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)

An indirect immunofluorescence method was utilized to identify substance P-like immunoreactive (SPLI) and neurofilament protein immunoreactive (NFIR) fibers in the lumbar facet joint capsule and supraspinous ligament of the rabbit. The results demonstrated a large population of NFIR fibers, indicating that these tissues are richly innervated, and a smaller population of SPLI fibers. In some fibers, neurofilament protein and substance P were colocalized. The data suggest that the facet joint capsule and the supraspinous ligament contain SPLI nociceptive fibers that could be a source of low back pain.
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PMID:Localization of substance P and neurofilament immunoreactive fibers in the lumbar facet joint capsule and supraspinous ligament of the rabbit. 246 64

The taste buds and associated nerves in the guinea pig, rat, cat, and mouse were investigated by immunocytochemistry and formaldehyde-induced fluorescence histochemistry. The antisera used were against spot 35 protein, neuron-specific enolase (NSE), neurofilament protein (NFP), and substance P. The spot 35 protein immunoreactivity was confined to taste bud cells in the guinea pig and rat; the immunoreactive cells, slender in shape, comprised half the number of the total taste bud cells in the guinea pig but were fewer in the rat. For NSE, on the other hand, taste bud cells as well as neural elements localized in both the taste bud and the subepithelial connective tissue were immunoreactive in all the species investigated. Furthermore, all of the spot 35 protein-immunoreactive cells proved to be NSE-immunoreactive in the guinea pig and rat. For NFP, neither the bud cells nor the nerves in the taste bud were reactive, whereas a part of nerves in the connective tissue was immunostained in all the species. The antiserum against substance P exclusively detected some parts of nerves in and out of the taste buds in the cat, rat, and mouse. The aminergic innervation was rather meager and appeared in the nerve fibers localized in the taste buds and connective tissue of the cat and mouse.
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PMID:Immunocytochemistry of neuron-specific proteins and neuropeptides in taste buds and associated nerves. 247 4

Rat trigeminal neurons innervating tooth pulps were retrogradely labelled with fluorogold and analysed enzyme- and immunohistochemically for their content of substance P, calcitonin gene-related peptide, fluoride-resistant acid phosphatase, GM 1 ganglioside, carbonic anhydrase and neurofilament protein. The data showed that both small, medium-sized and large trigeminal neurons were labelled after fluorogold deposition in maxillary molar pulps, with a majority of the cells being medium-sized and large. Less than 2% of the pulpal neurons showed substance P-like immunoreactivity. Fifty-six per cent of the pulpal nerve cells were calcitonin gene-related peptide-positive. These cells were small, medium-sized and large. Only 1% of the fluorogold-labelled cells contained fluoride-resistant acid phosphatase enzyme activity. This paralleled the finding that the pulpal neurons were unstained by Griffonia simplicifolia isolectin I-B4, a plant lectin which preferentially binds to fluoride-resistant acid phosphatase-positive cells. Choleragenoid-like immunoreactivity, which identifies cells with the GM 1 ganglioside receptor, was found in 70% of the fluorogold-labelled pulpal neurons. Approximately 80% of the fluorogold-labelled cells showed RT 97-immunoreactivity. RT 97 labels neurofilament protein and is present in large light primary sensory neurons. No pulpal neurons appeared to contain carbonic anhydrase, as judged from both enzyme- and immunocytochemical observations. The findings suggest that, in the rat, trigeminal tooth pulp neurons, which according to the classical view are nociceptive, form a heterogeneous group of neurons with a minority of small cells which may contain calcitonin gene-related peptide but rarely either substance P or fluoride-resistant acid phosphatase. However, the vast majority of pulpal nerve cells appear to have sizes and cytochemical characteristics which are not generally associated with nociceptive primary sensory neurons.
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PMID:Combined retrograde tracing and enzyme/immunohistochemistry of trigeminal ganglion cell bodies innervating tooth pulps in the rat. 248 Dec 44

1. The primary sensory neurones have been classified into large light (LLC), type A, small dark (SDC), type B and type C cells on the basis of size, ultrastuctural and immunocytochemical characteristics. 2. Subclassifications have been described according to the configuration and spatial organization of cytoplasmic organelles. 3. Furthermore, the LLC are immunoreactive with a monoclonal antibody, RT97, directed against a neurofilament protein and the SDC are positive with anti-arginine vasopressin (AVP). 4. The majority of the neurochemical substances including substance P (SP), somatostatin (SOM), fluoride resistant acid phosphatase (FRAP), 5-hydroxytryptamine (5-HT) and glutamate were localized to the small and intermediate diameter neurones measuring 9-40 microns. 5. The cytochemistry of the dorsal horn was similar to the dorsal root ganglia (DRG). 6. There is good evidence that substance P (SP) and somatostatin (SOM) are transmitters for a proportion of nociceptive neurones but the neurotransmitters utilized by the rest of the subtypes are unknown. 7. 5-hydroxytryptamine (5-HT) and glutamate may be putative transmitters of the primary sensory neurones as they are localized in 28-30% of the SDC. 8. The wider distribution and extensive coexistence of the neuropeptides is incompatible with neurotransmitter function, but some may be neuromodulators whereas others such as arginine vasopressin (AVP) are useful markers for identifying type B neurones.
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PMID:Cytochemistry of the trigeminal and dorsal root ganglia and spinal cord of the rat. 256 21

There is experimental evidence suggesting that the interstitial cells of Cajal are essential for rhythmic slow waves of the smooth muscle layers of the mammalian small intestine. Different investigators have identified them variously as modified neurons, glia, fibroblasts or modified smooth muscle cells. Since histological categorization bears on understanding their function, we have examined the immunoreactivity of the myenteric plexus of the rat small intestine, paying special attention to the cell type identified as Thuneberg's Type I-ICC. Polyclonal and monoclonal antisera directed against 4 intermediate filament proteins: neurofilament protein, glial fibrillary acidic protein, vimentin and desmin were used. In addition, antisera directed against neuron-specific enolase, substance P and vasoactive intestinal polypeptide were also tested for reactivity. Type I-ICCs were immunonegative to all the antisera directed against intermediate filament proteins and neuropeptides. However, some Type I-ICCs were immunopositive to antisera against neuron-specific enolase. On the basis of these results and the distribution of immunoreactivities to these kinds of antisera in other tissues, we suggest that Type I-ICCs are distinct from typical myenteric neurons, from glia, from fibroblasts and from smooth muscle fibers. Staining with antiserum against neuron-specific enolase suggests a relation to some type of neuron.
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PMID:Immunocytochemistry of the interstitial cells of Cajal in the rat intestine. 279 41

Neuroendocrine (NE) neoplasms of the human bronchopulmonary tract were examined by electron microscopy, immunocytochemistry, and gel electrophoresis of cytoskeletal proteins from microdissected tissue samples. All samples (carcinoids, well-differentiated NE carcinoma, NE carcinomas of intermediate type, NE carcinomas of the small cell type) contained significant numbers of cells that immunostained for one or more of the following neuroendocrine markers tested: bombesin, calcitonin, ACTH, leu-enkephalin, gastrin, serotonin, somatostatin, alpha-melanocyte-stimulating hormone, vasoactive intestinal peptide, glucagon, insulin, substance P, and neuron-specific enolase. Electron microscopy revealed typical NE cell features, including variable abundant and frequently heterogeneous neurosecretory granules. Tumor cells contained filaments specifically stained with different conventional and monoclonal antibodies to cytokeratins and displayed punctate plasma membrane staining with antibodies to desmoplakins, in agreement with the electron microscopic demonstration of tonofilament bundles and desmosomes. Immunocytochemistry for NE markers and cytoskeletal proteins on consecutive sections revealed both cytokeratins and neuroendocrine substances in single cells. Using gel electrophoresis of cytoskeletal proteins of tissue regions extracted with high salt buffer and detergent, we could detect, in the tumors tested, appreciable amounts of cytokeratin polypeptides 8, 18, and 19, i.e., major cytokeratins also found in certain other lung carcinomas such as adenocarcinomas. Tumor cells were not significantly stained with antibodies to other intermediate filament proteins such as vimentin, desmin, glial filament protein, and neurofilament protein. The results show that NE substances can be synthesized in cells containing a typical epithelial cytoskeleton, i.e., cytokeratin filaments and desmosomes. These findings support the notion of an epithelial character of these tumors and appear in contrast with recent reports that neurofilaments are the only type of intermediate filaments present in carcinoids and other pulmonary NE tumors. These observations may have important implications for the histogenesis of NE carcinomas and for diagnostic pathology.
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PMID:Coexpression of neuroendocrine markers and epithelial cytoskeletal proteins in bronchopulmonary neuroendocrine neoplasms. 298 72

Endopeptidase-24.11, a plasma membrane ectoenzyme with the ability to hydrolyse a variety of neuropeptides, has been localized in the pig nervous system by an immunoperoxidase technique. The endopeptidase was mapped in cryostat sections of the fore and mid-brain to the following structures: caudate-putamen, globus pallidus, olfactory tubercle, nucleus interpeduncularis and substantia nigra. Endopeptidase-24.11-like immunoreactivity was also found in the pia mater, choroid plexus and ependymal lining of the central canal. In the spinal cord, weak staining was observed in the dorsal horn, but strong staining was found in the dorsal root ganglia and nerve roots. Within the central nervous system, endopeptidase immunoreactivity was confined to gray matter and within the positive areas of the striatum densely staining areas, corresponding to striosomes, were discernible. These well-defined structures were exploited in serial sections to examine the alignment of the enzyme-rich patches of neuropil with correspondingly strong staining for other antigens. A consistent match was observed with a monoclonal antibody to neurofilament protein, but there was a poor correlation with a polyclonal antibody to glial fibrillary acidic protein. Substance P-like and [Leu]enkephalin-like immunoreactivity were also studied in sections adjacent to those stained for the endopeptidase. Good matching between enzyme-rich and peptide-rich areas was observed, but some enkephalin-rich areas did not align with enzyme staining and indeed endopeptidase-rich areas were not necessarily matched with areas rich in either peptide. These findings suggest a neuronal rather than an astrocytic location for endopeptidase-24.11 in the CNS and lend support to the view that it plays a central role in neuropeptide metabolism at membrane surfaces. In the peripheral nervous system, the endopeptidase was located in Schwann cell membranes surrounding dorsal root ganglion cells and nerve fibres, while in the pituitary the main concentration was in the adenohypophysis, where only a proportion of the endocrine cells were found to be immunoreactive.
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PMID:An immunohistochemical study of endopeptidase-24.11 ("enkephalinase") in the pig nervous system. 309 17

Trigeminal (V) ganglion cells with different neurochemical phenotypes or different birth dates are affected differently by neonatal axonal transection. The aim of the present study was to determine if V ganglion cell birth date and neurochemical phenotype were correlated and if these two variables could be related to responses to neonatal axonal transection. Immunocytochemistry, histochemistry, and [3H]thymidine labelling were used to determine the birth dates of V ganglion cells recognized by antibodies directed against neurofilament protein (NF), calcitonin gene-related peptide (CGRP), and substance P (SP) and those that bound the lectin Bandierea simplicifolia-I (BS-I). All V ganglion cells were born between embryonic days (E-) 9.5 and 14.5. All ganglion cells were born between E-9.5 and E-14.5. In a normalized population (percentages normalized to equal 100%), over 90% of NF-positive V ganglion cells were born between E-10.5 and E-12.5. The majority of CGRP-positive and SP-positive ganglion cells (> 90%) were generated from E-13.5 to E-14.5 and E-12.5 through E-14.5, respectively. Almost 85% of BS-I-positive ganglion cells were generated on E-12.5 through E-14.5. Previous results and additional data from this study indicated that NF- and BS-I-positive ganglion cells are proportionally more likely to be lost after neonatal axotomy and that SP-positive cells are more likely to remain. The percentage of CGRP-positive cells in the V ganglion was not significantly altered by neonatal infraorbital nerve transection. Overall, these findings do not indicate a strong relationship between cell birth date and the probability of survival after neonatal axonal damage for all V ganglion cell phenotypes.
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PMID:Birth dates and survival after axotomy of neurochemically defined subsets of trigeminal ganglion cells. 753 57

Histologically normal liver biopsy specimens from patients with Hodgkin's lymphoma were investigated with three immunohistochemical methods for the occurrence of peptidergic nerve fibers and endocrine cells. Numerous immunoreactive nerve fibers were seen with antisera against peripheral nerves markers (neuron-specific enolase, neurofilament protein, and S-100). These nerve fibers were localized in the tunica media of branches of both the hepatic artery and portal vein, around the bile ducts, and in the connective tissue of the interlobular septa. In the liver, 10 types of peptidergic nerve fibers were detected: glucagon-, glucagon-like peptide- (GLP), somatostatin-, neuropeptide Y- (NPY), vasoactive intestinal polypeptide-, neurotensin-, gastrin/cholecystokinin C-terminus-, substance P-, serotonin-, and galanin-immunoreactive nerve fibers. GLP-, somatostatin-, NPY-, neurotensin-, substance P-, and galanin-immunoreactive nerve fibers were abundant; the other nerve fibers were scarce. The nerve fibers showed two distinct patterns of distribution: they occurred in the blood vessel wall and in connective tissue of the interlobular septum. Pancreatic polypeptide- and NPY-immunoreactive cells were found among the lining epithelial cells of the bile ducts in the interlobular septum.
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PMID:Peptidergic innervation and endocrine cells in the human liver. 769 56

A number of neuroendocrine and neuronal markers were demonstrated in Leydig cells of the testes of 18 men aged between 20 and 81 years. Tissue sections were divided into five groups, i.e. carcinoma of the prostate (control cases; n = 4), seminoma (n = 8), anti-androgen therapy (n = 3), oestradiol therapy (n = 2) and cryptorchidism (n = 1). The following substances were immunocytochemically tested: the monoamine synthesizing enzymes tyrosine hydroxylase, aromatic L-amino acid decarboxylase, dopamine-beta-hydroxylase and phenylethanolamine-N-methyltransferase, the indolamine serotonin, the calcium-binding proteins parvalbumin, calbindin and S-100 protein, the microtubule associated protein-2, as well as neurofilament protein 200, synaptophysin, neuron specific enolase, substance P and chromogranin A + B. All these substances were found in Leydig cells of all sections independently of the pathological changes of the testes. Compared with the control cases, all the other groups showed a significantly weaker immunoreactivity for all markers. The uniformity of staining among the different antibodies allows the deduction that these neuroactive peptides may belong to a basic equipment of Leydig cells probably stabilizing their function in an autocrine manner. On the other hand, Leydig cells themselves seem to be a stable structural component of the testis, which are not essentially involved in the pathogenesis of the disturbances mentioned above.
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PMID:Neuroendocrine marker substances in human Leydig cells--changes by disturbances of testicular function. 790 79


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