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

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

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

1. Cells were dispersed from human foreskin using a mixture of collagenase and hyaluronidase and separated into mast cell-depleted (less than 1%) or enriched (greater than 75%) preparations by density-gradient centrifugation. 2. Challenge of gradient fractions with epsilon-chain-specific anti-human IgE stimulated the release of histamine, prostaglandin D2 (PGD2) and leukotriene C4 (LTC4). The release of eicosanoids was significantly correlated with that of histamine, suggesting that they are derived from the mast cell population of the dispersate. In highly purified (76.2 +/- 4.2%) mast cell preparations, maximum net release of histamine, PGD2 and LTC4 was 3432 +/- 725, 84.9 +/- 10.8 and 6.6 +/- 1.2 pmol/10(6) nucleated cells. 3. The non-immunological stimuli substance P, vasoactive intestinal peptide (VIP), somatostatin, compound 48/80, morphine and poly-L-lysine released similar amounts of histamine to anti-IgE, but 12 to 21 fold less PGD2 and LTC4. 4. These studies suggest that IgE-dependent and non-immunological stimuli activate human skin mast cells by different secretory mechanisms, a hypothesis supported by our previous findings of differences in Ca2+ requirements and time-course of histamine release. Activation by the non-immunological mechanism may be of importance in vivo due to the close anatomical association between skin mast cells and dermal nerve-terminals containing neuropeptides.
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PMID:Differential release of histamine and eicosanoids from human skin mast cells activated by IgE-dependent and non-immunological stimuli. 247 53

An improved protocol for the internal radiolabelling of monoclonal antibodies with tritiated lysine is described. Hybridoma cell lines producing monoclonal antibodies against the biosynthetic enzyme tyrosine hydroxylase and the neuropeptides, substance P and enkephalin, were employed in this investigation. Immunocytochemical detection of the endogenous antigens with these internally labelled antibodies was performed and when used in immunocytochemistry, the subsequent data were in complete agreement with previous light and electron microscopic studies. These results indicate that the present internal radiolabelling procedure does not alter the ability of the monoclonal antibody to recognise the endogenous antigen. This study, therefore, supports the use of internally labelled antibodies with compatible immunocytochemistry techniques in double staining procedures.
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PMID:Immunocytochemical use of internally radiolabelled monoclonal antibodies against tyrosine hydroxylase, substance P and enkephalin. 247 61

Highly specific radioimmunoassays (RIAs) for neurokinin A (NKA) and neurokinin B (NKB) were developed. Antisera were produced by the procedure which involved immunization with NKA or NKB, both conjugated with keyhole limpet hemocyanin, and treatments with a tolerogenic conjugate of kassinin and a copolymer of D-glutamic acid and D-lysine (D-GL) to inhibit the production of cross-reactive antibodies against common C-terminal region of tachykinins. Cross-reactivities of anti-NKA antiserum (R704), thus produced, with NKB, kassinin, eledoisin were 12.6%, 10.6% and 11.5%, respectively. This was in sharp contrast with those of antiserum obtained from the rabbit not treated with kassinin-D-GL, these values corresponding to 129.0%, 42.5% and 94.4%, respectively. The cross-reactivities of R704 with substance P and physalaemin were 0.3% and 1.5%, respectively. This antiserum also bound 35.6% of neuropeptide K which contains NKA at its C-terminal. More importantly, anti-NKB antiserum (R707) obtained by the above tolerizing regimen was highly specific for NKB and the cross-reactivities with NKA, neuropeptide K, kassinin and other tachykinins were all less than 0.001%. RIAs using these specific antisera allowed us to measure directly NKA and NKB in tissue extracts without their fractionation by chromatography prior to RIAs. Measurements of immunoreactive NKA and NKB in different rat brain regions and spinal cord revealed that they are present with various ratios (NKA/NKB: 1.1-9.9) depending on the region.
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PMID:Establishment of highly specific radioimmunoassays for neurokinin A and neurokinin B and determination of tissue distribution of these peptides in rat central nervous system. 254 May 12

Explants and cell cultures of embryonic chick ganglia trigeminalia, telencephalon and retina or hippocampus from fetal rats were incubated in maximow chambers in the presence of cyclic AMP and the dipeptide cyclo(Lys-Pro).HCL under various conditions. Maintenance of nerve cells and growth of nerve fibers were observed by morphometrical methods. 1. Cyclo(Lys-Pro).HCL promoted the maintenance of neuroblasts and the growth of nerve fibres in explants of the ganglion trigeminal and retinal cell cultures. The effect depended on the presence of serum in the medium by use of poly-I-lysine substrate. 2. Extern applicated cyclic AMP and the dipeptide SP3-4 = cyclo(Lys-Pro).HCL facilitated neurite growth in PNS cultures. In the presence of the drugs the length of nerve fibers increased for a short term. On CNS explants substance P (SP1-11) and SP3-4 were without effect. Cyclic AMP stimulated the growth of nerve fibers in CNS explants and cell cultures in number and length. 3. Discussed is the effect of SP1-11 and cyclo(Lys-Pro).HCL for competence of nerve fibre regeneration in vitro in relation to increasing cAMP levels, which may then act as an initial second messenger. It is suggested that explants and cell cultures of nervous tissues will be useful as a tool for the further characterisation of factors with neuronotrophic activities.
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PMID:[Effects of cyclic adenosine-3',5'-monophosphate and cyclo(Lys-Pro).HCl neuronotrophic factors in tissue culture]. 282 94

Low concentrations of six peptide hormones; glucagon, vasoactive intestinal peptide, substance P, angiotensin II, lysine-vasopressin, arginine-vasopressin, and the chemotactic peptide fMet-Leu-Phe, activated the capacity for pinocytosis in starved Amoeba proteus. Competitive inhibitors of the chemotactic peptide in leucocytes inhibited activation by fMet-Leu-Phe, suggesting that its action in the amoeba is mediated by specific receptors. The opioid peptides, beta-endorphin, dynorphin (1-13) and leu-enkephalin abolished through a naloxone-sensitive mechanism activation by hormones and several other activating agents. Also, low concentrations of beef and pork insulin inhibited activation by peptide hormones. An insulin analogue of low potency in mammalian cells was inactive in the amoeba. These results support the hypothesis that besides opioid receptors, there may be insulin receptors and possibly receptors for several other peptide hormones in Amoeba proteus.
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PMID:Peptides as modifiers of Na+-induced pinocytosis in starved Amoeba proteus. 300 25


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