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)

Neurotropin, a nonprotein component extracted from the skin of rabbits treated with vaccinia virus, has been clinically and experimentally reported to demonstrate analgesic effects. In this study, we investigated the antinociceptive action of neurotropin in relation to the serotonergic system, a pain inhibitory system, and substance P, a pain transmitter; we also attempted to determine whether it acts at the spinal or supraspinal level in mice. 1) The spinal cord (T6-T10) transection completely abolished the antinociceptive action of neurotropin, attenuated that of morphine, and had no influence on the action of clonidine. 2) The intrathecal substance P-induced behavior was inhibited by [D-Pro2, D-Trp7,9]-substance P, but not by neurotropin. 3) Preadministration of p-chlorophenylalanine or cyproheptadine inhibited the antinociceptive action of neurotropin. These data suggest that neurotropin does not directly act on pain transmitters at the spinal cord level, but acts at the supraspinal level, resulting in an inhibition of pain transmitter release at the spinal level by mediating pain inhibitory systems such as the serotonergic system in addition to the noradrenergic and GABAergic systems previously reported.
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PMID:Analgesic mechanism of neurotropin: relation to the serotonergic system and influence of spinal cord transection. 248 Apr 65

The rat preprotachykinin I gene mRNA is alternatively spliced to yield three different mRNA species differing in their protein coding regions. We have produced recombinant vaccinia viruses expressing alpha-, beta-, and gamma-preprotachykinin to examine the tachykinin-related peptides produced upon post-translational processing of each individual precursor. Infection of BSC-40 or AtT-20 cell lines with a beta-preprotachykinin-encoding vaccinia virus recombinant results in the expression of the precursor protein. The pro-form (signal peptide removed) can be immunoprecipitated from extracts of infected cells. Infected cells of both types secrete into the culture medium a product(s) which reacts in radioimmunoassay with an antiserum shown to recognize precursor as well as mature substance P. Infected AtT-20, but not BSC-40, cells secrete into the culture medium a processed form(s) of beta-preprotachykinin which reacts in radioimmunoassay with an anti-serum which recognizes the amidated carboxyl terminus of substance P. The molecular nature of the tachykinin products produced in and secreted from AtT-20 cells infected with alpha-, beta-, and gamma-preprotachykinin-encoding recombinants was analyzed by combined high performance liquid chromatography and radioimmunoassay. Peptides were identified based on comigration with synthetic standards and antisera cross-reactivity. We determined that alpha-preprotachykinin is processed to the mature undecapeptide, substance P. beta-Preprotachykinin was processed into multiple products, including substance P, neurokinin A, neurokinin A(3-10), and neuropeptide K. gamma-Preprotachykinin was processed into substance P, neurokinin A, neurokinin A(3-10), and neuropeptide gamma. These five tachykinin peptide products were all routed through the regulated secretory pathway and were secreted into the medium in a cAMP-stimulatable fashion. Since all of these peptides have been shown to be biologically active, it is important to consider the biological consequences of their co-secretion in vivo.
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PMID:Multiple tachykinins are produced and secreted upon post-translational processing of the three substance P precursor proteins, alpha-, beta-, and gamma-preprotachykinin. Expression of the preprotachykinins in AtT-20 cells infected with vaccinia virus recombinants. 276 79