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| | <channel> |
| | <title>pubmed: conotoxin</title> |
| | <link>https://www.ncbi.nlm.nih.gov/sites/entrez?cmd=Search&db=PubMed&term=conotoxin</link> |
| | <description>NCBI: db=pubmed; Term=conotoxin</description> |
| | <language>en-us</language> |
| | <docs>http://blogs.law.harvard.edu/tech/rss</docs> |
| | <ttl>1440</ttl> |
| | <image> |
| | <title>NCBI pubmed</title> |
| | <url>https://www.ncbi.nlm.nih.gov/entrez/query/static/gifs/iconsml.gif</url> |
| | <link>https://www.ncbi.nlm.nih.gov/sites/entrez</link> |
| | <description>PubMed comprises more than millions of citations for biomedical literature from MEDLINE, life science journals, and online books. Citations may include links to full-text content from PubMed Central and publisher web sites.</description> |
| | </image> |
| | <item> |
| | <title>Structural and Functional Characterization of Conotoxins from Conus achatinus Targeting NMDAR.</title> |
| | <link>https://www.ncbi.nlm.nih.gov/pubmed/32111068?dopt=Abstract</link> |
| | <description> |
| | <![CDATA[<table border="0" width="100%"><tr><td align="left"/><td align="right"><a href="https://www.ncbi.nlm.nih.gov/sites/entrez?db=pubmed&cmd=Link&LinkName=pubmed_pubmed&from_uid=32111068">Related Articles</a></td></tr></table> |
| | <p><b>Structural and Functional Characterization of Conotoxins from Conus achatinus Targeting NMDAR.</b></p> |
| | <p>Mar Drugs. 2020 Feb 26;18(3):</p> |
| | <p>Authors: Liu X, Yao G, Wang K, Liu Y, Wan X, Jiang H</p> |
| | <p>Abstract<br/> |
| | Conotoxin-Ac1 and its variant conotoxin-Ac1-O6P, were isolated from the venom duct of Conus achatinus, a fish-hunting cone snail species collected in the Sea of Hainan, China. Conotoxin-Ac1 is linear peptide that contain 15 amino acids. In the present study, we synthesized and structurally and functionally characterized conotoxin-Ac1 as well as 19 variants. Electrophysiological results showed that conotoxin-Ac1 inhibited N-methyl-D-aspartate receptor subunit 2B (NR2B) with an IC50 of 8.22 ± 0.022 μM. Further structure-activity studies of conotoxin-Ac demonstrated that polar amino acid residues were important for modulating its active, and the replacement of N1, O9, E10, and S12 by Ala resulted in a significant decrease in potency to NR2B. °Furthermore, conotoxin-Ac1 and conotoxin-Ac1-O6P were tested in hot-plate and tail-flick assays to measure the potential analgesic activity to an acute thermal stimulus in a dose-dependent manner. Subsequently, the analgesic activity of conotoxin-Ac1 mutants was analyzed by the hot-plate method. The results show that N1, Y2, Y3, E10, N11, S12, and T15 play an important role in the analgesic activity of conotoxin-Ac1. N1 and S12 have significant effects on conotoxin-Ac1 in inhibiting NR2B and analgesic activity. In conclusion, we have discovered that conotoxin-Ac1 is an inhibitor of NMDAR and displays antinociceptive activity.<br/> |
| | </p><p>PMID: 32111068 [PubMed - in process]</p> |
| | ]]></description> |
| | <author> Liu X, Yao G, Wang K, Liu Y, Wan X, Jiang H</author> |
| | <category>Mar Drugs</category> |
| | <guid isPermaLink="false">PubMed:32111068</guid> |
| | </item> |
| | <item> |
| | <title>Dimerization of α-conotoxins as a strategy to enhance the inhibition of the human α7 and α9α10 nicotinic acetylcholine receptors.</title> |
| | <link>https://www.ncbi.nlm.nih.gov/pubmed/32101438?dopt=Abstract</link> |
| | <description> |
| | <![CDATA[<table border="0" width="100%"><tr><td align="left"><a href="https://dx.doi.org/10.1021/acs.jmedchem.9b01536"><img alt="Icon for American Chemical Society" title="Read full text in American Chemical Society" src="//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg" border="0"/></a> </td><td align="right"><a href="https://www.ncbi.nlm.nih.gov/sites/entrez?db=pubmed&cmd=Link&LinkName=pubmed_pubmed&from_uid=32101438">Related Articles</a></td></tr></table> |
| | <p><b>Dimerization of α-conotoxins as a strategy to enhance the inhibition of the human α7 and α9α10 nicotinic acetylcholine receptors.</b></p> |
| | <p>J Med Chem. 2020 Feb 26;:</p> |
| | <p>Authors: Liang J, Tae HS, Xu X, Jiang T, Adams DJ, Yu R</p> |
| | <p>Abstract<br/> |
| | The affinity of α-conotoxins, a class of nicotinic acetylcholine receptor (nAChR) peptide inhibitors, can be enhanced by dendrimerization. It has been hypothesized that this improvement arose from simultaneous binding of the α-conotoxins to several spatially adjacent sites. We here engineered several α-conotoxin dimers using a linker length compatible between neighboring binding sites on the same receptor. Remarkably, the dimer of α-conotoxin PeIA compared to the monomer displayed an increase in potency by 11-fold (IC50 = 1.9 nM) for the human α9α10 nAChR. The dimerization of α-conotoxin, RgIA# resulted in a dual inhibitor that targets both α9α10 and α7 nAChR subtypes with an IC50 = ~50 nM. The RgIA# dimer is therapeutically interesting because it is the first dual inhibitor that potently and selectively inhibits these two nAChR subtypes, which are both involved in the aetiology of several cancers. We propose that the dimerization of α-conotoxins is a simpler and efficient alternative strategy to dendrimers for enhancing the activity of α-conotoxins.<br/> |
| | </p><p>PMID: 32101438 [PubMed - as supplied by publisher]</p> |
| | ]]></description> |
| | <author> Liang J, Tae HS, Xu X, Jiang T, Adams DJ, Yu R</author> |
| | <category>J Med Chem</category> |
| | <guid isPermaLink="false">PubMed:32101438</guid> |
| | </item> |
| | <item> |
| | <title>11-Keto-β-Boswellic Acid Attenuates Glutamate Release and Kainic Acid-Induced Excitotoxicity in the Rat Hippocampus.</title> |
| | <link>https://www.ncbi.nlm.nih.gov/pubmed/32097973?dopt=Abstract</link> |
| | <description> |
| | <![CDATA[<table border="0" width="100%"><tr><td align="left"><a href="http://www.thieme-connect.com/DOI/DOI?10.1055/a-1107-9337"><img alt="Icon for Georg Thieme Verlag Stuttgart, New York" title="Read full text in Georg Thieme Verlag Stuttgart, New York" src="//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.thieme.de-classic-images-tc-logo_tc.jpg" border="0"/></a> </td><td align="right"><a href="https://www.ncbi.nlm.nih.gov/sites/entrez?db=pubmed&cmd=Link&LinkName=pubmed_pubmed&from_uid=32097973">Related Articles</a></td></tr></table> |
| | <p><b>11-Keto-β-Boswellic Acid Attenuates Glutamate Release and Kainic Acid-Induced Excitotoxicity in the Rat Hippocampus.</b></p> |
| | <p>Planta Med. 2020 Feb 25;:</p> |
| | <p>Authors: Lu CW, Lin TY, Wang SJ</p> |
| | <p>Abstract<br/> |
| | Excessive glutamate concentration induces neuronal death in acute brain injuries and chronic neurodegenerative diseases. Natural compounds from medicinal plants have attracted considerable attention for their use in the prevention and treatment of neurological disorders. 11-Keto-β-boswellic acid, a triterpenoid found in the medicinal plant Boswellia serrata, has neuroprotective potential. The present study investigated the effect of 11-keto-β-boswellic acid on glutamate release in vitro and kainic acid-induced glutamate excitotoxicity in vivo in the rat hippocampus. In rat hippocampal nerve terminals (synaptosomes), 11-keto-β-boswellic acid dose-dependently inhibited 4-aminopyridine-stimulated glutamate release. This effect was dependent on extracellular calcium, persisted in the presence of the glutamate transporter inhibitor DL-threo-β-benzyloxyaspartate, and was blocked by the vesicular transporter inhibitor bafilomycin A1. In addition, 11-keto-β-boswellic acid reduced the 4-aminopyridine-induced increase in intrasynaptosomal Ca2+ levels. The N- and P/Q-type channel blocker ω-conotoxin MVIIC and the protein kinase A inhibitor H89 significantly suppressed the 11-keto-β-boswellic acid-mediated inhibition of glutamate release, whereas the intracellular Ca2+-releasing inhibitors dantrolene, CGP37157, and xestospongin C, mitogen-activated protein kinase inhibitor PD98059, as well as protein kinase C inhibitor calphostin C had no effect. In a rat model of excitotoxicity induced by intraperitoneal kainic acid injection (15 mg/kg), intraperitoneal 11-keto-β-boswellic acid administration (10 or 50 mg/kg) 30 min before kainic acid injection considerably ameliorated kainic acid-induced glutamate concentration elevation and CA3 neuronal death. These data suggested that 11-keto-β-boswellic acid inhibits glutamate release from the rat hippocampal synaptosomes by suppressing N- and P/Q-type Ca2+ channels and protein kinase A activity, as well as exerts protective effects against kainic acid-induced excitotoxicity in vivo.<br/> |
| | </p><p>PMID: 32097973 [PubMed - as supplied by publisher]</p> |
| | ]]></description> |
| | <author> Lu CW, Lin TY, Wang SJ</author> |
| | <category>Planta Med</category> |
| | <guid isPermaLink="false">PubMed:32097973</guid> |
| | </item> |
| | <item> |
| | <title>Synthesis of disulfide surrogate peptides incorporating large-span surrogate bridges through a native chemical ligation-assisted diaminodiacid strategy.</title> |
| | <link>https://www.ncbi.nlm.nih.gov/pubmed/32060988?dopt=Abstract</link> |
| | <description> |
| | <![CDATA[<table border="0" width="100%"><tr><td align="left"><a href="https://doi.org/10.1002/anie.201915358"><img alt="Icon for Wiley" title="Read full text in Wiley" src="//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-7388-69-wiley-full-text.png" border="0"/></a> </td><td align="right"><a href="https://www.ncbi.nlm.nih.gov/sites/entrez?db=pubmed&cmd=Link&LinkName=pubmed_pubmed&from_uid=32060988">Related Articles</a></td></tr></table> |
| | <p><b>Synthesis of disulfide surrogate peptides incorporating large-span surrogate bridges through a native chemical ligation-assisted diaminodiacid strategy.</b></p> |
| | <p>Angew Chem Int Ed Engl. 2020 Feb 14;:</p> |
| | <p>Authors: Qu Q, Gao S, Wu F, Zhang MG, Li Y, Zhang LH, Tian C, Zheng JS, Liu L</p> |
| | <p>Abstract<br/> |
| | The use of synthetic bridges as surrogates for disulfide bonds has emerged as a practical strategy to obviate the poor stability of some disulfide-containing peptides. However, peptides incorporating large-span synthetic bridges are still beyond the reach of existing methods. Here we report a native chemical ligation (NCL)-assisted diaminodiacid (DADA) strategy that enables the robust generation of disulfide surrogate peptides incorporating surrogate bridges up to 50 amino acids in length. This strategy provides access, for this first time, to some highly desirable but otherwise impossible-to-obtain disulfide surrogates of bioactive peptides, including μ-conotoxin KIIIA, a potent inhibitor of voltage-gated sodium channels. The bioactivities and structures of the synthetic disulfide surrogates were verified by voltage clamp assays, NMR, and X-ray crystallography; and stability studies established that the disulfide replacements effectively overcame the problems of disulfide reduction and scrambling that often plague these pharmacologically important peptides. By expanding access to structurally more diverse disulfide surrogate peptides, the NCL-assisted DADA strategy is expected to facilitate the development of peptide-based diagnostic and therapeutic agents.<br/> |
| | </p><p>PMID: 32060988 [PubMed - as supplied by publisher]</p> |
| | ]]></description> |
| | <author> Qu Q, Gao S, Wu F, Zhang MG, Li Y, Zhang LH, Tian C, Zheng JS, Liu L</author> |
| | <category>Angew Chem Int Ed Engl</category> |
| | <guid isPermaLink="false">PubMed:32060988</guid> |
| | </item> |
| | <item> |
| | <title>Cone snail analogs of the pituitary hormones oxytocin/vasopressin and their carrier protein neurophysin. Proteomic and transcriptomic identification of conopressins and conophysins.</title> |
| | <link>https://www.ncbi.nlm.nih.gov/pubmed/32058072?dopt=Abstract</link> |
| | <description> |
| | <![CDATA[<table border="0" width="100%"><tr><td align="left"><a href="https://linkinghub.elsevier.com/retrieve/pii/S1570-9639(20)30032-7"><img alt="Icon for Elsevier Science" title="Read full text in Elsevier Science" src="//www.ncbi.nlm.nih.gov/corehtml/query/egifs/https:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif" border="0"/></a> </td><td align="right"><a href="https://www.ncbi.nlm.nih.gov/sites/entrez?db=pubmed&cmd=Link&LinkName=pubmed_pubmed&from_uid=32058072">Related Articles</a></td></tr></table> |
| | <p><b>Cone snail analogs of the pituitary hormones oxytocin/vasopressin and their carrier protein neurophysin. Proteomic and transcriptomic identification of conopressins and conophysins.</b></p> |
| | <p>Biochim Biophys Acta Proteins Proteom. 2020 May;1868(5):140391</p> |
| | <p>Authors: Kumar S, Vijayasarathy M, Venkatesha MA, Sunita P, Balaram P</p> |
| | <p>Abstract<br/> |
| | Transcriptomic analysis of cone snail venom duct tissue has permitted the identification of diverse conopressin/conophysin precursor sequences from seven distinct Conus species. Multiple precursor isoforms are present in C.monile, C.lividus and C.loroisii. Aqueous extracts of the venom duct tissue from C.monile yield a band, at ~ 15-20 kDa on SDS-PAGE. In-gel trypsin digestion, followed by mass spectrometry establishes the presence of two distinct conopressin/conophysin isoforms that differ at position 8 in the predicted conopressin nonapeptide sequence. Mass spectrometric analysis of aqueous extracts revealed the presence of four conopressin related peptides, whose sequences could be deduced from MS/MS fragmentation patterns. The four sequences determined in this study are CFIRNCPKG*, CFIRNCPEG*, CFIRNCPK* and CFIRNCPE* (∗ indicates amide), which were further confirmed by comparison with chemically synthesized peptides. A conophysin with a mass of 9419.7 Da was also detected, corresponding to one of the isoforms revealed by the transcriptome data. Complete conservation of fourteen Cys residues and the key residues involved in peptide hormone binding is established by comparison of conophysin sequences, with the crystallographically characterized sequence of bovine neurophysin, in complex with vasopressin. A survey of available sequences for oxytocin/vasopressin peptides in both vertebrates and invertebrates establishes the conopressins as a distinct group in this family. C-terminal amidated, truncated conopressin analogs may arise by alternate post-translational processing.<br/> |
| | </p><p>PMID: 32058072 [PubMed - in process]</p> |
| | ]]></description> |
| | <author> Kumar S, Vijayasarathy M, Venkatesha MA, Sunita P, Balaram P</author> |
| | <category>Biochim Biophys Acta Proteins Proteom</category> |
| | <guid isPermaLink="false">PubMed:32058072</guid> |
| | </item> |
| | <item> |
| | <title>The inhibitory effect of Phα1β toxin on diabetic neuropathic pain involves the CXCR4 chemokine receptor.</title> |
| | <link>https://www.ncbi.nlm.nih.gov/pubmed/32016848?dopt=Abstract</link> |
| | <description> |
| | <![CDATA[<table border="0" width="100%"><tr><td align="left"/><td align="right"><a href="https://www.ncbi.nlm.nih.gov/sites/entrez?db=pubmed&cmd=Link&LinkName=pubmed_pubmed&from_uid=32016848">Related Articles</a></td></tr></table> |
| | <p><b>The inhibitory effect of Phα1β toxin on diabetic neuropathic pain involves the CXCR4 chemokine receptor.</b></p> |
| | <p>Pharmacol Rep. 2020 Feb;72(1):47-54</p> |
| | <p>Authors: da Silva Junior CA, de Castro Junior CJ, Pereira EMR, Binda NS, da Silva JF, do Nascimento Cordeiro M, Diniz DM, Cecilia FS, Ferreira J, Gomez MV</p> |
| | <p>Abstract<br/> |
| | BACKGROUND: Diabetic neuropathy is a common cause of painful diabetic neuropathy (PDN). C-X-C chemokine receptor type 4 (CXCR4) expression is increased in peripheral nerve samples from diabetes patients, suggesting a role for CXCR4 in PDN. Therefore, we evaluated the effects of Phα1β, ω-conotoxin MVIIA, and AMD3100 in a model of streptozotocin (STZ)-induced PDN in rodents and naïve model of rats with the activation of the CXCR4/stromal cell-derived factor 1 (SDF-1) signal.<br/> |
| | METHODS: Diabetic neuropathy was induced by intraperitoneal (ip) injection of STZ in Wistar rats. Naïve rats were intrathecally injected with SDF-1 to test the CXCR4/SDF-1 signal. The effects of Phα1β intrathecal (it), ω-conotoxin MVIIA intrathecal (it), and AMD3100 intraperitoneal (ip) on rat hypersensitivity, IL-6, and the intracellular calcium [Ca2+]i content of diabetic synaptosomes were studied.<br/> |
| | RESULTS: The drugs reduced the hypersensitivity in diabetic rats. SDF-1 (1.0 µg/it) administration in naïve rats induced hypersensitivity. Phα1β (100 pmol/it) or AMD3100 (2.5 µg/ip) reduced this hypersensitivity after 2 h treatments, while ω-conotoxin MVIIA did not have an effect. IL-6 and [Ca2+]i content increased in the spinal cord synaptosomes in diabetic rats. The drug treatments reduced IL-6 and the calcium influx in diabetic synaptosomes.<br/> |
| | CONCLUSIONS: Phα1β, ω-conotoxin MVIIA, and AMD3100, after 2 h of treatment of STZ-induced PDN, reduced hypersensitivity in diabetic rats. In naïve rats with CXCR4/SDF-1 activation, the induced hypersensitivity decreased after 2 h treatments with Phα1β or AMD-3100, while ω-conotoxin MVIIA did not affect. The inhibitory effects of Phα1β on PDN may involve voltage-dependent calcium channels.<br/> |
| | </p><p>PMID: 32016848 [PubMed - in process]</p> |
| | ]]></description> |
| | <author> da Silva Junior CA, de Castro Junior CJ, Pereira EMR, Binda NS, da Silva JF, do Nascimento Cordeiro M, Diniz DM, Cecilia FS, Ferreira J, Gomez MV</author> |
| | <category>Pharmacol Rep</category> |
| | <guid isPermaLink="false">PubMed:32016848</guid> |
| | </item> |
| | <item> |
| | <title>Structure and Activity Studies of Disulfide-Deficient Analogues of αO-Conotoxin GeXIVA.</title> |
| | <link>https://www.ncbi.nlm.nih.gov/pubmed/31986036?dopt=Abstract</link> |
| | <description> |
| | <![CDATA[<table border="0" width="100%"><tr><td align="left"><a href="https://dx.doi.org/10.1021/acs.jmedchem.9b01409"><img alt="Icon for American Chemical Society" title="Read full text in American Chemical Society" src="//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg" border="0"/></a> </td><td align="right"><a href="https://www.ncbi.nlm.nih.gov/sites/entrez?db=pubmed&cmd=Link&LinkName=pubmed_pubmed&from_uid=31986036">Related Articles</a></td></tr></table> |
| | <p><b>Structure and Activity Studies of Disulfide-Deficient Analogues of αO-Conotoxin GeXIVA.</b></p> |
| | <p>J Med Chem. 2020 Feb 27;63(4):1564-1575</p> |
| | <p>Authors: Xu P, Kaas Q, Wu Y, Zhu X, Li X, Harvey PJ, Zhangsun D, Craik DJ, Luo S</p> |
| | <p>Abstract<br/> |
| | αO-conotoxin GeXIVA from Conus generalis is a potent antagonist of the α9α10 nAChR and analgesic in animal models of pain. This peptide has two disulfide bond cross-links, and the bead and ribbon isomers have similar inhibitory activity against α9α10 nAChRs. We synthesized 12 disulfide-deficient analogues of bead GeXIVA, and all remained potent inhibitors of α9α10 nAChR. The most potent disulfide-deficient analogue displayed IC50 values of 6 and 33 nM at rat and human α9α10 nAChRs, respectively, representing less than a 2-fold increase compared with bead GeXIVA. The disulfide-deficient analogs and parent peptides also do not have a well-defined structure according to NMR spectroscopy. Molecular simulations suggest that the disulfide bonds and termini of GeXIVA do not establish stable interactions with the receptor. Overall, this study proposes that the structure of the analgesic peptide GeXIVA could be simplified through disulfide bond deletions and potentially termini truncations.<br/> |
| | </p><p>PMID: 31986036 [PubMed - in process]</p> |
| | ]]></description> |
| | <author> Xu P, Kaas Q, Wu Y, Zhu X, Li X, Harvey PJ, Zhangsun D, Craik DJ, Luo S</author> |
| | <category>J Med Chem</category> |
| | <guid isPermaLink="false">PubMed:31986036</guid> |
| | </item> |
| | <item> |
| | <title>Expression of α3β2β4 nicotinic acetylcholine receptors by rat adrenal chromaffin cells determined using novel conopeptide antagonists.</title> |
| | <link>https://www.ncbi.nlm.nih.gov/pubmed/31967330?dopt=Abstract</link> |
| | <description> |
| | <![CDATA[<table border="0" width="100%"><tr><td align="left"><a href="https://doi.org/10.1111/jnc.14966"><img alt="Icon for Wiley" title="Read full text in Wiley" src="//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-7388-69-wiley-full-text.png" border="0"/></a> </td><td align="right"><a href="https://www.ncbi.nlm.nih.gov/sites/entrez?db=pubmed&cmd=Link&LinkName=pubmed_pubmed&from_uid=31967330">Related Articles</a></td></tr></table> |
| | <p><b>Expression of α3β2β4 nicotinic acetylcholine receptors by rat adrenal chromaffin cells determined using novel conopeptide antagonists.</b></p> |
| | <p>J Neurochem. 2020 Jan 22;:</p> |
| | <p>Authors: Hone AJ, Rueda-Ruzafa L, Gordon TJ, Gajewiak J, Christensen S, Dyhring T, Albillos A, McIntosh JM</p> |
| | <p>Abstract<br/> |
| | Adrenal chromaffin cells release neurotransmitters in response to stress and may be involved in conditions such as post-traumatic stress and anxiety disorders. Neurotransmitter release is triggered, in part, by activation of nicotinic acetylcholine receptors (nAChRs). However, despite decades of use as a model system for studying exocytosis, the nAChR subtypes involved have not been pharmacologically identified. Quantitative real-time PCR of rat adrenal medulla revealed an abundance of mRNAs for α3, α7, β2, and β4 subunits. Whole-cell patch-clamp electrophysiology of chromaffin cells and subtype-selective ligands were used to probe for nAChRs derived from the mRNAs found in adrenal medulla. A novel conopeptide antagonist, PeIA-5469, was created that is highly selective for α3β2 over other nAChR subtypes heterologously expressed in Xenopus laevis oocytes. Experiments using PeIA-5469 and the α3β4-selective α-conotoxin TxID revealed that rat adrenal medulla contain two populations of chromaffin cells that express either α3β4 nAChRs alone or α3β4 together with the α3β2β4 subtype. Conclusions were derived from observations that acetylcholine-gated currents in some cells were sensitive to inhibition by PeIA-5469 and TxID, while in other cells, currents were sensitive only to TxID. Expression of functional α7 nAChRs was determined using three α7-selective ligands: the agonist PNU282987, the positive allosteric modulator PNU120596, and the antagonist α-conotoxin [V11L,V16D]ArIB. The results of these studies identify for the first time the expression of α3β2β4 nAChRs as well as functional α7 nAChRs by rat adrenal chromaffin cells.<br/> |
| | </p><p>PMID: 31967330 [PubMed - as supplied by publisher]</p> |
| | ]]></description> |
| | <author> Hone AJ, Rueda-Ruzafa L, Gordon TJ, Gajewiak J, Christensen S, Dyhring T, Albillos A, McIntosh JM</author> |
| | <category>J Neurochem</category> |
| | <guid isPermaLink="false">PubMed:31967330</guid> |
| | </item> |
| | <item> |
| | <title>Differential Expression of Nicotine Acetylcholine Receptors Associates with Human Breast Cancer and Mediates Antitumor Activity of αO-Conotoxin GeXIVA.</title> |
| | <link>https://www.ncbi.nlm.nih.gov/pubmed/31963558?dopt=Abstract</link> |
| | <description> |
| | <![CDATA[<table border="0" width="100%"><tr><td align="left"/><td align="right"><a href="https://www.ncbi.nlm.nih.gov/sites/entrez?db=pubmed&cmd=Link&LinkName=pubmed_pubmed&from_uid=31963558">Related Articles</a></td></tr></table> |
| | <p><b>Differential Expression of Nicotine Acetylcholine Receptors Associates with Human Breast Cancer and Mediates Antitumor Activity of αO-Conotoxin GeXIVA.</b></p> |
| | <p>Mar Drugs. 2020 Jan 17;18(1):</p> |
| | <p>Authors: Sun Z, Zhangsun M, Dong S, Liu Y, Qian J, Zhangsun D, Luo S</p> |
| | <p>Abstract<br/> |
| | Nicotinic acetylcholine receptors (nAChRs) are membrane receptors and play a major role in tumorigenesis and cancer progression. Here, we have investigated the differential expression of nAChR subunits in human breast cancer cell lines and breast epithelial cell lines at mRNA and protein levels and the effects of the αO-conotoxin GeXIVA, antagonist of α9α10 nAChR, on human breast cancer cells. Reverse transcription polymerase chain reaction (PCR) demonstrated that all nAChR subunits, except α6, were expressed in the 20 tested cell lines. Real time quantitative PCR (QRT-PCR) suggested that the mRNA of α5, α7, α9 and β4 nAChR subunits were overexpressed in all the breast cancer cell lines compared with the normal epithelial cell line HS578BST. α9 nAChR was highly expressed in almost all the breast cancer cell lines in comparison to normal cells. The different expression is prominent (p <0.001) as determined by flow cytometry and Western blotting, except for MDA-MB-453 and HCC1395 cell lines. αO-conotoxin GeXIVA that targeted α9α10 nAChR were able to significantly inhibit breast cancer cell proliferation in vitro and merits further investigation as potential agents for targeted therapy.<br/> |
| | </p><p>PMID: 31963558 [PubMed - in process]</p> |
| | ]]></description> |
| | <author> Sun Z, Zhangsun M, Dong S, Liu Y, Qian J, Zhangsun D, Luo S</author> |
| | <category>Mar Drugs</category> |
| | <guid isPermaLink="false">PubMed:31963558</guid> |
| | </item> |
| | <item> |
| | <title>RgIA4 Accelerates Recovery from Paclitaxel-Induced Neuropathic Pain in Rats.</title> |
| | <link>https://www.ncbi.nlm.nih.gov/pubmed/31877728?dopt=Abstract</link> |
| | <description> |
| | <![CDATA[<table border="0" width="100%"><tr><td align="left"/><td align="right"><a href="https://www.ncbi.nlm.nih.gov/sites/entrez?db=pubmed&cmd=Link&LinkName=pubmed_pubmed&from_uid=31877728">Related Articles</a></td></tr></table> |
| | <p><b>RgIA4 Accelerates Recovery from Paclitaxel-Induced Neuropathic Pain in Rats.</b></p> |
| | <p>Mar Drugs. 2019 Dec 21;18(1):</p> |
| | <p>Authors: Huynh PN, Giuvelis D, Christensen S, Tucker KL, McIntosh JM</p> |
| | <p>Abstract<br/> |
| | Chemotherapeutic drugs are widely utilized in the treatment of human cancers. Painful chemotherapy-induced neuropathy is a common, debilitating, and dose-limiting side effect for which there is currently no effective treatment. Previous studies have demonstrated the potential utility of peptides from the marine snail from the genus Conus for the treatment of neuropathic pain. α-Conotoxin RgIA and a potent analog, RgIA4, have previously been shown to prevent the development of neuropathy resulting from the administration of oxaliplatin, a platinum-based antineoplastic drug. Here, we have examined its efficacy against paclitaxel, a chemotherapeutic drug that works by a mechanism of action distinct from that of oxaliplatin. Paclitaxel was administered at 2 mg/kg (intraperitoneally (IP)) every other day for a total of 8 mg/kg. Sprague Dawley rats that were co-administered RgIA4 at 80 µg/kg (subcutaneously (SC)) once daily, five times per week, for three weeks showed significant recovery from mechanical allodynia by day 31. Notably, the therapeutic effects reached significance 12 days after the last administration of RgIA4, which is suggestive of a rescue mechanism. These findings support the effects of RgIA4 in multiple chemotherapeutic models and the investigation of α9α10 nicotinic acetylcholine receptors (nAChRs) as a non-opioid target in the treatment of chronic pain.<br/> |
| | </p><p>PMID: 31877728 [PubMed - in process]</p> |
| | ]]></description> |
| | <author> Huynh PN, Giuvelis D, Christensen S, Tucker KL, McIntosh JM</author> |
| | <category>Mar Drugs</category> |
| | <guid isPermaLink="false">PubMed:31877728</guid> |
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