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)-ergic neurons from 16/17 day-embryonic rat brain stem in primary culture were identified by immunocytochemistry using biotinylated avidin and phosphatase alkaline methods with affinity-purified anti-SP antibodies. An average of 84% of neurons contained SP from day 9 to day 21 after plating. These in vitro data show that SP-containing neurons develop in our culture conditions. SP may act as a maturation factor as well as a neurotransmitter.
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PMID:Substance P immunoreactivity of rat brain stem neurons in primary culture. 137 81

The identity of 3H-labelled material ascribed to Ins(1,4,5)P3 in resting or bombesin-stimulated myo-[3H]inositol-labelled AR4-2J cells was investigated by determining its ability to serve as substrate for partially purified Ins(1,4,5)P3/Ins(1,3,4,5)-P4 5-phosphatase and Ins(1,4,5)P3 3-kinase. This 3H-labelled material was metabolized by these two enzymes at rates which were indistinguishable from those for an internal [32P]Ins(1,4,5)P3 standard, establishing its identity as authentic Ins(1,4,5)P3. In addition, and in contrast with findings in earlier studies utilizing substance P as an agonist, prolonged stimulation with bombesin resulted in an increase in an InsP4 which was degraded by Ins(1,4,5)P3/Ins(1,3,4,5)P4 5-phosphatase. These findings serve to confirm the previous estimate of Horstman, Takemura & Putney [(1988) J. Biol. Chem. 263, 15297-15303] for the intracellular concentrations of Ins(1,4,5)P3 in resting (2 microM) and agonist-stimulated (25 microM) AR4-2J cells. The implications of these findings for the physiological regulation of intracellular Ca2+ through this intracellular messenger are discussed.
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PMID:Identification in extracts from AR4-2J cells of inositol 1,4,5-trisphosphate by its susceptibility to inositol 1,4,5-trisphosphate 3-kinase and 5-phosphatase. 216 94

The distribution of adenosine deaminase-containing neurons and fibers in the spinal cord and medulla was examined and the relationship of dorsal root ganglia neurons containing this enzyme to those containing somatostatin, substance P, fluoride-resistant acid phosphatase (FRAP) and 5'-nucleotidase was determined using immunohistochemical and histochemical methods. In the spinal cord adenosine deaminase-immunoreactive fibers and neurons were confined to layer I and IIo. A similar localization of these was observed in the spinal trigeminal nucleus. In adult animals treated neonatally with capsaicin adenosine deaminase-positive fibers were totally depleted in layer IIo but only partially depleted in layer I. Analysis of lumbar sensory ganglia revealed that small type-B neurons immunoreactive for adenosine deaminase were also immunoreactive for somatostatin but not substance P. In addition, adenosine deaminase-positive neurons lacked histochemical reaction-product for FRAP and exhibited the lowest activity of 5'-nucleotidase. Examination of the neuronal populations containing the two phosphatase enzymes showed that a proportion of neurons exhibiting 5'-nucleotidase activity were devoid of FRAP activity. It is concluded that dorsal root ganglia neurons immunoreactive for adenosine deaminase and somatostatin constitute a single subpopulation of type-B ganglion cells separate from those containing substance P or FRAP. It appears that the lack of coexistence of adenosine deaminase with either FRAP or 5'-nucleotidase cannot be attributed simply to a coexistence of the two latter enzymes since some 5'-nucleotidase-positive neurons lacking FRAP were also devoid of adenosine deaminase-immunoreactivity. Insofar as these three enzymes may contribute to the regulation of transmission processes in primary sensory neurons, our results indicate a minimal functional relationship between adenine nucleoside and nucleotide degrading enzymes in these neurons. In addition, FRAP appears to have some functional independence from 5'-nucleotidase.
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PMID:Anatomical and cytochemical relationships of adenosine deaminase-containing primary afferent neurons in the rat. 241 72

1. An enzyme which can be extracted from brain inactivates nerveside in the optimum pH range 5.8-7.0.2. The polybasic acids trypan blue and its analogue trypan red, bromphenol blue and its analogue bromthymol blue at concentrations of 0.22 mM and ethylenediaminetetra-acetic acid (EDTA) at a concentration of 1 mM are strong inhibitors of the enzyme.3. Penicillin which is a monobasic carboxylic acid also inhibits the enzyme but only if concentrations as high as 3.6 mM are used. The antibiotic streptomycin which is a basic substance does not inhibit the enzyme.4. Caffeine at a concentration of 7.2 mM only weakly inhibits the enzyme.5. Chymotrypsin and wheat germ acid phosphatase also inactivate nerveside at pH 5.9 and are inhibited by the acidic dyes and penicillin. EDTA inhibits wheat germ phosphatase but activates chymotrypsin.6. Inactivation of nerveside by the brain enzyme and by wheat germ phosphatase is different from the action of chymotrypsin. Nerveside solutions incubated with chymotrypsin completely lose all biological activity whereas if incubation is carried out with either the brain enzyme or wheat germ acid phosphatase a residual biological activity remains even when the concentration of these two enzymes is increased. This residual biological activity is due to a peptide as it is destroyed by chymotrypsin.7. The manner in which nerveside is inactivated by the brain enzyme is uncertain as the preparation of the latter contained phosphodiesterase and protease activities which were similarly inhibited by the acid dyes, penicillin and EDTA.8. Pentylenetetrazole, picrotoxin, strychnine and tetanus toxin do not inhibit the brain enzyme.9. The nerveside-inactivating enzyme is not identical with the Substance P-inactivating enzyme in brain as the former is inhibited by EDTA while the latter is not.
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PMID:The inhibitory effect of convulsant agents on the enzyme in brain which inactivates nerveside. 439 Mar 85

The distribution of fluoride-resistant acid phosphatase, substance P and somatostatin were investigated in the dorsal horn of the spinal cord and in dorsal root ganglia. In the dorsal horn, the distribution of fluoride-resistant acid phosphatase closely paralleled that of somatostatin and only partly overlapped with that of substance P. In sensory ganglia, none of the fluoride-resistant acid phosphatase-containing neurones contained either substance P or somatostatin. The results suggest the existence of a population of fluoride-resistant phosphatase-positive sensory neurones which is distinct from neurones containing either of these peptides.
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PMID:Fluoride-resistant acid phosphatase-containing neurones in dorsal root ganglia are separate from those containing substance P or somatostatin. 617 4

We examined the effects of the phosphatase inhibitor, okadaic acid, on substance P and calcitonin gene-related peptide release from embryonic rat sensory neurons grown in culture. Exposing isolated sensory neurons to 500 or 1000 nM okadaic acid for 30 min resulted in a 2- to 5-fold increase in the release of either peptide above resting levels and this evoked release was dependent on extracellular calcium. Treating sensory neurons with 250 nM okadaic acid did not alter resting peptide release, but significantly enhanced peptide release evoked by either 50 nM capsaicin, 100 nM bradykinin, or 30 mM KCl. These results suggest that enhancing phosphorylation in sensory neurons is an important component in augmenting transmitter release.
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PMID:The phosphatase inhibitor, okadaic acid, increases peptide release from rat sensory neurons in culture. 752 84

We compared the desensitization of neurokinin1 and neurokinin2 (NK1 and NK2) receptors expressed in Chinese hamster ovary cells to substance P and neurokinin A, respectively. Substance P and neurokinin A stimulated a rapid increase in intracellular Ca2+ concentration ([Ca2+]i) for both receptors, which was due to release of Ca2+ from intracellular stores. This was followed by a plateau in [Ca2+]i, which was due to influx of extracellular Ca2+, and was more sustained for the NK2 receptor. When Ca2+ was present in the extracellular solution, the Ca2+ response of the NK1 receptor, but not the NK2 receptor, rapidly desensitized and slowly resensitized to two exposures to agonist. In contrast, the [Ca2+]i response, measured in Ca2+-free solution, and inositol triphosphate generation desensitized and resensitized similarly for the NK1 and NK2 receptors. Thus, differences in desensitization between the NK1 receptor and the NK2 receptor may be related to differences in entry of extracellular Ca2+. We compared endocytosis of the NK1 and NK2 receptors to determine whether disparities could account for differences in desensitization. Fluorescent and radiolabeled substance P and neurokinin A were internalized similarly by cells expressing NK1 and NK2 receptors. Thus, disparities in internalization cannot account for differences in desensitization. We used inhibitors to examine the contribution of endocytosis, recycling, and phosphatases to desensitization and resensitization of the NK1 receptor. Desensitization did not require endocytosis. However, resensitization required endocytosis, recycling, and phosphatase activity. This suggests that the NK1 receptor desensitizes by phosphorylation and resensitizes by dephosphorylation in endosomes and recycling.
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PMID:Mechanisms of desensitization and resensitization of G protein-coupled neurokinin1 and neurokinin2 receptors. 864 83

1. We have investigated the role of phosphatases in modulating contractile responses to electrical field stimulation (EFS), methacholine, substance P and capsaicin in guinea-pig isolated main bronchus by use of the phosphatase 1 and 2A inhibitor okadaic acid. 2. Non-adrenergic non-cholinergic (eNANC) contractile responses were elicited by EFS (3 Hz, 20 s, 0.5 ms max. voltage) in the guinea-pig isolated main bronchus in the presence of the non-selective muscarinic antagonist, atropine (1 microM), the non-selective beta-adrenoceptor antagonist; propranolol (1 microM), the neutral endopeptidase inhibitor thiorphan (10 microM) and the cyclo-oxygenase inhibitor, indomethacin (5 microM). Okadaic acid significantly attenuated eNANC contractile responses (% inhibition) elicited by EFS (0.01 microM, 15.2 +/- 26.9%; 0.03 microM, 30.4 +/- 13.9%; 0.01 microM, 39.8 +/- 5.1%; 0.3 microM, 59.5 +/- 8.7%; 1 microM 77.8 +/- 7.8%; P < 0.05, n = 4). In contrast, the inactive analogue 1-Nor okadaone (0.3 microM) failed to attenuate significantly eNANC contractile responses (% inhibition elicited by 1-Nor okadaone, -1.25 +/- 8.5% vs dimethylsulphoxide (DMSO), -13.5 +/- 21.5%; P > 0.05, n = 4). 3. Cholinergic contractile responses were elicited by EFS (1-30 Hz, 10 s, 0.5 ms max. voltage) in guinea-pig isolated bronchus in the presence of the nitric oxide synthase inhibitor, N omega-nitro-L-arginine methyl ester (L-NAME, 30 microM). Okadaic acid failed to attenuate significantly the contractile (% methacholine Emax) response elicited by EFS at all frequencies tested compared with the control (1 Hz, control, 22 +/- 7.9% vs okadaic acid, 18 +/- 7.7%; 3 Hz, control, 26 +/- 6.9% vs okadaic acid, 27 +/- 9.1%; 10 Hz, control, 36 +/- 7.6% vs okadaic acid, 33 +/- 8.9%; 30 Hz, control, 50 +/- 7.6% vs okadaic acid, 42 +/- 14%; P > 0.05, n = 4). 4. Okadaic acid (0.3 microM) failed to alter significantly the contractile potency (pD2) to capsaicin (okadaic acid, 9.0 +/- 0.5, vs DMSO, 9.2 +/- 0.4; P > 0.05 n = 6), substance P (okadaic acid, 7.6 +/- 0.3 vs DMSO, 8.2 +/- 0.2; P > 0.05 n = 7) or methacholine (okadaic acid, 6.4 +/- 0.2 vs DMSO, 6.4 +/- 0.3; P > 0.05 n = 4). 5. Okadaic acid (0.01-1 microM) did not appear to reverse substance P-induced tone. The maximal relaxant response (% reversal of substance P-induced tone) mediated by okadaic acid (1 microM) was 33 +/- 11.7% (n = 4), this was not significantly different from the DMSO (0.8%) or a time-dependent fall in tone of 34.3 +/- 23.1% (n = 4) and 33 +/- 15.8% (n = 4), respectively. Okadaic acid (0.3 microM) failed to augment isoprenaline-induced relaxation responses in substance P contracted bronchus (okadaic acid, 6.5 +/- 0.4 vs DMSO, 5.9 +/- 0.3; P > 0.05, n = 9). 6. These results indicate that protein phosphatases appear to regulate the release of sensory neuropeptides from airway sensory nerves in response to electrical field stimulation.
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PMID:The effect of okadaic acid on non-adrenergic non-cholinergic contraction in guinea-pig isolated bronchus. 915 25

We studied mesenteric arterial arcades from 3- and 35-day-old swine to determine the relationship between perfusate flow rate and release of nitric oxide (NO) into mesenteric effluent. Mesenteric arterial arcades were perfused under controlled-flow conditions with a peristaltic pump using warm oxygenated Krebs buffer. Basal rates of NO production were 43.6 +/- 4.2 vs. 12.1 +/- 2.5 nmol/min in 3- vs. 35-day-old mesentery during perfusion at in vivo flow rates (9 vs. 20 ml/min, respectively). Rate of NO production was directly related to flow rate over a wide range of flows (5-40 ml/min) in 3- but not 35-day-old mesentery. Both age groups demonstrated a brisk, albeit brief, increase in NO production in response to infusion of NO-dependent vasodilator substance P (10(-8) M/min). Tyrosine kinase inhibitor herbimycin A and L-arginine analog L-NMMA significantly attenuated flow-induced increase in NO production, and phosphatase inhibitor phenylarsine oxide increased magnitude of flow-induced increase in NO production in 3-day-olds. Removal of extracellular Ca(2+) and depletion of intracellular Ca(2+) stores (Ca(2+)-free Krebs with EGTA plus thapsigargin) had no effect on NO production in either group. Thus, basal rate of NO production is greater in mesenteric arterial arcades from 3- than from 35-day old swine, a direct relationship between flow rate and NO production rate is present in mesentery from 3- but not 35-day-olds, and phosphorylation events are necessary for this interaction to occur.
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PMID:Relationship between flow rate and NO production in postnatal mesenteric arteries. 1112 96

The possibility of using yeast from alcohol distilleries as a source of nutrients in soil was investigated. The following treatments were used: no fertilization (control), 0.5% (w/w) yeast, 1% (w/w) yeast, and NPK. The decomposition of yeast was monitored for 90 days in two soils. The CO2 production and the microbial biomass were increased by an average of 1- to 3-fold by yeast incorporation compared to control. Protease activity also was enhanced 3- to 8-fold in the soils supplemented with yeast compared to control. The phosphatase activities were higher than control only during the first days. While nitrate contents increased in all treatments compared to control, available P only increased in the soils amended with 1% yeast or NPK by 45-119% and 309-489%, respectively. These results indicate that there exists an excellent potential for the use of yeast in the soil as a source of nitrate and available P for plant nutrition.
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PMID:Carbon, nitrogen and phosphorus mineralization in two soils amended with distillery yeast. 1515 8


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