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 synthetic peptide [D-Arg1,D-Pro2,D-Trp7,9,Leu1]substance P inhibits the stimulation of DNA synthesis induced in Swiss 3T3 cells by bombesin or vasopressin, but not that induced by a wide range of other growth factors and mitogens. The stimulation induced by 10 pM-3 nM-bombesin is inhibited by 1-30 microM-antagonist in a manner consistent with competition at the bombesin receptor. The inhibition by the antagonist of the stimulation induced by vasopressin suggests a previously unrecognized interaction of the antagonist with vasopressin receptors. The antagonist should be useful in studies of cell proliferation both in vivo and in vitro.
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PMID:A peptide that inhibits the mitogenic stimulation of Swiss 3T3 cells by bombesin or vasopressin. 241 11

Although many peptides have been reported in the vicinity of hypothalamic magnocellular nuclei, their role in the control of neurohypophysial hormone release was only studied for few peptides: opiates, angiotensin II, substance P, CRF, oxytocin and vasopressin. Their effects are briefly recalled and then compared to the more detailed study of their role in the firing pattern of oxytocin and vasopressin neurones. This technique, in some cases, revealed the action site and mechanism of these peptides in the hypothalamo-neurohypophysial system.
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PMID:[Peptidergic control of electrical activities in the magnocellular neurons of the hypothalamus]. 241 39

A whole mount immunofluorescence method was used for the localization of immunoreactivity (IR) to four regulatory peptides and the bioamine serotonin in the nervous system of Stenostomum leucops (Turbellaria, Platyhelminthes). The flatworm S. leucops belongs to the taxon Catenulida which, according to the new phylogenetic system by Ax [2], forms a key group between the coelenterates and more advanced flatworm species. Positive IR was obtained using antisera against FMRF-amide, beta-endorphin, growth hormone releasing factor (GRF), substance P, and serotonin. The distribution patterns of these neuropeptide-like immunoreactivities differ significantly from each other. Antisera against Leu-enkephalin, bovine pancreatic polypeptide (BPP), bombesin, cholecystokinin (CCK-8), neurotensin, somatostatin, growth hormone (GH), secretin, and neurophysin II gave negative results. This primitive flatworm shows similarities with hydra in the lack of IR to anti-somatostatin, anti-Leu-enkephalin, and anti-BPP. These antisera give positive IR in more advanced flatworm species, indicating a later convergent evolution of vertebrate-like peptides within the phylum Platyhelminthes.
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PMID:Neuropeptides in a microturbellarian--whole mount immunocytochemistry. 242 Dec 67

The medial preoptic nucleus (MPN) is a sexually dimorphic complex with three major subdivisions. The cell-dense central (MPNc) and medial (MPNm) subdivisions are larger in male rats, while the cell-sparse lateral subdivision (MPNl) occupies a majority of the nucleus in females. In the present study we evaluated the distribution of possible monoaminergic and peptidergic cells and fibers within the MPN, as well as in adjacent regions of the medial preoptic area of the adult male rat. For this, we used an indirect immunohistochemical method with antisera to serotonin (5HT), dopamine beta-hydroxylase (DBH), tyrosine hydroxylase (TH), neuropeptide Y (NPY), cholecystokinin (CCK), vasoactive intestinal polypeptide (VIP), substance P (SP), neurotensin (NT), corticotropin-releasing factor (CRF), luteotropin-releasing hormone (LRH), somatostatin (SS), thyrotropin-releasing hormone (TRH), oxytocin (OXY), vasopressin (VAS), adrenocorticotropic hormone (1-24; ACTH), alpha-melanocyte-stimulating hormone (alpha-MSH), leucine-enkephalin (L-ENK), and calcitonin gene-related peptide (CGRP). The results suggest that cell bodies and/or fibers crossreacting with all of these putative neurotransmitters are differentially distributed within the MPN. Within the MPNm, the densest plexuses of fibers were stained with antisera to SP and NPY, while moderate densities of fibers were stained with anti-DBH, SS, CCK, CGRP, ACTH, and alpha-MSH, and only a few fibers were stained with anti-5HT, TH, NT, VAS, and L-ENK. Moderate numbers of SP- and L-ENK-immunoreactive cell bodies, and a few SS-, NT-, CRF-, and TRH-stained cell bodies were also found within the MPNm. The MPNc contained a dense plexus of CCK-immunoreactive fibers, as well as a few CRF-immunoreactive fibers. Both fiber types were localized almost exclusively to this subdivision, while most of the others studied here appeared to avoid it selectively. This suggests that there are relatively few inputs to the MPNc, and that they tend to avoid other parts of the nucleus, although moderate densities of DBH- and NPY-immunoreactive fibers were found in both the MPNm and MPNc. The MPNc contained several CCK-immunoreactive cell bodies as well as a moderate number of TRH-stained cell bodies. Both cell types were nearly completely localized to the MPNc. The major inputs to the MPNl studied here appear to be stained with antisera to 5HT and L-ENK, although moderate numbers of NT- and CRF- immunoreactive fibers were also found in this part of the nucleus.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:Neurotransmitter specificity of cells and fibers in the medial preoptic nucleus: an immunohistochemical study in the rat. 242 28

While vasopressin and peptides of the bombesin family bind to different receptors in quiescent Swiss 3T3 cells, the antagonist [D-Arg1,D-pro2,D-Trp7,9,Leu11] substance P blocks the specific binding of both (3H) vasopressin and 125I-gastrin-releasing peptide to these cells. In addition, the antagonist inhibits the mobilization of Ca2+ and induction of DNA synthesis by vasopressin. These results indicate that [D-Arg1,D-Pro2,D-Trp7,9,Leu11] substance P has the ability to interact with the receptors for three structurally unrelated peptide hormones.
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PMID:A substance P antagonist also inhibits specific binding and mitogenic effects of vasopressin and bombesin-related peptides in Swiss 3T3 cells. 242 43

The effects of intrathecally administered arginine-vasopressin (AVP) and substance P (SP) on adrenal medullary secretion of epinephrine were examined in anesthetized Sprague-Dawley rats. Plasma epinephrine levels were measured in blood samples taken directly from the adrenal vein using a novel micropuncture technique. The blood samples (20-30 microliter in volume) were taken before, and 2 min, 15 min and 30 min after intrathecal injections of AVP, SP or vehicle only. Plasma was assayed for epinephrine using high pressure liquid chromatography. Adrenal venous epinephrine levels were not significantly altered by the intrathecal administration of AVP, thereby suggesting that adrenal epinephrine secretion is not involved in the cardiovascular responses previously reported to occur following similar doses of intrathecal AVP. Intrathecal SP administration, while causing blood pressure responses similar to those produced by AVP, resulted in significant increases in adrenal vein epinephrine. This finding suggests that activation of adrenal secretion of epinephrine may contribute to SP-initiated blood pressure changes.
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PMID:The effects of intrathecal administration of arginine-vasopressin and substance P on blood pressure and adrenal secretion of epinephrine in rats. 242 66

A bland procedure, conducted in ice, is described for the extraction with HCl of smooth-muscle-contracting substances from plexus-containing ileal longitudinal muscle (l.m.) sheets obtained mainly from rabbits and some guinea-pigs. The spasmogenic activity in rabbit extracts was distinguished from acetylcholine, histamine and 5-hydroxytryptamine by antagonists; and from prostaglandins, by its insolubility in ether at acid pH and by pretreatment of the animals with indomethacin. The fact that it contracts the separated l.m. of the guinea-pig ileum, whether plexus-containing or plexus-free, and in atropine distinguishes it also from methionine-enkephalin, somatostatin, 13-norleucine motilin, bombesin, and cholecystokinin octapeptide (CCK8). This activity was partially purified, first by several partitions with ether at pH 1.4-2.2 and then by treatment at pH 4.5-5 with lead acetate. The virtual absence of ATP was confirmed by the firefly bioluminescence technique. The guinea-pig-ileum-contracting component in the partially purified extracts was destroyed by pepsin, chymotrypsin and DPCC-treated trypsin, indicating its peptide nature and distinguishing it from oxytocin, vasopressin, bradykinin, etc. In parallel assays the partially purified rabbit extracts were considerably more active than Substance P on jird or rat ascending colons than on the guinea-pig l.m., suggesting the presence of a second spasmogenic component in the extracts. In guinea-pig extracts the partially purified activity was 8-16 times greater when plexus-containing than when plexus-free, pointing to Auerbach's plexus as the source of the activity.
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PMID:Extraction and partial purification of spasmogenic substances in Auerbach's plexus. 242 21

The neuropeptide field has witnessed considerable research interest over the past decade, and a growing body of anatomic, biochemical, and electrophysiologic data have since emerged, supporting the existence and putative neuromodulatory function of a large variety of these peptide hormones in several extrahypothalamic brain regions. It is now evident that neuropeptides not only fulfill criteria required of putative neurotransmitters, but more generally act as modulators of neuronal activity. The author discusses vasopressin and oxytocin pathways, corticotropin releasing factor, atrial natriuretic factor, thyrotropin releasing hormone, somatostatin, motilin, growth hormone releasing factor, dopamine, gonadotropin releasing hormone, and substance P.
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PMID:Chemical anatomy of the hypothalamus. 243 89

Vasopressin and related peptides cause behavioral excitation after intracerebroventricular injection in mice. This behavioral excitation is characterized by excessive scratching and grooming behavior in the unrestrained animal and enhanced escape-directed activity in stressful situations. These effects of vasopressin were found to be blocked by the administration of analogs which act as competitive antagonists of the pressor-activity of vasopressin. The potencies of these analogs in suppressing the behavioral effect paralleled the pressor antagonist potencies. The antagonists did not cause the characteristic behavioral alterations by themselves, nor did they block grooming and/or scratching behavior induced by the structurally-unrelated substances, mescaline, bombesin and substance P. It is suggested that these antagonists provide useful tools for studying the role of endogenous vasopressin in behavior.
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PMID:Specific antagonists of the acute behavioral response to centrally-administered vasopressin in mice. 243 82

Microvillar membranes derived from the brush border of the renal proximal tubule are very rich in peptidases. Pig kidney microvilli contain endopeptidase-24.11 associated with a battery of exopeptidases. The manner by which some neuropeptides are degraded by the combined attack of the peptidases of this membrane has been investigated. The contribution of individual peptidases was assessed by including inhibitors (phosphoramidon, captopril, amastatin and di-isopropyl fluorophosphate) with the membrane fraction when incubated with the peptides. Substance P, bradykinin and angiotensins I, II and III and insulin B-chain were rapidly hydrolysed by kidney microvilli. Oxytocin was hydrolysed much more slowly, but no products were detected from [Arg8]vasopressin or insulin under the conditions used for other peptides. The peptide bonds hydrolysed were identified and the contributions of the different peptidases were quantified. For each of the susceptible peptides, the main contribution came from endopeptidase-24.11 (inhibited by phosphoramidon). Peptidyl dipeptidase A (angiotensin-I-converting enzyme) was of less importance, even in respect of angiotensin I and bradykinin. When [2,3-Pro3,4-3H]bradykinin was also investigated at a lower concentration (20 nM), the conclusions in regard to the contributions of the two peptidases were unchanged. The possibility that endopeptidase-24.11 might attack within the six-residue disulphide-bridged rings of oxytocin and vasopressin was examined by dansyl(5-dimethylaminonaphthalene-1-sulphonyl)ation and by reduction and carboxymethylation of the products after incubation. Additional peptides were only observed after prolonged incubation, consistent with hydrolysis at the Tyr2-Ile3 and Tyr2-Phe3 bonds respectively. These results show that a range of neuropeptides are efficiently degraded by microvillar membranes and that endopeptidase-24.11 plays a key role in this process.
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PMID:Metabolism of neuropeptides. Hydrolysis of the angiotensins, bradykinin, substance P and oxytocin by pig kidney microvillar membranes. 243 10


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