Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UNIPROT:P20366 (substance P)
 21,176 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Twenty-two endocrine carcinomas of the skin were examined immunohistochemically for the presence of several polypeptides and serotonin. Eight tumors contained one or more polypeptides. Occasional cells containing calcitonin were found in several tumors. Rare cells with substance P, somatostatin, and ACTH were present in only one tumor each. None of the patients presented a clinical syndrome associated with any of these polypeptides. Met-enkephalin and serotonin were negative in all tumors. The lack of demonstration of met-enkephalin in these tumors makes their relationship to the Merkel cell uncertain.
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PMID:Immunohistochemical studies in endocrine carcinoma of the skin. 620 32

Characteristics of histamine (Hi) and 5-hydroxytryptamine (5-HT) release from rat peritoneal mast cells in response to the polypeptide adrenocorticotropin (ACTH) were studied. During a 15 min incubation at 37 degrees C, ACTH evoked Hi as well as 5-HT release from rat mast cells at concentrations of 1 X 10(-4) M-1 X 10(-3) M. The release was dose-dependent and very rapid. After 15 sec the amount of the amines released was the same as after 4.5 min. In most experiments, the percentage of Hi release was slightly but significantly higher than the percentage of 5-HT release. Hi and 5-HT release induced by ACTH also took place in a calcium-free medium. However, the release of the amines was decreased when calcium was omitted. Comparison of the effects of ACTH, compound 48/80 and substance P on mast cell secretion showed that ACTH is about 100 times less active then substance P which was in turn about 100 times less active than compound 48/80. When both ACTH and compound 48/80 were used together as liberators , the release was significantly higher than with either liberator alone. Our results indicate that there are receptor sites for the endogenous polypeptide ACTH on the mast cell membrane which mediate Hi and 5-HT release. This release was found to resemble that evoked by the basic secretogogue compound 48/80 but in some aspects to be different from that evoked by substance P.
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PMID:The effect of adrenocorticotropin on histamine and 5-hydroxytryptamine secretion from rat mast cells. 620 67

Synaptic connections between substance P (SP)- and ACTH-containing neurons in the rat arcuate nucleus were studied by a technique of combined pre- and postembedding immunohistochemical staining. The results showed that immunoreactive (ir) SP fiber terminals form synapses with ir ACTH cell bodies. This strongly suggests that the activity of ACTH neurons is under neuronal regulation by SP neurons.
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PMID:Synaptic regulation of hypothalamic neurons containing ACTH by substance P. 620 17

The discovery of opiate receptors has resulted in the isolation of endogenous morphinomimetics called endorphins. The enkephalins, which are pentapeptides, are located diffusely within the brain and are thought to act locally as neuromodulators for the release of noradrenaline, dopamine and substance P. beta-endorphin, a peptide with 31 aminoacids, is released from the pituitary with ACTH during stress. The peptide sequency of the common precursor of these hormones, pro-opiocortin, is now established.
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PMID:[Endorphins: neuromodulators and hormones (author's transl)]. 625 35

125I-angiotensin II (125I-AII) binding was examined in the hypothalamic-thalamic-septal-midbrain (HTSM) region of HLA-Wistar rats in the presence of CNS-active agents. Angiotensin I, II, and III and saralasin competed for 125 I-AII binding, whereas structurally unrelated peptides such as arginine and lysine vasopressin, oxytocin, LHRH, TRH, bradykinin, and substance P did not. In contrast, ACTH and neurotensin exhibited a weak, dose-dependent competition for 125 I-AII binding. The relative potencies of AII, AI, neurotensin and ACTH were 100:1:0.1:0.05, respectively. Neurotensin and ACTH competition was not additive with AII suggesting interaction at shared binding sites. Most importantly, a wide variety of other CNS active agents such as methyldopa, naloxone, catecholamines, clondidine, and reserpine, failed to inhibit 125 I-AII binding, thus further defining the specificity of the CNS AII receptor.
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PMID:The specificity of angiotensin II receptor binding in rat brain. 627 72

Polypeptide-hormone producing cells were localized in the alimentary tract and cerebral ganglion of Ciona intestinalis using cytochemical, immunocytochemical and electron-microscopical methods. Antisera to the following peptides of vertebrate type were employed: bombesin, human prolactin (hPRL), bovine pancreatic polypeptide (PP), porcine secretin, motilin, vasoactive intestinal polypeptide (VIP), beta-endorphin, leu-enkephalin, met-enkephalin, neurotensin, 5-hydroxytryptamin (5-HT), cholecystokinin (CCK), human growth (GH), ACTH, corticotropin-like intermediate lobe peptide (CLIP) and gastric inhibitory peptide (GIP). Immunoreactive cells were found both in the alimentary tract epithelium and in the cerebral ganglion for bombesin, PP, substance P, somatostatin, secretin and neurotensin. Additionally, in the cerebral ganglion only, there were cells immunoreactive for beta-endorphin, VIP, motilin and human prolactin. 5-HT positive cells, however, were restricted to the alimentary tract. No immunoreactivity was obtained either in the cerebral ganglion or in the alimentary tract with antibodies to leu-enkephalin, met-enkephalin, CCK, growth hormone, ACTH, CLIP and GIP. Prolactin-immunoreactive and pancreatic polypeptide-immunoreactive cells were argyrophilic with the Grimelius' stain and were found in neighbouring positions in the cerebral ganglion. At the ultrastructural level five differently granulated cell types were distinguished in the cerebral ganglion. Granules were present in the perikarya as well as in axons. The possible functions of the peptides as neurohormones, neuroregulators and neuromodulators are discussed.
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PMID:Gastro-intestinal and neurohormonal peptides in the alimentary tract and cerebral complex of Ciona intestinalis (Ascidiaceae). 627 5

Peptide extracts of rat brain powerfully inhibited the cyclic AMP phosphodiesterase activity of rat brain homogenate. Similar extracts of ox brain showed comparable although less potent activity. Preliminary investigation of the physicochemical properties of brain extracts indicated that the rat brain extract contained an active peptide of low molecular weight (about 1400), whereas ox brain contained two such peptides (about 1400 and 900). These studies indicate that endogenous oligopeptides that inhibit cyclic AMP phosphodiesterase are present in brain. Experiments on several pure peptides known to be present in brain. Experiments on several pure peptides known to be present in the CNS showed that the majority were inactive against brain phosphodiesterase, but ACTH(1-24), somatostatin, substance P and Lys8-vasopressin, in descending order of potency, were active. To help distinguish the peptides found in rat and ox brain extracts from known peptides, preliminary analyses of amino acid composition were performed. These suggested that the peptides found in brain extracts were distinct from known peptides having the ability to inhibit cyclic AMP phosphodiesterase.
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PMID:Endogenous peptides that inhibit brain cyclic AMP phosphodiesterase. 628 80

Tonin, an esteroprotease isolated from rat submaxillary gland, is a serine protease with trypsin- and chymotrypsin-like activity. The substrate specificity of tonin shows that it differs from kallikreins and is definitely not a renin-like enzyme or an angiotensin-converting enzyme. Tonin can produce directly the vasoactive peptide angiotensin II, from angiotensin I, angiotensinogen and the synthetic tetradecapeptide substrate of renin by cleavage of a Phe-His bond. It has also been found to cleave some Phe and Arg bonds in various substrates such as beta-lipotropin (beta-LPH), adrenocorticotropin (ACTH), pro-opiomelanocortin (POMC) and substance P. Here we describe the complete amino acid sequence of rat submaxillary gland, tonin. Comparison of the sequence of 219 amino acids with other serine proteases, particularly kallikreins, gamma-subunit of nerve growth factor (NGF) and the recently described gamma-renin, reveals extensive similarities. More interestingly, it also reveals the substitution of an Asp residue always found in the serine protease active site triad (Asp, His, Ser) by a Leu residue. This unusual substitution does not seem to affect the proteolytic activity of the enzyme.
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PMID:Amino acid sequence of rat submaxillary tonin reveals similarities to serine proteases. 632 14

The frontal ganglion of the adult forms of the tobacco hornworm, Manduca sexta, was investigated immunocytochemically for the occurrence of the gastro-entero-pancreatic (GEP) neurohormonal peptides, namely insulin, nerve growth factor, epidermal growth factor, insulin C-peptide, somatostatin, glucagon, glicentin, pancreatic polypeptide (PP), polypeptide YY (PYY), secretin, vasoactive intestinal peptide (VIP), gastric inhibitory peptide (GIP), gastrin, cholecystokinin (CCK), enkephalin, alpha- and beta-endorphins, substance P, neurotensin, bombesin, motilin, ACTH, serotonin, and calcitonin. Among all the antisera tested, positive immunostaining was obtained with anti-insulin B-chain serum only. The insulin B-chain immunoreactivity was localized in 4-6 large (30-40 microns) neurons, in the neuropile, and in the recurrent nerve. It is speculated that the insulin-like immunoreactive material may be transported to the neurohaemal organ (corpora cardiaca) through the nervi cardiaco-somatogastrici.
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PMID:Immunocytochemical evidence for the occurrence of insulin in the frontal ganglion of a Lepidopteran insect, the tobacco hornworm moth, Manduca sexta L. 637 93

Calmodulin (CaM) binding by turkey gizzard myosin light chain kinase (MLCK) causes subtle changes in the fluorescence emission and polarization excitation spectra of the enzyme. Fluorescence experiments using 9-anthroyl-choline (9AC), which competes with ATP in binding, demonstrate mutually stabilizing interactions between the CaM and ATP binding sites corresponding to delta G = -0.6 to -0.7 kcal/mol. Fluorescence titrations in the presence of 9AC or 5,5'-bis[8-(phenylamino)-1-naphthalenesulfonate] confirm the stoichiometry of 1 mol of CaM/MLCK. Phosphorylation of MLCK has no effect on either the protein fluorescence or the binding of ATP and 9AC. The dissociation constant for the MLCL-CaM complex is increased approximately 500-fold on phosphorylation. Values of Kd for the phosphorylated enzyme range from 0.5 to 1.1 microM in 0.2 N KCl, pH 7.3, 25 degrees C. We showed competition between MLCK and other CaM binding proteins and peptides by using both fluorescence and catalytic activity measurements. Competition for CaM occurs with ACTH, beta-endorphin, substance P, glucagon, poly(L-arginine), myelin basic protein, troponin I, and histone H2A. Phosphorylation of the last three proteins by the adenosine cyclic 3',5'-phosphate dependent protein kinase diminishes their ability to compete. Phosphorylation of MLCK by the protein kinase gives 0.95 +/- 0.04 and 2.2 +/- 0.4 mol of incorporated 32P in the presence and absence of CaM, respectively. These stoichiometries agree with those recently reported [Conti, M. A. & Adelstein, R. S. (1981) J. Biol. Chem. 256, 3178].
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PMID:Functional interactions between smooth muscle myosin light chain kinase and calmodulin. 689 95


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