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)

We have investigated the neurogenic factors inducing relaxation in the intraocular segment of the bovine long posterior ciliary artery. In precontracted vessels, electrical field stimulation (EFS, 0.5-128 Hz, 10 s trains) in the presence of guanethidine (30 microM) evoked biphasic relaxation: optimal relaxation for the first and second components occurred at 10 and 50 s, respectively. The first component, but not the second, was abolished by L-NAME (100 microM) or ODQ (3 microM). Relaxation to exogenous CGRP (0.1-300 nM) was inhibited by the CGRP antagonist, CGRP(8-37) (1-5 microM), but neither component of neurogenic relaxation was affected. Preincubation with the sensory nerve excitotoxin, capsaicin (1 microM), had no effect on either the first or second components of neurogenic relaxation. Substance P (0.1 nM-0.1 microM) induced relaxation, but rapid and complete desensitisation occurred within minutes. Neither desensitisation to substance P (0.1 microM) nor incubation with the NK(1) antagonist, L-733,060 (0.3 microM), had any effect on the first or second components of neurogenic relaxation.VIP (0.1 nM-0.3 microM) induced relaxation and this was followed by substantial desensitisation. Neither desensitisation to VIP (0.6 microM) nor treatment with the protease, alpha-chymotrypsin (10 U ml(-1)), had any effect on the first or second components of neurogenic relaxation. The results indicate that nitric oxide mediates the first component of neurogenic relaxation in the bovine intraocular ciliary artery. The neurotransmitter mediating the second component remains to be determined but is unlikely to be CGRP, substance P or VIP.
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PMID:Biphasic neurogenic vasodilatation in the bovine intraocular long posterior ciliary artery: involvement of nitric oxide and an additional unidentified neurotransmitter. 1591 33

The present study was designed to characterize the urinary bladder-derived relaxant factor that was demonstrated by acetylcholine-induced relaxation response in a coaxial bioassay system consisting of rat bladder as the donor organ and rat anococcygeus muscle as the assay tissue. The concentration-dependent relaxation to acetylcholine (10 nM-1 mM) was inhibited by atropine but was not altered by the antagonists of calcitonin gene-related peptide (CGRP 8-37), vasoactive intestinal peptide (VIP 6-28), tachykinin NK1 (L-732138), tachykinin NK2 (MEN-10376), tachykinin NK3 (SB-218795), purinergic P2 (PPADS) and adenosine (CGS 15943) receptors as well as alpha-chymotrypsin. Adenylate cyclase inhibitor SQ-22536 and protein kinase A inhibitor KT-5720 significantly inhibited the acetylcholine response while guanylate cyclase inhibitor ODQ, and protein kinase C inhibitor H-7 did not have any effect. The P2X agonist alpha,beta-methylene ATP (10 nM-0.1 mM) also produced concentration-dependent relaxation response that was inhibited by PPADS, SQ-22536 and KT-5720 in the coaxial bioassay system. In bladder strips, acetylcholine and alpha,beta-methylene ATP elicited concentration-dependent contractions that were not altered in the presence of SQ-22536 and KT-5720. In conclusion, the urinary bladder-derived relaxant factor that was recognized by the coaxial bioassay system is neither a peptide of the bladder neurons nor a purinergic mediator but adenylate cyclase and protein kinase A are involved in its release and/or relaxant effect. Furthermore, activation of purinergic P2X receptors besides the muscarinic receptors leads to the release of this factor.
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PMID:Rat urinary bladder-derived relaxant factor: studies on its nature and release by coaxial bioassay system. 1862 Oct 43

We previously substantiated that Ci-TK, a tachykinin of the protochordate, Ciona intestinalis (Ci), triggered oocyte growth from the vitellogenic stage (stage II) to the post-vitellogenic stage (stage III) via up-regulation of the gene expression and enzymatic activity of the proteases: cathepsin D, carboxypeptidase B1, and chymotrypsin. In the present study, we have elucidated the localization, gene expression and activation profile of these proteases. In situ hybridization showed that the Ci-cathepsin D mRNA was present exclusively in test cells of the stage II oocytes, whereas the Ci-carboxypeptidase B1 and Ci-chymotrypsin mRNAs were detected in follicular cells of the stage II and stage III oocytes. Double-immunostaining demonstrated that the immunoreactivity of Ci-cathepsin D was largely colocalized with that of the receptor of Ci-TK, Ci-TK-R, in test cells of the stage II oocytes. Ci-cathepsin D gene expression was detected at 2h after treatment with Ci-TK, and elevated for up to 5h, and then slightly decreased. Gene expression of Ci-carboxypeptidase B1 and Ci-chymotrypsin was observed at 5h after treatment with Ci-TK, and then decreased. The enzymatic activities of Ci-cathepsin D, Ci-carboxypeptidase B1, and Ci-chymotrypsin showed similar alterations with 1-h lags. These gene expression and protease activity profiles verified that Ci-cathepsin D is initially activated, which is followed by the activation of Ci-carboxypeptidase B1 and Ci-chymotrypsin. Collectively, the present data suggest that Ci-TK directly induces Ci-cahtepsin D in test cells expressing Ci-TK receptor, leading to the secondary activation of Ci-chymotrypsin and Ci-carboxypeptidase B1 in the follicle in the tachykininergic oocyte growth pathway.
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PMID:Localization and enzymatic activity profiles of the proteases responsible for tachykinin-directed oocyte growth in the protochordate, Ciona intestinalis. 2182 5


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