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)

The goal of the present study was to identify cytochemical markers characteristic of muscle afferents in hatchling chicks. To this end, we stained neurons in the trigeminal mesencephalic nucleus with a variety of markers that label subsets of neurons in avian dorsal root ganglia. We found that trigeminal mesencephalic neurons are surprisingly heterogeneous in their cytochemical make-up, expressing, to varying degrees, substance P, cholecystokinin, carbonic anhydrase, calbindin D-28k, parvalbumin, and S-100 beta. Calbindin D28k and S-100 beta appeared to be expressed equally in medial and lateral divisions of the trigeminal mesencephalic nucleus. In contrast, substance P- and cholecystokinin-immunoreactive neurons were more abundant in the medial division, whereas carbonic anhydrase activity and parvalbumin immunoreactivity were stronger in the lateral division. We were unable to detect met-enkephalin, neuropeptide Y, calcitonin gene-related peptide, vasoactive intestinal peptide, somatostatin, gamma-aminobutyric acid, or tyrosine hydroxylase in the trigeminal mesencephalic nucleus. Moreover, these neurons did not appear to bind the lectin Dolichos biflorus agglutinin. The heterogeneity of expression of markers among trigeminal mesencephalic nucleus neurons, especially between neurons in the medial and lateral divisions, suggests that these neurons are functionally diverse.
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PMID:Cytochemical characteristics of neurons in the trigeminal mesencephalic nucleus of hatchling chicks. 788 44

Immunocytochemical properties of dorsal root ganglion neurons innervating the kidney were studied with retrograde tracing of Fluorogold or Fast Blue dyes applied to the cut renal nerves in the rat. The proportions and sizes of renal afferent neurons labelled with a variety of markers were quantified in T9-L1 dorsal root ganglia from five rats. Compared with the overall size distribution in these ganglia, renal afferent neurons were mainly small with a few medium-sized neurons. The majority (79%) of renal afferent dorsal root ganglion neuronal somata were unlabelled by an anti-neurofilament antibody, RT79, and classified as neurofilament-poor with probable C-fibres. These had an approximately normal distribution of cell sizes. Only 21% were RT79-positive and classified as neurofilament-rich with probable A-fibres, and even these were small to medium sized cells, consistent with them being mostly A delta-fibre neurons. Percentages of renal afferent neurons showing labelling were as follows: peripherin-like immunoreactivity: 69%; calcitonin-gene related peptide: 93%; substance P: 37%; the lectins soybean agglutinin: 57% and peanut agglutinin: 68%; Calbindin D28k-like immunoreactivity: 21% (only weak labelling); carbonic anhydrase like immunoreactivity: 0%. There were differences between probable C-fibre and probable A-fibre neurons, classified according to their labelling with RT97. The percentages of RT97-negative and RT97-positive neurons respectively labelled with the other markers were as follows: peripherin-like immunoreactivity: 82%, 25%; calcitonin gene-related peptide-like immunoreactivity: 99%, 79%; substance P-like immunoreactivity: 43%, 0%; soybean agglutinin: 69%, 24%; peanut agglutinin: 76%, 47%; calbindin-like immunoreactivity: 26%, 0%. Thus, the biggest differences between the probable A- and C-fibre renal afferent neurons were in their peripherin, substance P and calbindin contents. Thus, renal afferent neurons in the dorsal root ganglion are not homogeneous and it is suggested the differences may relate to the known different afferent receptor types within the kidney. It is suggested that the low proportion of neurons with substance P-like immunoreactivity in the renal afferent innervation compared to that of other viscera may relate to the role of the renal vasculature in urine formation.
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PMID:Immunocytochemical properties of rat renal afferent neurons in dorsal root ganglia: a quantitative study. 789 54

Dorsal root ganglion neurons innervating skin via the saphenous nerve, muscle via the gastrocnemius nerve and viscera via the splanchnic nerve, were identified by retrograde tracing with Fast Blue applied to the cut nerve. Only neuronal profiles with nuclei were counted. At the survival times used no changes in immunohistochemical labelling patterns were detectable in the axotomized neurons. Percentages of Fast Blue-labelled neuronal profiles that were immunolabelled were calculated. The values for markers of carbohydrate groups were for skin, muscle and viscera, respectively: the lectin peanut agglutinin 55%, 24%, and 50%; the lectin soybean agglutinin 72%, 56%, 61%; the antibody 2C5 (against lactoseries groups) 43%, 20%, 6%; the antibodies SSEA-4 (against globoseries groups) 6%, 12%, 0% and SSEA-3 (against globoseries groups) 6%, 5%, 0%. The values for neurofilament rich profiles were for skin, muscle and viscera, respectively: 34%, 43%, 19%, and for carbonic anhydrase were 10%, 33%, 2%. Values for neuropeptides were, for calcitonin gene-related peptide 51%, 70%, 99%, for substance P 21%, 51%, 82%, and for somatostatin 10%, 2% and 0%. The population of skin afferents therefore contained the highest proportion of profiles expressing galactose containing carbohydrate groups labelled by 2C5 and the lectins and the highest proportion of cells with somatostatin. In contrast they had the lowest proportions of cells with calcitonin gene-related peptide and substance P, compared with the other tissues. Muscle afferents had the highest proportions compared with the other tissues of the neurofilament-rich, carbonic anhydrase-positive and SSEA-4-labelled profiles, but the lowest proportions of profiles with lectin binding. The splanchnic visceral afferents had the highest proportions, compared with the other tissues, of neuronal profiles labelled for calcitonin gene-related peptide and substance P, but the lowest proportions of neurofilament rich profiles and of profiles with carbonic anhydrase or 2C5 labelling and they totally lacked any labelling for globoseries carbohydrates and somatostatin. Both the muscle and skin afferent populations had clear small cell and large cell peaks in their size distributions, with the small cell peak being larger for skin than muscle afferents and the large cell peak being more marked for muscle afferents. The visceral afferent profiles had a unimodal size distribution with the peak size being between the small and large cell peaks of the somatic afferent units. This study therefore shows that the patterns of immunohistochemical labelling and cell size of primary afferent neurons differ according to their peripheral target tissue.
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PMID:Differences in expression of oligosaccharides, neuropeptides, carbonic anhydrase and neurofilament in rat primary afferent neurons retrogradely labelled via skin, muscle or visceral nerves. 960 20

Since ancient times, bile secretion has been considered vital for maintaining health. One of the main functions of bile secretion is gastric acid neutralization with biliary bicarbonate during a meal or Pavlovian response. Although the liver has many extrinsic and intrinsic nerve innervations, the functional role of these nerves in biliary physiology is poorly understood. To understand the role of neural regulation in bile secretion, our recent studies on the effect of bombesin, a neuropeptide, on bile secretion and its underlying mechanisms will be reviewed. Using isolated perfused rat livers (IPRL) from both normal and 2 week bile duct ligated rats, as well as hepatocyte couplets and isolated bile duct units (IBDU) from normal rat livers, bombesin was shown to stimulate biliary bicarbonate and fluid secretion from bile ducts. Detailed pH studies indicated that bombesin stimulated the activity of Cl-/HCO3- exchanger, which was counterbalanced by a secondary activation of electrogenic Na+/HCO3- symport. Quantitative videomicroscopic studies showed that bombesin-stimulated fluid secretion in IBDU was dependent on Cl- and HCO3- in the media, anion exchanger(s), Cl- and K+ channels, and carbonic anhydrase, but not on the microtubular system. Furthermore, this bombesin response is inhibited by somatostatin but not substance P. Finally, studies of secondary messengers in isolated cholangiocytes and IBDU indicated that bombesin had no effect on intracellular cAMP, cGMP, or Ca++ levels in cholangiocytes. These results provide evidence that neuropeptides such as bombesin can directly stimulate fluid and bicarbonate secretion from cholangiocytes by activating luminal Cl-/HCO3- exchange, but by different mechanisms from those established for secretin. These findings, in turn, suggest that neuropeptides may play an important regulatory role in biliary transport and secretion. Thus, this neuropeptidergic regulation of bile secretion may provide a plausible mechanism for the bicarbonate-rich choleresis seen with meals or Pavlovian response.
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PMID:Role of the neuropeptide, bombesin, in bile secretion. 962 61

The lectin soybean agglutinin (SBA) from Glycine max binds to small-sized dorsal root ganglion cells and their central terminals in the superficial dorsal horn of the spinal cord. Here we investigated the ability of SBA and SBA conjugated to horseradish peroxidase (SBA-HRP) to trace thin calibre afferents into the spinal cord from a peripheral nerve. Following injection into the sciatic nerve, labelled cells in the dorsal root ganglion were predominantly small-sized but some medium-sized cells were also labelled. Colocalization studies of transported SBA with various neuronal markers showed that all neurons that transported SBA-HRP showed SBA binding, indicating high uptake specificity for the conjugate. 15% were immunoreactive for RT97 indicating that some axons were myelinated, and 54% also expressed binding sites for isolectin B4 from Griffonia simplicifolia, a selective marker for a subpopulation of unmyelinated afferents. With regard to neurotransmitter content, 43% of the SBA cells contained calcitonin gene-related peptide, 33% contained substance P and 2.5% somatostatin. In addition, 3% contained carbonic anhydrase. Centrally, injection of SBA in the sciatic nerve resulted in labelled terminals in somatotopically appropriate regions of laminae I-II of the dorsal horn, and in the gracile nucleus. A few neurons in the dorsal horn were labelled indicating that some transneuronal transport of SBA had occurred. The results show that SBA can be used as a transganglionic tracer to label fine calibre primary afferents that project to laminae I-II of the spinal cord and the gracile nucleus. It appears to label more afferents than isolectin B4, including also a subpopulation of myelinated afferents.
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PMID:Transganglionic transport of the lectin soybean agglutinin (Glycine max) following injection into the sciatic nerve of the adult rat. 1064 Jan 82


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