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1.
Chinese Journal of Cancer ; (12): 325-334, 2015.
Article in English | WPRIM | ID: wpr-349588

ABSTRACT

Ribosome-inactivating proteins (RIPs) belong to a family of enzymes that attack eukaryotic ribosomes and potently inhibit cellular protein synthesis. RIPs possess several biomedical properties, including anti-viral and anti-tumor activities. Multiple RIPs are known to inhibit tumor cell proliferation through inducing apoptosis in a variety of cancers, such as breast cancer, leukemia/lymphoma, and hepatoma. This review focuses on the anti-tumor activities of RIPs and their apoptotic effects through three closely related pathways: mitochondrial, death receptor, and endoplasmic reticulum pathways.


Subject(s)
Animals , Humans , Antineoplastic Agents , Apoptosis , Endoplasmic Reticulum , Mitochondria , Plant Proteins , Receptors, Death Domain , Ribosome Inactivating Proteins , Ribosomes
2.
Journal of Biomedical Engineering ; (6): 1181-1184, 2011.
Article in Chinese | WPRIM | ID: wpr-274930

ABSTRACT

Three BALB/c mice were immunized four times with alpha-momorcharins (alpha-MMC). Using polyethylene glycol (PEG) method, the immunized splenocytes were fused with SP2/0 cells. One strain of hybridoma cells was obtained which secrete antibodies against alpha-MMC. To get ascites, the hybridoma cells were injected into the abdominal cavity of mice. The antibodies were purified from ascites. Indirect enzyme linked immunosorbent assay (ELISA) and Western blot assay were applied to determine the specifity of the monoclonal antibody (McAb). The results showed that the McAb was specific to alpha-MMC without detectable cross-activity with MAP30. The McAb provided detecting method for further research of the structure and function of alpha-MMC.


Subject(s)
Animals , Female , Mice , Antibodies, Monoclonal , Allergy and Immunology , Blotting, Western , Enzyme-Linked Immunosorbent Assay , Hybridomas , Metabolism , Mice, Inbred BALB C , Ribosome Inactivating Proteins , Allergy and Immunology
3.
Journal of Central South University(Medical Sciences) ; (12): 584-589, 2010.
Article in Chinese | WPRIM | ID: wpr-814414

ABSTRACT

OBJECTIVE@#To detect the expression of galectin-3 (gal-3) and Sambucus nigra agglutinin (SNA) and determine their clinicopathological significance in breast cancers and benign breast lesions.@*METHODS@#Envison immunohistochemistry for staining gal-3 expression, and ABC affinity-cytochemistry to detect SNA expression were used in paraffin-embedded slides from specimens of breast cancers (n=60) and benign lesions (n=30).@*RESULTS@#The positive rates and scoring means of gal-3 and SNA were significantly higher in breast cancer (48.3%, 2.07 +/- 2.25, 2.12 +/- 2.26) than those in benign lesions (26.7%, 1.03 +/- 1.63, 1.07 +/- 1.59, P < 0.05). The scoring means of gal-3 and SNA expression were significantly lower in the positive cases of estrogen receptor (ER) and the negative ones of CA15-3 than those in the negative cases and the positive ones (P < 0.05).The survival analysis of Kaplan-Meier showed the 5-year survival rate and mean survival period were significantly lower in the gal-3 or SNA expression positive cases than those in the negative cases of breast cancer (P<0.01).@*CONCLUSION@#The expressive level of gal-3 and SNA lectins might have important effect on the carcinogenesis, progression and biologic behaviors of breast cancer. The positive cases of gal-3 and /or SNA expression might have poor prognosis.


Subject(s)
Adolescent , Adult , Aged , Female , Humans , Middle Aged , Young Adult , Breast Neoplasms , Metabolism , Pathology , Fibrocystic Breast Disease , Metabolism , Pathology , Galectin 3 , Genetics , Metabolism , Mucin-1 , Metabolism , Plant Lectins , Genetics , Metabolism , Prognosis , Receptors, Estrogen , Metabolism , Ribosome Inactivating Proteins , Genetics , Metabolism
4.
Chinese Journal of Gastrointestinal Surgery ; (12): 297-300, 2009.
Article in Chinese | WPRIM | ID: wpr-326509

ABSTRACT

<p><b>OBJECTIVE</b>To study the expressive levels of galectin-3(gal-3) and Sambucus nigra agglutinin(SNA) and their clinicopathological significance in the benign and malignant lesions of stomach.</p><p><b>METHODS</b>EnVision immunohistochemistry for assaying gal-3 expressive level and ABC cytochemistry for determining SNA expressive level were used in conventional paraffin-embedded sections from specimens of gastric cancer(n=49), peritumoral tissues(n=20), metastatic foci of lymph nodes(n=36), and different types of benign lesions(n=80).</p><p><b>RESULTS</b>The positive rates of gal-3 and SNA were significantly higher in gastric cancer tissues than those in peritumoral tissues and different types of benign lesions(P<0.05, P<0.01). The positive cases of gal-3 and/or SNA in peritumoral tissues and benign lesions showed mild- to severe-atypical hyperplasia of mucous epithelial cells. No difference was found between the primary foci and metastatic foci in gal-3 and SNA expressions(P>0.05). The positive rates of gal-3 and SNA were significantly lower in histologic grade II(, infiltrating depth T1,T2 and no-metastasis of regional lymph node than those in histologic grade III(,IIII(, infiltrating depth T3,T4 and metastasis of lymph node in gastric cancer(P<0.05). The positive rates of gal-3 and SNA were higher in lymphnode metastatic site N1 and no-metastasis of distant organs than those in lymphnode metastatic site N2,N3 and metastasis of distant organs, but no significant difference was found(P>0.05). The consistency was found between the expression of gal-3 and SNA in gastric cancer tissues(chi(2)=6.59,P<0.05).</p><p><b>CONCLUSIONS</b>The expressive levels of gal-3 and SNA may be important molecular markers of lectins for reflecting the carcinogenesis, progression and biological behaviors in gastric cancer.</p>


Subject(s)
Adult , Aged , Female , Humans , Male , Middle Aged , Adenoma , Pathology , Galectin 3 , Metabolism , Gastritis , Pathology , Immunohistochemistry , Lymphatic Metastasis , Neoplasm Staging , Plant Lectins , Metabolism , Polyps , Pathology , Ribosome Inactivating Proteins , Metabolism , Stomach Neoplasms , Metabolism , Pathology
5.
J Biosci ; 2008 Mar; 33(1): 91-101
Article in English | IMSEAR | ID: sea-111306

ABSTRACT

A full-length cDNA encoding ribosome-inactivating/antiviral protein (RIP/AVP)from the leaves of Bougainvillea x buttiana was isolated.The cDNA consisted of 1364 nucleotides with an open reading frame (ORF)of 960 nucleotides encoding a 35.49 kDa protein of 319 amino acids.The deduced amino acid sequence has a putative active domain conserved in RIPs/AVPs and shows a varying phylogenetic relationship to the RIPs from other plant species.The deduced protein has been designated BBAP1 (Bougainvillea x buttiana antiviral protein1).The ORF was cloned into an expression vector and expressed in E.coli as a fusion protein of approximately 78 kDa.The cleaved and purified recombinant BBAP1 exhibited ribosome-inhibiting rRNA N-glycosidase activity,and imparted a high level of resistance against the tobacco mosaic virus (TMV).


Subject(s)
Amino Acid Sequence , Antiviral Agents/chemistry , Base Sequence , Cloning, Molecular , DNA, Complementary/genetics , Escherichia coli/genetics , Gene Expression , Genes, Plant , Glycoside Hydrolases/analysis , Molecular Sequence Data , Nyctaginaceae/anatomy & histology , Open Reading Frames , Phylogeny , Plant Leaves/chemistry , Plant Proteins/chemistry , Protein Sorting Signals , Protein Structure, Tertiary , Protein Synthesis Inhibitors/chemistry , Recombinant Fusion Proteins/analysis , Ribosome Inactivating Proteins/chemistry , Tobacco Mosaic Virus/physiology
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