About: Clematis montana lectin, a novel mannose-binding lectin from traditional Chinese medicine with antiviral and apoptosis-inducing activities

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About: Clematis montana lectin, a novel mannose-binding lectin from traditional Chinese medicine with antiviral and apoptosis-inducing activities Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Clematis montana lectin, a novel mannose-binding lectin from traditional Chinese medicine with antiviral and apoptosis-inducing activities
Creator	Wang, Ying Lv, Hui Meng, Liang Peng, Hao Bao, Jin-Ku Li, Chun-Yang Liu, Yan-Hong
Source	Elsevier; Medline; PMC
abstract	Abstract A novel mannose-binding lectin (designated CML) was isolated from Clematis montana Buch.-Ham stem (Ranunculaceae) using ion exchange and gel filtration chromatographies on DEAE-Sepharose and Sephacryl S-100. The purified C. montana lectin was a homodimer of 11,968.9Da subunits as determined by gel filtration and MS. The hemagglutinating activity of CML was inhibited by branched oligomannosides. The N-terminal 15-amino acid sequence of CML, DNVKYSGQVKNTGSA, has not been reported for other lectins. Also, the peptide mass fingerprinting assay confirmed that there is no match result of similar plant lectins for CML, indicating CML may be a novel plant lectin. CML showed marked antiviral activity against various viruses in cell culture. Subsequently, CML was also found to exhibit remarkable inhibitory effect on L929, HeLa, MCF7 and HepG2 cells. Furthermore, CML specially induced L929 cell apoptosis in dose-dependent manner as evidenced by MTT, fluorescent microscopy, LDH activity-based cytotoxicity assays and DNA ladder. Moreover, due to both caspase inhibitors and Western blot analyses, caspase was also found to play the important role in the potential apoptotic mechanism of CML. When the carbohydrate-binding site was fully inhibited by sugars, cytotoxicity was abruptly decreased and apoptotic phenomenon in L929 cells was not observed, suggesting a significant correlation between mannose-binding-specific activity and the antineoplastic mechanism.
has issue date	2009-10-31(xsd:dateTime)
bibo:doi	10.1016/j.peptides.2009.06.027
bibo:pmid	19577602
has license	els-covid
sha1sum (hex)	3178ce8195f3f42963e3bf058ef3932ee9743cb9
schema:url	https://doi.org/10.1016/j.peptides.2009.06.027
resource representing a document's title	Clematis montana lectin, a novel mannose-binding lectin from traditional Chinese medicine with antiviral and apoptosis-inducing activities
has PubMed Central identifier	PMC7115534
has PubMed identifier	19577602
schema:publication	Peptides
resource representing a document's body	covid:3178ce8195f3f42963e3bf058ef3932ee9743cb9#body_text
is schema:about of	named entity 'MANNOSE-BINDING LECTIN' named entity 'hemagglutinating' named entity 'dose-dependent' named entity 'CML' named entity 'viruses' named entity 'match' named entity 'BINDING SITE' named entity 'DOSE-DEPENDENT' named entity 'MANNOSE-BINDING LECTIN' named entity 'CASPASE INHIBITORS' named entity 'ISOLATED' named entity 'CYTOTOXICITY ASSAYS' named entity 'CORRELATION' named entity 'PURIFIED' named entity 'VIRUSES' named entity 'LECTIN' named entity 'INDICATING' named entity 'NOVEL' named entity 'HAM' named entity 'PHENOMENON' named entity 'DUE TO' named entity 'DNA LADDER' named entity 'INDUCED' named entity 'FULLY' named entity 'FOUND' named entity 'WAS A' named entity 'DECREASED' named entity 'MS.' named entity 'APOPTOTIC' named entity 'MANNOSE' named entity 'CLEMATIS MONTANA' named entity 'LECTIN' named entity 'APOPTOSIS' named entity 'IMPORTANT' named entity 'ANTIVIRAL' named entity 'ACTIVITIES' named entity 'TRADITIONAL CHINESE MEDICINE' named entity 'APOPTOSIS' named entity 'L929 CELLS' named entity 'FLUORESCENT MICROSCOPY' named entity 'PEPTIDE MASS FINGERPRINTING ASSAY' named entity 'CHROMATOGRAPHIES' named entity 'CASPASE' named entity 'NOVEL' named entity 'SUGARS' named entity 'MECHANISM' named entity 'RESULT' named entity 'GEL FILTRATION' named entity 'AMINO ACID SEQUENCE' named entity 'NOT OBSERVED' named entity 'DEAE' named entity 'ION EXCHANGE' named entity 'ANTINEOPLASTIC' named entity 'SIGNIFICANT' named entity 'OLIGOMANNOSIDES' named entity 'CLEMATIS MONTANA' named entity 'HEPG2' named entity 'CML' named entity 'CYTOTOXICITY' named entity 'EXHIBIT' named entity 'CELLS' named entity 'PLANT LECTINS' named entity 'SPECIFIC ACTIVITY' named entity 'MTT' named entity 'HELA' named entity 'BASED' named entity 'S-100' named entity 'HOMODIMER' named entity 'L929' named entity 'INDUCING' named entity 'STEM' named entity 'POTENTIAL' named entity 'DETERMINED BY' named entity 'CONFIRMED' named entity 'BINDING'

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