reaction products having been examined by both sodium dodecyl sulfate-polyacrylamide gel electrophoresis and fast atom bombardment mass spectrometry. Electrophoretic experiments showed that Substance P incorporated 14C-labeled polyamines when incubated with purified guinea pig liver transglutaminase and Ca2+. Extensive use of fast atom bombardment mass spectrometry allowed to establish that: i) a 1:1 adduct Substance P-spermine is formed; ii) only a single glutamine residue out of two, i.e. Gln-5, acts as acyl donor, iii) the single lysine residue of the neuropeptide is unable to act as acyl acceptor. A direct analytical methodology to detect transglutaminase reaction products is described.
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PMID:Substance P as a transglutaminase substrate: identification of the reaction products by fast atom bombardment mass spectrometry. 246 Nov 17

The use of a collagenase dispersion technique has allowed us to compare size, histamine content and the secretory characteristics of mast cells from the mucosal and muscle layers of the human large intestine. Mast cells from the mucosa, which constituted 1.8% of the total nucleated cells, contained approximately equal numbers of formalin-sensitive and -insensitive mast cells. Those dispersed from the muscle layer constituted 3.2% of the total nucleated cells and were almost all formalin insensitive. The cells from both layers were similar with respect to size and mean cell histamine content. Anti-IgE released up to 15.1% and 16.5% of total cell histamine in the mucosa and muscle, respectively, with similar concentration-response characteristics. The kinetics of anti-IgE-induced release, however, were different, mucosal mast cells releasing histamine 55 seconds (P less than 0.05) faster than cells dispersed from intestinal muscle. Cells from both layers also released histamine in response to A23187 in a similar concentration-related fashion. Neither mucosal or muscle mast cells released significant amounts of histamine in response to compound 48/80, substance P, morphine, poly-L-lysine or f-met-leu-phe. Our results show intestinal mast cells possess secretory characteristics similar to those of human lung, adenoids and tonsils, but are different from human skin mast cells. The absence of significant histamine release in response to basic secretagogues from either layer of the human intestine contrasts with studies in the rodent intestine. Furthermore it suggests that in human mast cells, histochemical properties, protease content and secretory characteristics may not be closely associated.
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PMID:The secretory characteristics of mast cells isolated from the human large intestinal mucosa and muscle. 246 23

1. Human skin mast cells, unlike other human mast cells so far studied, released histamine in a concentration-related manner in response to substance P, vasoactive intestinal peptide (VIP) and somatostatin (1 microM to 30 microM). In contrast, eledoisin, physalaemin, neurokinin A, neurokinin B, calcitonin gene-related peptide (CGRP), neurotensin, bradykinin and Lys-bradykinin induced negligible histamine release. 2. The low histamine releasing activity of physalaemin, eledoisin, neurokinin A and neurokinin B relative to substance P suggests that the human skin mast cell activation site is distinct from the tachykinin NK-1, NK-2 or NK-3 receptors described in smooth muscle. 3. The relative potencies of substance P and its fragments SP2-11, SP3-11, SP4-11 and SP1-4 in releasing histamine from human skin mast cells suggests that both the basic N-terminal amino acids and the lipophilic C-terminal portion of substance P are essential for activity. 4. Peptide-induced histamine release, like that induced by compound 48/80, morphine and poly-L-lysine, is rapid, reaching completion in 10-20 s, is largely independent of extracellular calcium but requires intact glycolysis and oxidative phosphorylation. 5. The substance P analogue, [D-Pro4,D-Trp7,9,10] SP4-11 (SPA), not only reduced substance P-induced histamine release in a concentration-related manner but also inhibited that induced by VIP, somatostatin, compound 48/80, poly-L-lysine and morphine but not anti-IgE. 6. The similar characteristics of histamine release induced by substance P, VIP, somatostatin, compound 48/80, poly-L-lysine and morphine suggest that they share a common pathway of activation-secretion coupling distinct from that of IgE-dependent activation. Furthermore, the ability of human skin mast cells to respond to basic non-immunological stimuli including neuropeptides may reflect a specialised function for these cells.
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PMID:Characterization of neuropeptide-induced histamine release from human dispersed skin mast cells. 246 82


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