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Article ; Online: Bioactive Proteins in Panax notoginseng Roots and Other Panax Species.

Chan, Yau Sang / Wong, Jack Ho / Ng, Tzi Bun

2018 Volume 20, Issue 3, Page(s) 231–239

Abstract: The genus Panax consists of a group of prized medicinal herbs. Major members of the Panax genus include P. ginseng, P. notoginseng, P. quinquefolius, and P. vietnamensis. They possess various bioactive constituents such as ginsenosides, saponins, ... ...

Abstract	The genus Panax consists of a group of prized medicinal herbs. Major members of the Panax genus include P. ginseng, P. notoginseng, P. quinquefolius, and P. vietnamensis. They possess various bioactive constituents such as ginsenosides, saponins, polysaccharides and proteins. Many of them were reported to show beneficial effects on human health. Ginsenosides and saponins of ginsengs caught the sight of most researchers. Precise investigations revealed their roles on improvement of the functioning of the nervous system, cardiovascular system, and other functions. In contrast, our knowledge of the bioactive Panax proteins is relatively limited. A number of proteins from P. ginseng, the most valuable member of Panax species, have been investigated and proved to be beneficial to our body. Meanwhile, a few bioactive P. notoginseng proteins, such as ribonucleases and antifungal proteins, have been characterized and reported. We summarize herein the proteins present in P. notoginseng that have been identified, and try to compare them with those from other Panax species with a similar structure or bioactivity, and conclude whether the proteins in P. notoginseng have any distinctive features.
MeSH term(s)	Animals ; Humans ; Panax notoginseng/chemistry ; Plant Proteins/chemistry ; Plant Proteins/metabolism ; Plant Proteins/pharmacology ; Plant Roots/chemistry
Chemical Substances	Plant Proteins
Language	English
Publishing date	2018-06-12
Publishing country	United Arab Emirates
Document type	Journal Article ; Review
ZDB-ID	2045662-1
ISSN	1875-5550 ; 1389-2037
ISSN (online)	1875-5550
ISSN	1389-2037
DOI	10.2174/1389203719666180612083650
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Article ; Online: Shiga toxins: from structure and mechanism to applications.

Chan, Yau Sang / Ng, Tzi Bun

Applied microbiology and biotechnology

2015 Volume 100, Issue 4, Page(s) 1597–1610

Abstract: Shiga toxins are a group of type 2 ribosome-inactivating proteins (RIPs) produced in several types of bacteria. The toxins possess an AB5 structure, which comprises a catalytic A chain with N-glycosidase activity, and five identical B chains and ... ...

Abstract	Shiga toxins are a group of type 2 ribosome-inactivating proteins (RIPs) produced in several types of bacteria. The toxins possess an AB5 structure, which comprises a catalytic A chain with N-glycosidase activity, and five identical B chains and recognize and bind to the target cells with specific carbohydrate moieties. In humans, the major molecular target which recognizes the Shiga toxins is the Gb3 receptor, which is mainly expressed on the cell surface of endothelial cells of the intestine, kidney, and the brain. This causes these organs to be susceptible to the toxicity of Shiga toxins. When a person is infected by Shiga toxin-producing bacteria, the toxin is produced in the gut, translocated to the circulatory system, and carried to the target cells. Toxicity of the toxin causes inflammatory responses and severe cell damages in the intestine, kidneys, and brain, bringing about the hemolytic uremic syndrome (HUS), which can be fatal. The Shiga toxin requires a couple of steps to exert its toxicity to the target cells. After binding with the target cell surface receptor, the toxin requires a complicated process to be transported into the cytosol of the cell before it can approach the ribosomes. The mechanisms for the interactions of the toxin with the cells are described in this review. The consequences of the toxin on the cells are also discussed. It gives an overview of the steps for the toxin to be produced and transported, expression of catalytic activity, and the effects of the toxin on the target cells, as well as effects on the human body.
MeSH term(s)	Brain/drug effects ; Brain/pathology ; Endothelial Cells/drug effects ; Globosides/metabolism ; Humans ; Intestines/drug effects ; Intestines/pathology ; Kidney/drug effects ; Kidney/pathology ; Protein Synthesis Inhibitors/chemistry ; Protein Synthesis Inhibitors/metabolism ; Protein Synthesis Inhibitors/toxicity ; Protein Transport ; Ribosomes/drug effects ; Shiga Toxins/chemistry ; Shiga Toxins/metabolism ; Shiga Toxins/toxicity ; Trihexosylceramides/metabolism
Chemical Substances	Globosides ; Protein Synthesis Inhibitors ; Shiga Toxins ; Trihexosylceramides ; globotrihexosylceramide
Language	English
Publishing date	2015-12-19
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	392453-1
ISSN	1432-0614 ; 0171-1741 ; 0175-7598
ISSN (online)	1432-0614
ISSN	0171-1741 ; 0175-7598
DOI	10.1007/s00253-015-7236-3
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Article ; Online: Bauhinia variegata var. variegata lectin: isolation, characterization, and comparison.

Chan, Yau Sang / Ng, Tzi Bun

Applied biochemistry and biotechnology

2015 Volume 175, Issue 1, Page(s) 75–84

Abstract: Bauhinia variegata var. variegata seeds are rich in proteins. Previously, one of the major storage proteins of the seeds was found to be a trypsin inhibitor that possessed various biological activities. By using another purification protocol, a glucoside- ...

Abstract	Bauhinia variegata var. variegata seeds are rich in proteins. Previously, one of the major storage proteins of the seeds was found to be a trypsin inhibitor that possessed various biological activities. By using another purification protocol, a glucoside- and galactoside-binding lectin that demonstrated some differences from the previously reported B. variegata lectin could be isolated from the seeds. It involved affinity chromatography on Affi-gel blue gel, ion exchange chromatography on Q-Sepharose and Mono Q, and also size exclusion chromatography on Superdex 75. The lectin was not retained on Affi-gel blue gel but interacted with Q-Sepharose. The lectin was a 64-kDa protein with two 32-kDa subunits. It had low thermostability (stable up to 50 °C) and moderate pH stability (stable in pH 3-10). It exhibited anti-proliferative activity on nasopharyngeal carcinoma HONE1 cells with an IC50 of 12.8 μM after treatment for 48 h. It also slightly inhibited the growth of hepatoma HepG2 cells. The lectin may have potential in aiding cancer treatments.
MeSH term(s)	Bauhinia/chemistry ; Cell Proliferation/drug effects ; Hep G2 Cells ; Humans ; Lectins/chemistry ; Lectins/isolation & purification ; Lectins/pharmacology ; Protein Stability ; Seeds/chemistry
Chemical Substances	Lectins
Language	English
Publishing date	2015-01
Publishing country	United States
Document type	Journal Article
ZDB-ID	392344-7
ISSN	1559-0291 ; 0273-2289
ISSN (online)	1559-0291
ISSN	0273-2289
DOI	10.1007/s12010-014-1261-z
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Article ; Online: Northeast red beans produce a thermostable and pH-stable defensin-like peptide with potent antifungal activity.

Chan, Yau Sang / Ng, Tzi Bun

Cell biochemistry and biophysics

2013 Volume 66, Issue 3, Page(s) 637–648

Abstract: A 5.4-kDa antifungal peptide was purified from Phaseolus vulgaris L. cv. "northeast red bean" using a protocol that entailed affinity chromatography, ion exchange chromatography, and gel filtration. The molecular mass was determined by matrix-assisted ... ...

Abstract	A 5.4-kDa antifungal peptide was purified from Phaseolus vulgaris L. cv. "northeast red bean" using a protocol that entailed affinity chromatography, ion exchange chromatography, and gel filtration. The molecular mass was determined by matrix-assisted laser desorption ionization time-of-flight. The N-terminal amino acid sequence of the peptide was highly homologous to defensins and defensin-like peptides from several plant species. The peptide impeded the growth of a number of pathogenic fungi, including Mycosphaerella arachidicola Khokhr. (IC50 = 1.7 μM), Setosphaeria turcica Luttr., Fusarium oxysporum Schltdl., and Valsa mali Miyabe & G. Yamada. Antifungal activity of the peptide was fully preserved at temperatures up to 100 °C and pH values from 0 to 12. Congo red deposition at the hyphal tip of M. arachidicola was detected after exposure to the peptide, signifying that the peptide had suppressed hyphal growth. The antifungal peptide did not manifest antiproliferative activity toward human breast cancer MCF7 cells and hepatoma HepG2 cells, in contradiction to the bulk of previously reported plant defensins. The data suggest distinct structural requirements for antifungal and antiproliferative activities.
MeSH term(s)	Amino Acid Sequence ; Antifungal Agents/chemistry ; Antifungal Agents/isolation & purification ; Antifungal Agents/pharmacology ; Defensins/chemistry ; Fungi/drug effects ; Hydrogen-Ion Concentration ; Molecular Sequence Data ; Phaseolus/chemistry ; Plant Proteins/chemistry ; Plant Proteins/isolation & purification ; Plant Proteins/pharmacology ; Protein Stability ; Temperature
Chemical Substances	Antifungal Agents ; Defensins ; Plant Proteins
Language	English
Publishing date	2013-07
Publishing country	United States
Document type	Journal Article
ZDB-ID	1357904-6
ISSN	1559-0283 ; 1085-9195
ISSN (online)	1559-0283
ISSN	1085-9195
DOI	10.1007/s12013-012-9508-1
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Article ; Online: A lectin with highly potent inhibitory activity toward breast cancer cells from edible tubers of Dioscorea opposita cv. nagaimo.

Chan, Yau Sang / Ng, Tzi Bun

PloS one

2013 Volume 8, Issue 1, Page(s) e54212

Abstract: A 70-kDa galactose-specific lectin was purified from the tubers of Dioscorea opposita cv. nagaimo. The purification involved three chromatographic steps: anion exchange chromatography on a Q-Sepharose column, FPLC-anion exchange chromatography on a Mono ... ...

Abstract	A 70-kDa galactose-specific lectin was purified from the tubers of Dioscorea opposita cv. nagaimo. The purification involved three chromatographic steps: anion exchange chromatography on a Q-Sepharose column, FPLC-anion exchange chromatography on a Mono Q column, and FPLC-gel filtration on a Superdex 75 column. The purified nagaimo lectin presented as a single 35-kDa band in reducing SDS-PAGE while it exhibited a 70-kDa single band in non-reducing SDS-PAGE suggesting its dimeric nature. Nagaimo lectin displayed moderate thermostability, retaining full hemagglutinating activity after heating up to 62°C for 30 minutes. It also manifested stability over a wide pH range from pH 2 to 13. Nagaimo lectin was a galactose-specific lectin, as evidenced by binding with galactose and galactose-containing sugars such as lactose and raffinose. The minimum concentration of galactose, lactose and raffinose required to exert an inhibitory effect on hemagglutinating activity of nagaimo lectin was 20 mM, 5 mM and 40 mM, respectively. Nagaimo lectin inhibited the growth of some cancer cell lines including breast cancer MCF7 cells, hepatoma HepG2 cells and nasopharyngeal carcinoma CNE2 cells, with IC(50) values of 3.71 µM, 7.12 µM and 19.79 µM, respectively, after 24 hour treatment with nagaimo lectin. The induction of phosphatidylserine externalization and mitochondrial depolarization indicated that nagaimo lectin evoked apoptosis in MCF7 cells. However, the anti-proliferative activity of nagaimo lectin was not blocked by application of galactose, signifying that the activity was not related to the carbohydrate binding specificity of the lectin.
MeSH term(s)	Amino Acid Sequence ; Apoptosis/drug effects ; Breast Neoplasms/metabolism ; Breast Neoplasms/pathology ; Cell Line, Tumor ; Cell Proliferation/drug effects ; Chromatography, Ion Exchange ; Dioscorea/metabolism ; Electrophoresis, Polyacrylamide Gel ; Flow Cytometry ; Galactose/metabolism ; Hep G2 Cells ; Humans ; Hydrogen-Ion Concentration ; Inhibitory Concentration 50 ; MCF-7 Cells ; Molecular Weight ; Phosphatidylserines/metabolism ; Plant Lectins/chemistry ; Plant Lectins/metabolism ; Plant Lectins/pharmacology ; Plant Tubers/metabolism ; Plants, Edible/metabolism ; Protein Binding ; Protein Stability ; Sequence Analysis, Protein ; Temperature
Chemical Substances	Phosphatidylserines ; Plant Lectins ; Galactose (X2RN3Q8DNE)
Language	English
Publishing date	2013-01-21
Publishing country	United States
Document type	Journal Article
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0054212
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Article ; Online: White kidney bean lectin exerts anti-proliferative and apoptotic effects on cancer cells.

Chan, Yau Sang / Xia, Lixin / Ng, Tzi Bun

International journal of biological macromolecules

2016 Volume 85, Page(s) 335–345

Abstract: A 60-kDa glucosamine binding lectin, white kidney bean lectin (WKBL), was purified from Phaseolus vulgaris cv. white kidney beans, by application of anion exchange chromatography on Q-Sepharose, affinity chromatography on Affi-gel blue gel, and FPLC-size ...

Abstract	A 60-kDa glucosamine binding lectin, white kidney bean lectin (WKBL), was purified from Phaseolus vulgaris cv. white kidney beans, by application of anion exchange chromatography on Q-Sepharose, affinity chromatography on Affi-gel blue gel, and FPLC-size exclusion on Superdex 75. The anti-proliferative activity of WKBL on HONE1 cells and HepG2 cells was stronger than the activity on MCF7 cells and WRL68 cells (IC50 values for a 48-h treatment with WKBL on HONE1 cells: 18.8 μM; HepG2 cells: 19.7 μM; MCF7 cells: 26.9 μM; and WRL68 cells: >80 μM). The activity could be reduced by addition of glucosamine, which occupies the binding sites of WKBL, indicating that carbohydrate binding is crucial for the activity. Annexin V-FITC and PI staining, JC-1 staining and Hoechst 33342 staining revealed that apoptosis was induced on WKBL-treated HONE1 cells and HepG2 cells, but not as obviously on MCF7 cells. Cell cycle analysis also showed a slight cell cycle arrest on HONE1 cells after WKBL treatment. Western blotting suggested that WKBL induced apoptosis of HONE1 cells occurred through the extrinsic apoptosis pathway, with detection of increased level of active caspase 3, 8 and 9.
MeSH term(s)	Antineoplastic Agents, Phytogenic/chemistry ; Antineoplastic Agents, Phytogenic/pharmacology ; Apoptosis/drug effects ; Caspases/metabolism ; Cell Line, Tumor ; Cell Proliferation/drug effects ; Flow Cytometry ; Glucosamine/chemistry ; Humans ; Hydrogen-Ion Concentration ; Phaseolus/chemistry ; Phytohemagglutinins/chemistry ; Plant Extracts/chemistry ; Plant Extracts/pharmacology ; Plant Lectins/chemistry ; Plant Lectins/pharmacology
Chemical Substances	Antineoplastic Agents, Phytogenic ; Phytohemagglutinins ; Plant Extracts ; Plant Lectins ; Caspases (EC 3.4.22.-) ; Glucosamine (N08U5BOQ1K)
Language	English
Publishing date	2016-04
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	282732-3
ISSN	1879-0003 ; 0141-8130
ISSN (online)	1879-0003
ISSN	0141-8130
DOI	10.1016/j.ijbiomac.2015.12.094
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Article: White kidney bean lectin exerts anti-proliferative and apoptotic effects on cancer cells

Chan, Yau Sang / Lixin Xia / Tzi Bun Ng

International journal of biological macromolecules. 2016 Apr., v. 85

2016

Abstract	A 60-kDa glucosamine binding lectin, white kidney bean lectin (WKBL), was purified from Phaseolus vulgaris cv. white kidney beans, by application of anion exchange chromatography on Q-Sepharose, affinity chromatography on Affi-gel blue gel, and FPLC-size exclusion on Superdex 75. The anti-proliferative activity of WKBL on HONE1 cells and HepG2 cells was stronger than the activity on MCF7 cells and WRL68 cells (IC50 values for a 48-h treatment with WKBL on HONE1 cells: 18.8Î¼M; HepG2 cells: 19.7Î¼M; MCF7 cells: 26.9Î¼M; and WRL68 cells: >80Î¼M). The activity could be reduced by addition of glucosamine, which occupies the binding sites of WKBL, indicating that carbohydrate binding is crucial for the activity. Annexin V-FITC and PI staining, JC-1 staining and Hoechst 33342 staining revealed that apoptosis was induced on WKBL-treated HONE1 cells and HepG2 cells, but not as obviously on MCF7 cells. Cell cycle analysis also showed a slight cell cycle arrest on HONE1 cells after WKBL treatment. Western blotting suggested that WKBL induced apoptosis of HONE1 cells occurred through the extrinsic apoptosis pathway, with detection of increased level of active caspase 3, 8 and 9.
Keywords	affinity chromatography ; anion exchange chromatography ; apoptosis ; binding sites ; carbohydrate binding ; caspase-3 ; cell cycle checkpoints ; gels ; glucosamine ; human cell lines ; inhibitory concentration 50 ; kidney beans ; lectins ; neoplasm cells ; neoplasms ; Phaseolus vulgaris ; staining ; Western blotting
Language	English
Dates of publication	2016-04
Size	p. 335-345.
Publishing place	Elsevier B.V.
Document type	Article
ZDB-ID	282732-3
ISSN	1879-0003 ; 0141-8130
ISSN (online)	1879-0003
ISSN	0141-8130
DOI	10.1016/j.ijbiomac.2015.12.094
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Article ; Online: SCD1/FADS2 fatty acid desaturases equipoise lipid metabolic activity and redox-driven ferroptosis in ascites-derived ovarian cancer cells.

Xuan, Yang / Wang, Huogang / Yung, Mingo Mh / Chen, Fushun / Chan, Wai-Sun / Chan, Yau-Sang / Tsui, Stephen Kw / Ngan, Hextan Ys / Chan, Karen Kl / Chan, David W

Theranostics

2022 Volume 12, Issue 7, Page(s) 3534–3552

Abstract: Rationale: ...

Abstract	Rationale:
MeSH term(s)	Animals ; Ascites ; Carcinoma, Ovarian Epithelial ; Cisplatin/pharmacology ; Delta-5 Fatty Acid Desaturase ; Fatty Acid Desaturases/genetics ; Fatty Acid Desaturases/metabolism ; Fatty Acids, Unsaturated ; Female ; Ferroptosis ; Humans ; Iron ; Mice ; Ovarian Neoplasms/drug therapy ; Oxidation-Reduction ; Peritoneal Neoplasms ; Stearoyl-CoA Desaturase/genetics ; Stearoyl-CoA Desaturase/metabolism ; Tumor Microenvironment
Chemical Substances	Delta-5 Fatty Acid Desaturase ; Fatty Acids, Unsaturated ; Iron (E1UOL152H7) ; Fatty Acid Desaturases (EC 1.14.19.-) ; SCD1 protein, human (EC 1.14.19.1) ; Scd1 protein, mouse (EC 1.14.19.1) ; Stearoyl-CoA Desaturase (EC 1.14.19.1) ; FADS2 protein, human (EC 1.14.19.3) ; Cisplatin (Q20Q21Q62J)
Language	English
Publishing date	2022-04-24
Publishing country	Australia
Document type	Journal Article
ZDB-ID	2592097-2
ISSN	1838-7640 ; 1838-7640
ISSN (online)	1838-7640
ISSN	1838-7640
DOI	10.7150/thno.70194
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Article: A Glucosamine-Specific Lectin from Green Dragon No. 8 Beans (Phaseolus vulgaris) Induced Apoptosis on Nasopharyngeal Carcinoma Cells.

Chan, Yau Sang / Xia, Lixin / Ng, Tzi Bun

Evidence-based complementary and alternative medicine : eCAM

2015 Volume 2015, Page(s) 760539

Abstract: A lectin exhibiting antiproliferative activity on tumor cell lines but devoid of antifungal activity has been purified from Phaseolus vulgaris cv. Green Dragon no. 8 seeds. The lectin was a 60 kDa dimeric protein with two 30 kDa subunits. It was a ... ...

Abstract	A lectin exhibiting antiproliferative activity on tumor cell lines but devoid of antifungal activity has been purified from Phaseolus vulgaris cv. Green Dragon no. 8 seeds. The lectin was a 60 kDa dimeric protein with two 30 kDa subunits. It was a glucosamine-specific lectin as implied from the inhibitory effect of glucosamine on hemagglutinating activity of the lectin. The steps for isolation of the lectin involved Affi-gel blue gel (affinity gel), Mono Q (anion exchanger), and Superdex 75 column (size exclusion). The lectin was purified 20.8-fold from the crude extract of the beans. The purified lectin showed antiproliferative activity on breast cancer MCF7 cell line and nasopharyngeal cancer HONE1 and CNE2 cell lines, but a low activity on normal skin fibroblast HSF98 cell line. The lectin was shown to induce apoptosis on HONE1 cells, as indicated by increased phosphatidylserine externalization and mitochondrial depolarization. It also blocked HONE1 cell division and kept the cells at the G2/M phase of the cell cycle.
Language	English
Publishing date	2015-07-28
Publishing country	United States
Document type	Journal Article
ZDB-ID	2171158-6
ISSN	1741-4288 ; 1741-427X
ISSN (online)	1741-4288
ISSN	1741-427X
DOI	10.1155/2015/760539
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Article: Bauhinia variegata var. variegata Lectin: Isolation, Characterization, and Comparison

Chan, Yau Sang / Ng, Tzi Bun

Applied biochemistry and biotechnology. 2015 Jan., v. 175, no. 1

2015

Abstract	Bauhinia variegata var. variegata seeds are rich in proteins. Previously, one of the major storage proteins of the seeds was found to be a trypsin inhibitor that possessed various biological activities. By using another purification protocol, a glucoside- and galactoside-binding lectin that demonstrated some differences from the previously reported B. variegata lectin could be isolated from the seeds. It involved affinity chromatography on Affi-gel blue gel, ion exchange chromatography on Q-Sepharose and Mono Q, and also size exclusion chromatography on Superdex 75. The lectin was not retained on Affi-gel blue gel but interacted with Q-Sepharose. The lectin was a 64-kDa protein with two 32-kDa subunits. It had low thermostability (stable up to 50 °C) and moderate pH stability (stable in pH 3–10). It exhibited anti-proliferative activity on nasopharyngeal carcinoma HONE1 cells with an IC₅₀of 12.8 μM after treatment for 48 h. It also slightly inhibited the growth of hepatoma HepG2 cells. The lectin may have potential in aiding cancer treatments.
Keywords	Bauhinia variegata ; affinity chromatography ; biotechnology ; carcinoma ; gel chromatography ; gels ; growth retardation ; hepatoma ; human cell lines ; ion exchange chromatography ; lectins ; pH ; seeds ; storage proteins ; thermal stability ; trypsin inhibitors
Language	English
Dates of publication	2015-01
Size	p. 75-84.
Publishing place	Springer-Verlag
Document type	Article
ZDB-ID	392344-7
ISSN	0273-2289
ISSN	0273-2289
DOI	10.1007/s12010-014-1261-z
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