A sorghum xylanase inhibitor-like protein with highly potent antifungal, antitumor and HIV-1 reverse transcriptase inhibitory activities.
Identifieur interne : 001A00 ( Main/Exploration ); précédent : 001999; suivant : 001A01A sorghum xylanase inhibitor-like protein with highly potent antifungal, antitumor and HIV-1 reverse transcriptase inhibitory activities.
Auteurs : Peng Lin [République populaire de Chine] ; Jack Ho Wong ; Tzi Bun Ng ; Vincent Sai Man Ho ; Lixin XiaSource :
- Food chemistry [ 1873-7072 ] ; 2013.
Descripteurs français
- KwdFr :
- Animaux, Antienzymes (), Antienzymes (isolement et purification), Antienzymes (pharmacologie), Antifongiques (), Antifongiques (isolement et purification), Antifongiques (pharmacologie), Antinéoplasiques d'origine végétale (), Antinéoplasiques d'origine végétale (isolement et purification), Antinéoplasiques d'origine végétale (pharmacologie), Champignons (), Cinétique, Endo-1,4-beta xylanases (), Endo-1,4-beta xylanases (antagonistes et inhibiteurs), Graines (), Humains, Lignée cellulaire tumorale, Prolifération cellulaire (), Protéines végétales (), Protéines végétales (isolement et purification), Protéines végétales (pharmacologie), Sorghum (), Souris, Stabilité protéique, Transcriptase inverse du VIH (), Transcriptase inverse du VIH (antagonistes et inhibiteurs).
- MESH :
- antagonistes et inhibiteurs : Endo-1,4-beta xylanases, Transcriptase inverse du VIH.
- isolement et purification : Antienzymes, Antifongiques, Antinéoplasiques d'origine végétale, Protéines végétales.
- pharmacologie : Antienzymes, Antifongiques, Antinéoplasiques d'origine végétale, Protéines végétales.
- Animaux, Antienzymes, Antifongiques, Antinéoplasiques d'origine végétale, Champignons, Cinétique, Endo-1,4-beta xylanases, Graines, Humains, Lignée cellulaire tumorale, Prolifération cellulaire, Protéines végétales, Sorghum, Souris, Stabilité protéique, Transcriptase inverse du VIH.
English descriptors
- KwdEn :
- Animals, Antifungal Agents (chemistry), Antifungal Agents (isolation & purification), Antifungal Agents (pharmacology), Antineoplastic Agents, Phytogenic (chemistry), Antineoplastic Agents, Phytogenic (isolation & purification), Antineoplastic Agents, Phytogenic (pharmacology), Cell Line, Tumor, Cell Proliferation (drug effects), Endo-1,4-beta Xylanases (antagonists & inhibitors), Endo-1,4-beta Xylanases (chemistry), Enzyme Inhibitors (chemistry), Enzyme Inhibitors (isolation & purification), Enzyme Inhibitors (pharmacology), Fungi (drug effects), HIV Reverse Transcriptase (antagonists & inhibitors), HIV Reverse Transcriptase (chemistry), Humans, Kinetics, Mice, Plant Proteins (chemistry), Plant Proteins (isolation & purification), Plant Proteins (pharmacology), Protein Stability, Seeds (chemistry), Sorghum (chemistry).
- MESH :
- chemical , antagonists & inhibitors : Endo-1,4-beta Xylanases, HIV Reverse Transcriptase.
- chemical , chemistry : Antifungal Agents, Antineoplastic Agents, Phytogenic, Endo-1,4-beta Xylanases, Enzyme Inhibitors, HIV Reverse Transcriptase, Plant Proteins.
- chemical , isolation & purification : Antifungal Agents, Antineoplastic Agents, Phytogenic, Enzyme Inhibitors, Plant Proteins.
- chemical , pharmacology : Antifungal Agents, Antineoplastic Agents, Phytogenic, Enzyme Inhibitors, Plant Proteins.
- chemistry : Seeds, Sorghum.
- drug effects : Cell Proliferation, Fungi.
- Animals, Cell Line, Tumor, Humans, Kinetics, Mice, Protein Stability.
Abstract
A 25-kDa protein, with an N-terminal amino acid sequence homologous to that of xylanase inhibitor and designated as xylanase inbibitor-like protein (XILP) was purified from sorghum seeds. The isolation protocol consisted of affinity chromatography, ion exchange chromatography, and gel filtration. XILP inhibited mycelial growth in various phytopathogenic fungi. The antifungal activity was thermostable and pH-stable. XILP inhibited proliferation of various cancer cell lines but did not do so in human embryonic liver (WRL 68) cells. There was no mitogenic activity toward mouse splenocytes. XILP reduced the activity of HIV-1 reverse transcriptase with an IC50 of 11.1μM, but lacked inhibitory activity toward HIV-1 integrase and SARS coronavirus proteinase. In conclusion, sorghum XILP is thermostable and pH stable and exhibits potent antifungal, antiproliferative, and HIV-1 reverse transcriptase inhibitory activities.
DOI: 10.1016/j.foodchem.2013.04.013
PubMed: 23871041
Affiliations:
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Le document en format XML
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(chemistry)</term><term>Humans</term><term>Kinetics</term><term>Mice</term><term>Plant Proteins (chemistry)</term><term>Plant Proteins (isolation & purification)</term><term>Plant Proteins (pharmacology)</term><term>Protein Stability</term><term>Seeds (chemistry)</term><term>Sorghum (chemistry)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Antienzymes ()</term><term>Antienzymes (isolement et purification)</term><term>Antienzymes (pharmacologie)</term><term>Antifongiques ()</term><term>Antifongiques (isolement et purification)</term><term>Antifongiques (pharmacologie)</term><term>Antinéoplasiques d'origine végétale ()</term><term>Antinéoplasiques d'origine végétale (isolement et purification)</term><term>Antinéoplasiques d'origine végétale (pharmacologie)</term><term>Champignons ()</term><term>Cinétique</term><term>Endo-1,4-beta xylanases ()</term><term>Endo-1,4-beta xylanases (antagonistes et inhibiteurs)</term><term>Graines 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xml:lang="en">A 25-kDa protein, with an N-terminal amino acid sequence homologous to that of xylanase inhibitor and designated as xylanase inbibitor-like protein (XILP) was purified from sorghum seeds. The isolation protocol consisted of affinity chromatography, ion exchange chromatography, and gel filtration. XILP inhibited mycelial growth in various phytopathogenic fungi. The antifungal activity was thermostable and pH-stable. XILP inhibited proliferation of various cancer cell lines but did not do so in human embryonic liver (WRL 68) cells. There was no mitogenic activity toward mouse splenocytes. XILP reduced the activity of HIV-1 reverse transcriptase with an IC50 of 11.1μM, but lacked inhibitory activity toward HIV-1 integrase and SARS coronavirus proteinase. In conclusion, sorghum XILP is thermostable and pH stable and exhibits potent antifungal, antiproliferative, and HIV-1 reverse transcriptase inhibitory activities. </div></front></TEI><affiliations><list><country><li>République populaire de Chine</li></country><settlement><li>Sha Tin</li></settlement><orgName><li>Université chinoise de Hong Kong</li></orgName></list><tree><noCountry><name sortKey="Ho, Vincent Sai Man" sort="Ho, Vincent Sai Man" uniqKey="Ho V" first="Vincent Sai Man" last="Ho">Vincent Sai Man Ho</name><name sortKey="Ng, Tzi Bun" sort="Ng, Tzi Bun" uniqKey="Ng T" first="Tzi Bun" last="Ng">Tzi Bun Ng</name><name sortKey="Wong, Jack Ho" sort="Wong, Jack Ho" uniqKey="Wong J" first="Jack Ho" last="Wong">Jack Ho Wong</name><name sortKey="Xia, Lixin" sort="Xia, Lixin" uniqKey="Xia L" first="Lixin" last="Xia">Lixin Xia</name></noCountry><country name="République populaire de Chine"><noRegion><name sortKey="Lin, Peng" sort="Lin, Peng" uniqKey="Lin P" first="Peng" last="Lin">Peng Lin</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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