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)

Substance P (SP) binding protein of rat brain was solubilized by digitonin. The solubilized proteins were then purified by sequential gel filtration, concanavalin A lectin Sepharose, and SP-affinity chromatography. The calculated molecular weight of this purified SP binding protein was 76-74 kDa on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The rabbits were immunized with the purified protein and resulting polyclonal anti-sera were tested. The immune serum significantly inhibited [3H]SP binding to the 3-[(3-cholamidopropyl)dimethylammonio]-1-propane sulfonate solubilized membrane fractions from rat brain, whereas pre-bleed antiserum failed to inhibit the binding. This polyclonal antibody also inhibited the activity of 45Ca influx into astroglioma cells stimulated by SP, but does not inhibit that stimulated by histamine. Furthermore, this polyclonal antibody recognized the 76-74 kDa band as assessed by Western blotting. These data strongly suggest that this polyclonal antibody could recognize a part of the natural SP receptor site.
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PMID:Isolation of substance P binding protein from rat brain. 127 54

Several distinct populations of sensory neurons in the ophthalmic region of the mouse trigeminal ganglion have been identified by their reactivity to antibodies raised against substance P (SP), calcitonin gene-related peptide (CGRP), cell-surface glycoconjugates SSEA3 and LD2, and the plant lectin, Bandeiraea simplicifolia lectin 1, isolectin 4 (BSIL4). Thirty-six percent of the neurons in the ophthalmic portion of the mouse trigeminal ganglion express CGRP and 17%, SP. All neurons that express SP also express CGRP. Forty percent of the neurons in the ophthalmic region of the ganglion are recognized by monoclonal antisera to SSEA3, and 66% of this population also express the neuropeptides SP or CGRP. The neuronal population recognized by BSIL4 is identical to the population with the LD2 epitope. This population of cells (BSIL4/LD2) does not express the SSEA3 glycoconjugate and is largely nonpeptidergic. All four populations of sensory neurons (SP, CGRP, SSEA3, and LD2/BSIL4) can be infected by herpes simplex virus (HSV). However, the relative proportion of SSEA3- and LD2/BSIL4-labeled cells that were infected productively with HSV was much less than expected based on the relative size of the populations of these neurons in the ophthalmic region of the ganglion.
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PMID:Herpes simplex viral infection of the mouse trigeminal ganglion. Immunohistochemical analysis of cell populations. 137 Dec 69

The staining patterns produced by the lectin Vicia villosa and by a commercially available polyclonal antibody generated to substance P were analysed and compared in monkey visual cortex at the light and electron microscopic levels. Vicia villosa lectin labels the cell surface of a subpopulation of cortical cells, producing a meshlike pattern over the soma and proximal dendrites. The polyclonal antibody labels three distinct elements in the cortex: a pericellular epitope present on a subpopulation of non-pyramidal cells, and putative intracellular sites in a type of small pyramidal cell located at the layer 5/6 border, and in a small number of non-pyramidal cells in the underlying white matter. Because of the similarity of the appearance of the Vicia villosa lectin labelling and the pericellular labelling produced by the polyclonal antibody, further experiments were conducted to determine the relationship between the cell surface sites recognized by these markers. Double-labelling experiments show that both sites are present on the same population of cells, and at the ultrastructural level both markers appear to outline the intersynaptic cell membrane, sometimes extending around presynaptic elements. However, preadsorption experiments indicate that the markers recognize different sites on the cell membrane. Preadsorption experiments also show that the pericellular epitope recognized by the polyclonal antibody is unlikely to be substance P, but it may be structurally similar to keyhole limpet haemocyanin. Comparison of cortical and subcortical staining patterns produced with the polyclonal antibody and with a commonly used monoclonal antibody to substance P reveal that one of the putative intracellular epitopes recognized by the polyclonal antibody is likely to be substance P.
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PMID:VVA-labelled cells in monkey visual cortex are double-labelled by a polyclonal antibody to a cell surface epitope. 137 82

By use of light microscopic immunohistochemical and lectin histochemical methods, the interrelation of galactose-containing glycoprotein (GCGP), calcitonin gene-related peptide (CGRP)-like, leu-enkephalin (L-ENK)-like, and substance P (SP)-like peptides has been evaluated on consecutive sections of dorsal root ganglia from colchicine-treated rats. The results showed that GCGP, CGRP, L-ENK and SP exist simultaneously in individual neurons of the dorsal root ganglia in rats. Almost all small neurons in dorsal root ganglion contained both GCGP and CGRP. The stronger peanut lectin affinity with small neurons, the weaker CGRP immunoreactivity, and vice versa. Some neurons of medium size were of strong CGRP-like immunoreactivity; however, they lacked in affinity with peanut lectin. The large spinal ganglionic cells rarely showed CGRP immunoreactivity and affinity with peanut lectin. The results suggested that there was a negative interrelation between GCGP and CGRP in small primary sensory neurons. From the above it may be suggested that the GCGP plays an important role in recognizing and transmitting information in primary sensory neurons.
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PMID:Simultaneous existence of galactose-containing glycoprotein and several neuropeptides in DRG of the rat. 137 55

The distribution of binding by the isolectin I-B4 from Griffonia simplicifolia in the rat trigeminal system has been investigated. This lectin binds to a sub-population of small-diameter trigeminal ganglion neurons. Double-labelling studies revealed that this lectin bound to all the trigeminal ganglion neurons containing somatostatin, whereas it bound to less than 25% of those containing calcitonin gene-related peptide or substance P. In the brainstem this lectin gave terminal-like staining in only the sub-nucleus caudalis of the trigeminal nuclei. In this nucleus, staining was most dense in the inner part of lamina II. Morphometric studies suggest that this lectin and that from the soybean recognize the same population of cells. The relationship of this data to those obtained in other studies using markers binding to glycoconjugates with a terminal alpha-galactose is discussed.
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PMID:The distribution of binding by isolectin I-B4 from Griffonia simplicifolia in the trigeminal ganglion and brainstem trigeminal nuclei in the rat. 137 53

Retrograde tracing, immunocytochemical, and histochemical methods were used to determine the manner in which different classes of trigeminal (V) ganglion cells respond to transection of their axons during infancy. Retrograde tracing with true blue (TB), histochemistry using the plant lectin Bandieraea simplicifolia-I (BS-I), and immunocytochemistry using an antiserum directed against substance P (SP) were carried out in the V ganglion and V brainstem complex of normal adult rats. In the adult V ganglion, 11.9 +/- 1.9% of the cells that sent axons into the infraorbital nerve (ION) contained SP-like immunoreactivity (SPLI) and 26.9 +/- 3.6% bound the lectin BS-I. Only 2.7 +/- 1.6% of ION cells were labelled by both the SP antiserum and BS-I. Transection of the ION on the day of birth had very different effects upon primary afferent neurons containing SPLI and those labelled by BS-I. We have previously shown that such lesions result in a significant expansion of the portion of SpC innervated by primary afferents containing SPLI and we have also provided data consistent with the proposal that ganglion cells recognized by an antiserum directed against SP are more likely than other primary afferent neurons to survive neonatal axotomy. In the present study, combination of retrograde tracing with TB and lectin binding histochemistry showed that cells recognized by BS-I were selectively lost after neonatal ION transection. Only 14.2 +/- 4.4% of the ION ganglion cells that projected into this nerve at the time of the lesion and that survived neonatal axotomy were BS-I positive when the animals reached adulthood. Neonatal ION transection also resulted in a permanent reduction in the density of BS-I binding in SpC. Bandieraea simplicifolia-I binding in the brainstem ipsilateral to the damaged nerve was almost completely gone within 1 day of the nerve transection and recovered only partially by the time the rats were 2 months of age. In alternate sections tested with the SP antiserum, there was a slight reduction in the density of SPLI in the deafferented SpC on postnatal days 4 and 5, but this change never approached that observed for BS-I binding.
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PMID:Neonatal infraorbital nerve transection in the rat: comparison of effects on substance P immunoreactive primary afferents and those recognized by the lectin Bandierea simplicifolia-I. 170 74

In order to examine the synaptic input to dopaminergic neurones in the substantia nigra from GABAergic terminals and terminals that contain substance P, double and triple immunocytochemical studies were carried out at the light and electron microscopic levels in the rat. In a first series of experiments sections of the substantia nigra were incubated to reveal axon terminals containing either substance P or glutamate decarboxylase and then incubated to reveal dopaminergic neurones using tyrosine hydroxylase immunocytochemistry. Examination of this material in the light microscope revealed that many substance P- and glutamate decarboxylase-immunoreactive boutons were associated with the dopaminergic cells. In the electron microscope it was found that the perikarya and dendrites of the dopaminergic neurons received symmetrical synaptic input from terminals that displayed immunoreactivity for substance P or glutamate decarboxylase. A small proportion of the substance P-positive boutons formed asymmetrical synapses. In a second series of experiments sections of the substantia nigra were processed by the pre-embedding immunocytochemical technique for tyrosine hydroxylase and then the post-embedding immunogold technique for gamma-aminobutyric acid (GABA). Examination in the electron microscope revealed that the tyrosine hydroxylase-positive neurons received symmetrical synaptic input from many GABA-positive terminals. Quantitative analyses demonstrated that a minimum of 50-70% of all boutons afferent to the dopaminergic neurones display glutamate decarboxylase or GABA immunoreactivity. Triple immunocytochemical studies i.e. pre-embedding immunocytochemistry for tyrosine hydroxylase and substance P, combined with post-embedding immunogold staining for GABA, revealed that some of the substance P-immunoreactive boutons that were in contact with the dopaminergic neurones also displayed GABA immunoreactivity. In a third series of experiments the combination of anterograde transport of lectin-conjugated horseradish peroxidase or biocytin with post-embedding GABA immunocytochemistry demonstrated that at least one of the sources of GABA-containing terminals in the substantia nigra is the striatum. The results of the present study: (1) demonstrate that dopaminergic neurones in the substantia nigra receive symmetrical synaptic input from GABAergic and substance P-containing terminals, (2) show that a proportion of these terminals contain both substance P and GABA and (3) suggest that the major synaptic input to dopaminergic neurones is from GABAergic terminals and that a part of this innervation is derived from the striatum.
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PMID:The GABA and substance P input to dopaminergic neurones in the substantia nigra of the rat. 170 87

The characteristics of the carbohydrate chain on the rat cerebral cortical substance P (SP) receptor were studied. We examined the effects of pretreatment with three lectins (concanavalin A, wheat germ agglutinin, lens culinaris agglutinin) on the [3H]SP binding activities. Each lectin can bind to the specific carbohydrate chain. Among these lectins, only concanavalin A inhibited specific [3H]SP binding by reducing the affinity of the binding sites. The inhibitory action of concanavalin A was dose-dependent and diminished by the addition of alpha-methyl-D-mannoside. The present results suggest that the rat cortical SP receptor has either a biantennary complex-type or a high mannose-type of carbohydrate chain, and that the carbohydrate chain is implicated in the SP binding activity of the SP receptor system.
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PMID:Characterization of the carbohydrate chain on the substance P receptor in the rat brain cortex: effect of lectins on [3H]substance P binding. 170 59

Peptidergic fibers in the globus pallidus of the monkey appear in the morphological form referred to as woolly fibers. These fibers are composed of a dense plexus of thin beaded axons which ensheath an unstained central core. Such structures are not confined to the globus pallidus, but are also present in the bed nucleus of the stria terminalis, the hypothalamus, the dorsal part of the amygdala, and ventrally in the basal forebrain. The present study describes the relationship between projections from the rostral and ventral striatum and the enkephalin- and substance P-positive woolly fibers. Following injections of either tritiated amino acids or the lectin Phaseolus vulgaris-leucoagglutinin in the ventral striatum, anterogradely labeled fibers and terminals in the forebrain were visualized simultaneously with enkephalin- or substance P immunoreactivity in the same tissue section in order to determine: (i) the extent to which the woolly fiber distribution represents striatal output systems; (ii) whether woolly fibers can be considered as a marker for the entire striatal forebrain projection; and (iii) whether enkephalin and substance P are involved differentially in distinct ventral striatopallidal pathways. Phaseolus vulgaris-leucoagglutinin labeling is seen in the globus pallidus and adjacent structures either as single, beaded fibers or in a profile strikingly similar to that of woolly fibers. In tissue sections treated for a double immunohistochemical protocol, following which the Phaseolus vulgaris-leucoagglutinin-immunoreactive fibers turn black and the peptidergic woolly fibers brown; many of the lectin-positive fibers are seen to enter the peptide-positive woolly fiber plexus. Likewise, following the injections with tritiated amino acids in the ventral striatum, coarse structures that have dimensions resembling those of the woolly fibers are identified. In sections immunohistochemically stained and subsequently treated for autoradiography, peptide-positive woolly fibers can be identified underlying the silver grains. In sections stained for both peptide immunoreactivity and tracer substances, enkephalin or substance P-positive woolly fibers are present in all pallidal regions that receive ventral striatal input. However, the ventral striatum also sends fibers to the hypothalamus, bed nucleus of the stria terminalis, the dorsal part of the amygdala, the septum, the preoptic area, and other areas of the basal forebrain. In these nuclei the peptide-positive woolly fiber distribution is less extensive than the terminal labeling. The distribution of substance P-positive fibers in the subcommissural pallidal region is more limited than the distribution of enkephalinergic fibers.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:The relationship between ventral striatal efferent fibers and the distribution of peptide-positive woolly fibers in the forebrain of the rhesus monkey. 170 14

The histamine release induced by compound 48/80, bradykinin or polyethylenimine with a molecular weight of 600 (PEI6) was inhibited by wheat germ agglutinin (WGA) and phytohemagglutinin E-subunits (PHA-E4), and the inhibition was specifically reversed by N-acetyl glucosamine and N-acetyl galactosamine, respectively. Concanavalin A (Con A) and phytohemagglutinin L-subunits (PHA-L4) did not inhibit the histamine release induced by compound 48/80, bradykinin or PEI6. The histamine release induced by substance P was also inhibited sugar-specifically by WGA and PHA-E4. The binding sites for compound 48/80, bradykinin, PEI6 and substance P, therefore, seemed to especially overlap each other. These binding sites were found to be glycoproteins having affinities to WGA and PHA-E4, but not to Con A and PHA-L4. The binding of WGA and PHA-E4 to the glycoproteins resulted in inhibition of the interaction between the basic secretagogues including bradykinin and substance P and their binding sites on the mast cells. The bindings of five lectins to mast cell glycoproteins were examined by lectin-blotting. Several glycoproteins, which had specific affinities to WGA and PHA-E4, but not to Con A and PHA-L4 were detected. We assumed that the binding sites for basic secretagogues which are coupled with histamine-releasing mechanisms exist among these glycoproteins. A 41-kDa protein (alpha-subunit of pertussis toxin-sensitive G protein) was not detected by WGA, suggesting that the binding sites for the basic secretagogues were not G proteins.
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PMID:Sugar-specific inhibitory effects of wheat germ agglutinin and phytohemagglutinin-E4 on histamine release induced by basic secretagogues from rat peritoneal mast cells and their possible action sites. 172 87


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