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)

Polylysine, polyornithine and, to a lesser extent, polyarginine were found to stimulate the GTPase activity of the purified recombinant alpha subunit of the human G(i)-3 transducing protein alpha i-3. Optimal stimulation of 4- to 5-fold was obtained with polylysine concentrations between 1 and 20 microM, higher concentrations being inhibitory. Polylysine at similar concentrations stimulated by 50% the GTPase of transducin (GT), the vision transducing protein, but had only a very slight effect on the GTPase of the p21 product of the H-ras protooncogene. The stimulation of the alpha i-3 GTPase caused by polylysine was due to a reduction of the apparent Km for GTP from 3.8 to 1.3 microM. The stimulation by polylysine was observed at free Mg2+ concentrations below 1 microM. These results indicate that polylysine acts in a fashion similar to mastoparan and substance P in mimicking the action of an agonist-bound receptor on G-proteins.
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PMID:Differential stimulation of the GTPase activity of G-proteins by polylysine. 151 Jul 3

A sensitive alpha-amidating enzyme (alpha AE) assay using C-terminal glycine-extended substance P (SP-Gly) as a substrate was developed. The product, substance P (SP), was measured by a radioimmunoassay with specific polyclonal antibodies which recognize SP with an affinity 10,000-fold higher than that of SP-Gly. The sensitivity of the radioimmunoassay was 5 fmol. Enzyme activity could be readily detected with 25 ng alpha AE partially purified from the conditioned medium of rat medullary thyroid carcinoma CA-77 cells. The Km and Vmax values were 2.0 +/- 0.2 microM and 1.7 +/- 0.1 nmol/mg/min (mean +/- SE, n = 3), respectively. The assay enabled the kinetic characterization of alpha AE from a single rat pituitary homogenate. Optimal Cu2+ required was 30 microM and greater than 3 mM of ascorbate was needed for maximal enzyme activity. The sensitivity of this assay will aid efforts to examine the regulation of in vivo alpha AE activity.
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PMID:A radioimmunoassay for measuring alpha-amidating enzyme activity. 169 69

Rat peritoneal mast cells co-cultured with mouse 3T3 fibroblasts (MC/3T3) are fully responsive to immunologic stimuli. To assess their nonimmunologic activation MC/3T3 were challenged with various peptides. Optimal concentrations of substance P (10(-4) M) and bradykinin (5 x 10(-5) M) induced histamine release of 58.2 +/- 9.3 and 66.8 +/- 6.6%, respectively, while neurotensin (10(-4) M) released only 16.6 +/- 3.7% histamine. Freshly isolated mast cells (F-MC) challenged with the same concentrations of peptides released lower percentages of histamine (substance P 45.6 +/- 5.1%, bradykinin 32.5 +/- 5.3%, neurotensin 11.3 +/- 6.0%). In both MC/3T3 and F-MC, only minute amounts of prostaglandin D2 (PGD2) were produced. In contrast, activation with anti-IgE antibodies and compound 48/80 caused both histamine release and PGD2 generation. Compound 48/80-stimulated MC/3T3 and F-MC released 80.2 +/- 3.4 and 51.8 +/- 6.2% histamine, respectively, and produced 15.4 +/- 2.8 ng/10(6) mast cells and 3.9 +/- 1.4 ng/10(6) mast cells PGD2, respectively. These findings indicate that peptides and bradykinin induce selective release of histamine with no PGD2 production in both F-MC and MC/3T3. Moreover, MC/3T3 preserve their functional characteristics of connective tissue mast cells since they are fully responsive to these peptides as F-MC.
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PMID:Differential release of histamine and prostaglandin D2 in rat peritoneal mast cells activated with peptides. 248 57

Specific binding sites for somatostatin have been identified in cytosolic fraction of rabbit kidney (cortex and outer medulla) using 125I-Tyr11-somatostatin. The binding was saturable and reversible, as well as time and temperature dependent. Optimal pH for binding was observed at about 7.4. Scatchard plots were compatible with the existence of two classes of binding sites: a first class with a high affinity (Kd = 40 nM) and a low binding capacity (2.0 pmol somatostatin/mg protein) and a second class with a low affinity (Kd = 222 nM) and a high binding capacity (114.3 pmol somatostatin/mg protein). Vasoactive intestinal peptide, neurotensin, substance P, Leu-enkephalin and vasopressin had practically no effect on somatostatin binding. The properties of these binding sites strongly support the concept that somatostatin could behave as a regulatory peptide on the rabbit kidney.
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PMID:Evidence for somatostatin binding sites in rabbit kidney. 287 91

The production of recombinant anti-HIV peptide, T-20, in Escherichia coli was optimized by statistical experimental designs (successive designs with multifactors) such as 2(4-1) fractional factorial, 2(3) full factorial, and 2(2) rotational central composite design in order. The effects of media compositions (glucose, NPK sources, MgSO4, and trace elements), induction level, induction timing (optical density at induction process), and induction duration (culture time after induction) on T-20 production were studied by using a statistical response surface method. A series of iterative experimental designs was employed to determine optimal fermentation conditions (media and process factors). Optimal ranges characterized by %T-20 (proportion of peptide to the total cell protein) were observed, narrowed down, and further investigated to determine the optimal combination of culture conditions, which was as follows: 9, 6, 10, and 1 mL of glucose, NPK sources, MgSO4, and trace elements, respectively, in a total of 100 mL of medium inducted at an OD of 0.55-0.75 with 0.7 mM isopropyl-beta-D-thiogalactopyranoside in an induction duration of 4 h. Under these conditions, up to 14% of T-20 was obtained. This statistical optimization allowed the production of T-20 to be increased more than twofold (from 6 to 14%) within a shorter induction duration (from 6 to 4 h) at the shake-flask scale.
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PMID:Sequential and simultaneous statistical optimization by dynamic design of experiment for peptide overexpression in recombinant Escherichia coli. 1705 56

Mucociliary activity is an important clearance mechanism in the respiratory system of air breathing vertebrates. Substance P (SP) and acetylcholine play a key role in the stimulation of the mucociliary transport in the frog palate. In this study, retrograde neuronal tracing was combined with immunocytochemistry for SP and choline acetyl transferase (ChAT) in the trigeminal ganglion and for neurokinin-1 receptor (NK1R) in the palate of Rana pipiens. The cells of origin of the palatine nerve were identified in the trigeminal ganglion using the retrograde tracer Fluorogold (FG). Optimal labeling of FG cells in the trigeminal ganglion was obtained at 96 h of exposure. Immunoflorescent shows that SP and acetylcholine are co-localized in 92% of the cells labeled with FG in the trigeminal ganglion. NK1 receptors were found in the membrane of epithelial and goblet cells of the palate. Ultrastructural study of the palate showed axonal-like endings with vesicles in connection with epithelial and goblet cells. These results further support the concerted action of both neurotransmitters in the regulation of mucociliary activity in the frog palate.
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PMID:Substance P and acetylcholine are co-localized in the pathway mediating mucociliary activity in Rana pipiens. 1727 13