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)

Immunological and biological studies have shown that many of the mammalian gastroenteropancreatic (GEP) hormones have counterparts in lower vertebrates. Hormonal localization in cyclostomes and fishes suggests that insulin was phylogenetically the first islet hormone, followed by somatostatin, glucagon and, last, pancreatic polypeptide (PP). Some of the GEP peptides are present in the central and peripheral nervous system of lower vertebrates as well as mammals. GEP hormone-like substances resembling insulin, somatostatin, glucagon, PP, gastrin, secretin, VIP, substance P and enkephalin also occur in protostomian invertebrates (Annelida, Arthropoda, Mollusca), particularly in their nervous system. These findings indicate that the vertebrate hormones may have originated in neural tissue before the development of the vertebrate line of evolution.
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PMID:Gut-islet endocrinology-some evolutionary aspects. 615 46

Substance P-, neurotensin- and bombesin-like immunoreactivities were localised in some gill epithelial cells in the pharynx of Ciona intestinalis L. No immunoreactivity was obtained with antisera to gastrin, glucagon, insulin, pancreatic polypeptide or calcitonin. Some of the epithelial cells of the gills were shown to be argyrophilic with the Grimelius technique.
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PMID:Substance P-, neurotensin- and bombesin-like immunoreactivities in the gill epithelium of Ciona intestinalis L. 615 65

Nine polypeptides of gastrointestinal origin were tested for their possible effect on vascular smooth muscle of the rat portal vein. The substances tested were bombesin, caerulein, glucagon, insulin, pentagastrin, secretin, somatostatin, substance P and vasoactive intestinal polypeptide (VIP). Cumulative dose-response relations of integrated mechanical activity (mean tension) were obtained with maximal concentrations of the various peptides of 1-10 microgram/ml. Within this concentration range, only substance P and VIP showed clearcut effects; substance P causing contraction and VIP relaxation. The dose of substance P needed to produce contraction was high (ED50 greater than 1 microM) so that the physiological importance of this response is doubtful. On the other hand, ED50 for the relaxing effect of VIP was about 15 nM, which is in accordance with concentrations reported to produce significant vasodilatation in vivo. The results support the view that vascular effects which have been reported to occur in response to the other 7 peptides are mainly of indirect origin and not mediated via direct action on vascular smooth muscle.
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PMID:Effects of nine different gastrointestinal polypeptides on vascular smooth muscle in vitro. 616 66

C-peptide immunoreactivity (CPR) levels were measured in dog superior pancreaticoduodenal vein using synthetic dog C-peptide and its antiserum. The basal CPR level was approximately twice as high as the basal immunoreactive insulin (IRI) level on a molar basis. Glucose (10 mg/kg/min) or arginine (250 mg/kg/min) infusion for 5 min into the superior pancreaticoduodenal artery caused a prompt, parallel increase in IRI and CPR. IRI and CPR were closely equimolar at peak secretions. One bolus administration of synthetic neurotensin (10 microgram/kg) into the same artery produced a mild hyperglycemic response and biphasic IRI and CPR responses at 30 min in the vein. The IRI and CPR increases were closely equimolar during the first phase of secretion, but during the second peak a larger increase was found in CPR than IRI. Upon infusion of synthetic substance P (50 ng/kg/min) for 30 min, IRI and CPR concentrations showed a parallel and closely equimolar fall. These results indicate that insulin and C-peptide were released from beta cells in equimolar concentrations.
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PMID:Immunoreactive dog C-peptide level in the pancreatic vein. 616 71

Substance P is present in numerous organs (salivary glands, trachea, pancreas, kidneys, bladder and prostate) and in various parts of the central and peripheral nervous system, notably substantia nigra, hypothalamus, pineal body and dorsal horn of the spinal cord. It is a potent stimulant of salivary secretion and intestinal motility, a vasodilator in muscles and fatty tissues and an inhibitor of insulin release. Its main role, however, lies in the transmission of pain, where it seems to act as neuromodulator. Released when nociceptive fibers are activated at the same time as the fast-acting neuromediator, it enhances and prolongs the effects of the latter. Opiates inhibit its release. In addition, substance P is present in the excitatory neurones of the corpus striatum-substantia nigra pathway, which also has GABA-containing inhibitory neurones, and this pathway is known to modulate the dopaminergic nigra-striatum pathway. The global function of substance P, therefore, seems to keep the central nervous system in a state of alert through activation of the cerebral cortex and assistance in the transmission of pain.
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PMID:[Substance P]. 616 77

Using rabbit and guinea-pig antisera, raised against GEP neurohormonal peptides of mammalian origin, cells were observed in the brain and/or in the fused ventral ganglia of the last (fifth) larval instar of the hoverfly, Eristalis aeneus, being immunoreactive with antisera against insulin, somatostatin, glucagon, PP, secretin, gastrin/CCK/caerulein; substance P, enkephalin and endorphin. Most of these GEP neurohormonal peptides also occurred in nerve fibers. No immunoreactive cells or nerve fibers could be detected with antisera against GIP, VIP, (the central fragments of) CCK, bombesin or neurotensin. The antisera tested failed to reveal any immunoreactive cells or nerves in Weismann's ring (fused corpus allatum/corpus cardiacum and thoracic gland) or in different parts of the alimentary tract. The observations support the hypothesis that neuronal GEP hormonal peptide production in the brain is a genuinely original mechanism and the appearance of endocrine cells in the gut a later feature in evolution.
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PMID:Immunohistochemical evidence of gastro-entero-pancreatic neurohormonal peptides of vertebrate type in the nervous system of the larva of a dipteran insect, the hoverfly, Eristalis aeneus. 616 52

The unique specificity of Achromobacter protease I for lysine residue was investigated using synthetic and natural substrates, i.e., lysine derivatives, arginine derivatives, lysine vasopressin, substance P, ACTH and insulin. The enzyme cleaved only the -Lys-X- bonds in the above substrates. The binding affinity of alkylamines as determined by Ki was much stronger than that of the corresponding alkylguanidines.
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PMID:Studies on a new proteolytic enzyme from Achromobacter lyticus M497-1. II. specificity and inhibition studies of Achromobacter protease I. 616 93

The neuropeptide substance P forms polymeric fibrils similar to those previously reported for the hormone, insulin. Structural and chemical aspects of these two fibrillary forms have been compared and their possible existence in vivo considered. Numerous substance P fibrils are readily formed in vitro in mM solutions under conditions which are physiological with respect to salt concentration, pH and temperature, whereas more severe conditions (heat and acid) are apparently required for the rapid formation of numerous insulin fibrils. Morphologically, both fibrils appear to be relatively long and unbranched and the neuropeptide fibrils are similar in size to such naturally occurring structures as neurofilaments. Disaggregation of the neuropeptide fibril follows dilution (1000-fold) whilst more stringent (alkaline) treatment is apparently necessary for insulin fibril dissociation. These observations are discussed in relation to the role of an insulin-like peptide in the formation of certain types of amyloid and the possibility that fibrillary of similar polymeric forms of substance P may exist in normal tissue.
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PMID:Properties and possible significance of substance P and insulin fibrils. 617 29

Twenty-five endocrine tumors of the rectum (rectal carcinoids) were examined immunohistochemically for various pancreatic and gut neurohormonal polypeptides. Twenty-one of the tumors were found to contain cells displaying pancreatic polypeptide (PP), glucagon, somatostatin, insulin, substance P, enkephalin or beta-endorphin immunoreactivity. At least 11 of the tumors contained more than one peptide hormone. In some of the tumors PP cells made up the major cell population, in others the glucagon cells constituted the majority. Only four of the tumors contained 5-hydroxytryptamine. Rectal endocrine tumors seem unique among gut endocrine tumors in that they may store immunoreactive enkephalin, beta-endorphin and even insulin. None of the patients displayed the carcinoid syndrome; symptoms were usually vague and uncharacteristic. In many cases the tumor was found at routine examination.
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PMID:Immunohistochemical evidence of peptide hormones in endocrine tumors of the rectum. 617 Apr 21

The distribution of gastrin-, cholecystokinin-, glucagon-, secretin-, vasoactive intestinal polypeptide-, substance P-, bombesin-, neurotensin-, motilin-, somatostatin- and avian pancreatic polypeptide-like cells, demonstrated by indirect immunocytochemistry, was studied in samples from the following regions: proventriculus, gizzard, pylorus, duodenum, upper and lower ileum, caeca and rectum. The pylorus is particularly rich in gastrin-, neurotensin- and somatostatin-like cells. No cells immunoreactive for gastric inhibitory polypeptide or insulin were detected. In a number of instances the same cells were found to stain with antisera raised to different gut peptides. This happened with antisera detecting gastrin- and neurotensin-like cells, with secretin, vasoactive intestinal polypeptide, glucagon and substance P. The possibility that antigenic determinants to more than one peptide are contained in certain endocrine-like cells is considered.
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PMID:An immunocytochemical survey of endocrine cells in the gastrointestinal tract of chicks at hatching. 617 Apr 46


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