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PubMed2006

Mistletoe alkali inhibits peroxidation in rat liver and kidney.

AIM: To explore the antioxidant and free radical scavenger properties of mistletoe alkali (MA). METHODS: The antioxidant effect of mistletoe alkali on the oxidative stress induced by carbon tetrachloride (CCl4) in rats was investigated. The rats were divided into four groups (n = 8): CCl4-treated group (1 mL/kg body weight), MA -treated group (90 mg/kg), CCl4+MA-treated group and normal control group. After 4 wk of treatment, the level of malondialdehyde (MDA), a lipid peroxidation product (LPO) was measured in serum and homogenates of liver and kidney. Also, the level of glutathione (GSH), and activities of glutathione reductase (GR), glutathione peroxidase (GSPx), superoxide dismutase (SOD), and glutathione-S-transferase (GST) in liver and kidney were determined. Scavenging effects on hydroxyl free radicals produced in vitro by Fenton reaction were studied by ESR methods using 5,5-dimethyl-1-pyrroline-N-oxide (DMPO) as a spin trap reagent and H2O2/UV as the OH. source. Urinary 8-hydroxydeoxyguanosine (8-OHdG) was determined by competitive ELISA. RESULTS: In CCl4-treated group, the level of LPO in serum of liver and kidney was significantly increased compared to controls. The levels of GSH and enzyme activities of SOD, GSPx and GR in liver and kidney were significantly decreased in comparison with controls. In CCl4+MA-treated group, the changes in the levels of LPO in serum of liver and kidney were not statistically significant compared to controls. The levels of SOD, GSPx and GR in liver and kidney were significantly increased in comparison with controls. There was a significant difference in urinary excretion of 8-OHdG between the CCl4-treated and MA-treated groups. CONCLUSION: Oxidative stress may be a major mechanism for the toxicity of CCl4. MA has a protective effect against CCl4 toxicity by inhibiting the oxidative damage and stimulating GST activities. Thus, clinical application of MA should be considered in cases with carbon tetrachloride-induced injury.

Animals↗
PubMedDate not supplied

Outbreak of caterpillar dermatitis caused by airborne hairs of the mistletoe browntail moth (Euproctis edwardsi).

Caterpillars may be an under-recognised cause of skin and eye reactions. We report a four-month outbreak of recurrent papulourticarial rash among staff and visitors at a community centre. Caterpillar of the mistletoe browntail moth The cause was eventually diagnosed as airborne hairs from (Euproctis edwardsi). caterpillars of the mistletoe browntail moth (Euproctis edwardsi), which infested a eucalypt tree growing in front of the centre. To our knowledge, this is the first clear case of airborne caterpillar hairs causing dermatitis in an indoor environment.

Adult↗
PubMedDate not supplied

Influence of postoperative complementary treatment with lectin-standardized mistletoe extract on breast cancer patients. A controlled epidemiological multicentric retrolective cohort study.

This epidemiological study was performed to evaluate the influence of postoperative complementary treatment with lectin-standardized mistletoe extract (sME) on breast cancer patients. The design (retrolective cohort analysis with parallel groups) and conduct of the study were in agreement with current standards for prospectively randomized clinical trials. A cohort of 1,248 breast cancer patients on postoperative chemo-, radio-, hormone-therapy were studied in 27 randomized centers. Patients with complementary medications other than sME were excluded from the evaluation and the final analysis was performed on data of 689 patients. From this cohort 219 patients received a complementary treatment exclusively with sME (therapy group), while 470 patients were without complementary treatment (control group). The median follow-up time was 284 days (therapy group) and 285 days (control group). The primary end-point of the study was to determine the impact of complementary sME treatment on disease- or therapy-induced adverse reactions in breast cancer patients. Imbalances for causal effects (covariates) were adjusted by propensity scores. Final evaluation was performed by estimating the linear regression between change in symptom score and propensity score with all data and using the regression line to calculate the change in symptom score expected for each patient. Tumor-associated events were evaluated by number and time until event. The safety of sME treatment was analysed in terms of number, severity, duration and outcome of adverse reactions. As compared to breast cancer patients without complementary treatment (control group), the administration of sME (therapy group) resulted in a significant reduction of adverse reactions induced by the tumor-destructive therapies (e.g. nausea, gastro-intestinal tract symptoms, depression, fatigue, mental symptoms) and prolonged relapse-free intervals, most pronounced for UICC stages IIa and IIb. The rate of sME-associated adverse reactions was 12.8%. All side-effects were mild to moderate, predominantly local skin reactions and self-limiting without therapeutic intervention. Complementary treatment of breast cancer patients with lectin-standardized mistletoe extract (sME) proved to be a well tolerated optimization of standard tumor-destructive therapies, mainly improving quality of life and relapse-free intervals in defined UICC stages.

Adult↗
PubMedDate not supplied

Influence of treatment with the immunomodulatory effective dose of the beta-galactoside-specific lectin from mistletoe on tumor colonization in BALB/c-mice for two experimental model systems.

Mistletoe extracts have approval for clinical application. This warrants the quest for the definition of the active substances to optimize their application. Thus, the extent of immunomodulating and antimetastatic activity of the beta-galactoside-specific lectin from mistletoe extract (ML I) was investigated. In BALB/c-mice regular subcutaneous (s.c.) injections of small nontoxic doses of ML I yielded significant enhancement of peritoneal macrophage activity, as measured in chemiluminescence assays, as well as significant weight gain of thymus. Spleen weight, however, increased without statistical significance. To evaluate the anti-metastatic activity of ML I we intravenously (i.v.) inoculated sarcoma L-1 and fibrosarcoma RAW 117-H 10 cells which cause tumor colonization of lungs and livers in BALB/c-mice, respectively. After regular s.c. administration of ML I, the number of lung and liver tumor colonies significantly decreased in both experimental tumor models as compared to control mice which received injections of saline solution. Accordingly, ML I can be regarded as a potent immunomodulating and antimetastatic substance, which seems to be promising for clinical trials in human oncology.

Adjuvants, Immunologic↗
PubMed1990

[In vitro studies of the effect of a mistletoe preparation on melanoma cells].

In concentrations usually achieved in vivo, extracts of mistletoe (e.g. Iscador) exert no direct action on melanoma cells or human fibroblasts in tissue cultures. Only very high concentrations of Iscador in combination with prolonged incubation time (over several days) resulted in damaging the cells irreversibly. Therefore we are not able to confirm the suggestion that mistletoe extracts exert a deleterious action selectively on malignant cells.

Adult↗
PubMed1993

[Comparative studies on the immunoactive action of galactoside-specific mistletoe lectin. Pure substance compared to the standardized extract].

Comparative Studies on the Immunoactive Potency of Galactoside-specific Lectin from Mistletoe/Pure substance against standardized extract. Cellular and humoral aspects of the immunomodulating activity of the galactoside-specific lectin from mistletoe (ML-1) were investigated in cancer patients suffering from mammary carcinoma and compared to the immunoactive potency of a proprietary mistletoe extract standardized for ML-1 (ML-1 stand., Eurixor). Regular subcutaneous injections of the optimal dose of ML-1 and ML-1 stand. (1 ng/kg body weight; twice a week; for 4 weeks) yielded statistically significant increases of certain lymphocyte subsets (helper T-lymphocytes, natural killer (NK)-cells) which are generally believed to be involved in antitumor activity. Moreover, administration of either ML-1 preparation resulted in enhanced expression of interleukin (Il)-2 receptors on lymphatic cells and significantly increased serum levels of defined acute phase reactants (c-reactive protein, haptoglobin, C3 complement) as indicator of cellular and humoral activity. In vitro, exposition of human lymphocytes to ML-1 and ML-1 stand. resulted in enhanced expression of Il-2 receptors, which substantiated the capacity of both ML-1 preparations to affect immunological parameters within the host defense system. The effects of ML-1 and ML-1 stand. were comparable.

Acute-Phase Proteins↗
PubMed1995

[Immunoactive effects of various mistletoe lectin-1 dosages in mammary carcinoma patients].

Cellular aspects of the immunomodulating activity of a proprietary mistletoe extract (Eurixor) standardized for mistletoe lectin-1 (ML-1) were investigated in patients suffering from mammary carcinoma (n = 20). Regular subcutaneous injections of the different dosages (0.5 and 1.0 ng ML-1/kg body weight, twice a week, for 5 weeks) yielded statistically significant increases of defined peripheral blood lymphocyte subsets (helper T-cells, natural killer (NK)-cells) which are generally believed to be involved in antitumor activity. Moreover, administration of either ML-1 concentration resulted in enhanced expression of activation markers such as interleukin-2 receptors and HLA/DR-antigens on peripheral blood T-lymphocytes. This study suggests that regular subcutaneous administration of both ML-1 concentrations (0.5 and 1.0 ng/kg body weight) can efficiently stimulate the cellular immune system of cancer patients.

Adjuvants, Immunologic↗
PubMed1994

[Immunoactive action of mistletoe lectin-1 in relation to dose].

Galactoside-specific mistletoe lectin-1 (ML-1) was isolated by affinity chromatography from proprietary mistletoe extract and checked in BALB/c-mice for its immunoactive potency. To investigate the optimal immunomodulating dosage, ML-1 (0.5, 1.0, 2.5, 5.0 ng/kg body weight, b.w.) was subcutaneously administered for three subsequent days followed by another injection 48 h later. These studies proved that injections of 1 ng ML-1/kg b.w. induced optimal immunomodulation, since thymocyte proliferation, maturation and emigration were significantly enhanced in this murine model as compared to non-treated control mice. Further on, counts of peripheral blood lymphocytes and monocytes as well as expression of relevant activation markers on these cells revealed significant increases after ML-1 (1 ng/kg b.w.) administration. However, increase of cell counts and activity of peritoneal macrophages were less pronounced but still statistically significant for this ML-1 concentration. Determination of immune responses after low dose ML-1 treatment (0.5 ng/kg b.w.) presented relevant (partly statistically significant) increases, too. However, high dose ML-1 treatment (2.5, 5.0 ng/kg b.w.) did not enhance (but suppress) relevant immune functions. For future clinical/therapeutical treatment strategies, ML-1 dosages ranging from 0.5-1.0 ng/kg b.w. may be supposed to be optimal.

Adjuvants, Immunologic↗
PubMedDate not supplied

Efficiency of treatment with galactoside-specific lectin from mistletoe against rat glioma.

The cytotoxic activity of the galactoside-specific lectin from mistletoe (mistletoe lectin-1, ML-1) towards the anaplastic glioma cell line (F98) was investigated in vitro (three dimensional spheroid model) and in vivo (Fischer 344 rats). Both model systems demonstrated the dose dependent cytotoxicity of ML-1. F98 glioma cell spheroid growth was significantly inhibited after incubation with defined ML-1 concentrations of 10 and 100 ng/mL. To investigate the in vivo efficacy Fischer 344 rats were intracerebrally implanted with F98 glioma cells and assigned to local and systemic ML-1 treatment, respectively. Histological and immunohistochemical evaluations proved a reduction of tumor volume for both treatment modalities, most pronounced and statistically significant after systemic (immunomodulating) administration of the optimal ML-1 dosage (1 ng/kg BW, subcutaneously) and after low dose (10 ng ML-1 per application (10 microL) local treatment. High dose ML-1 administration (10 ng/kg BW; systemically; 100 ng/application, locally) was less effective than low (optimal) dose treatment and apparently the systemic/immunomodulating approach gained greater benefit for glioma bearing rats.

Animals↗
PubMed2003

Antiviral potency of mistletoe (Viscum album ssp. album) extracts against human parainfluenza virus type 2 in Vero cells.

Various extracts from the leaves of mistletoe (Viscum album L. ssp. album) were investigated for their antiviral activity on human parainfluenza virus type 2 (HPIV-2) growth in Vero cells. Plant extracts were prepared using distilled water, 50% ethanol, petroleum ether, chloroform and acetone. The 50% effective dose (ED(50)) of aqueous extract for HPIV-2 replication was 0.53 +/- 0.12 micro g/mL, and the antiviral index (AI), which was based on the ratio of the 50% inhibitory concentration (CD(50)) for host cell viability to the ED(50) for parainfluenza virus replication, was 10.05. The aqueous extract was found to be the most selective inhibitor. Furthermore, the aqueous extract at a concentration of 1 micro g/mL was found to inhibit HPIV-2 replication and the virus production was suppressed to more than 99% without any toxic effect on host cells. The chloroform extract was also found to be moderately active. In an effort to further analyse the mechanism of antiviral activity, the effectiveness of the aqueous extract on different steps of virus replication was examined. The antiviral activity could neither be attributed to the direct inactivation of the HPIV-2 nor to the inhibition of adsorption to Vero cells. The active aqueous extract has shown a dose-dependent antiviral activity on virus replication.

Animals↗
PubMed2001

Primary structure, isoforms, and molecular modeling of a chitin-binding mistletoe lectin.

From mistletoe Viscum album L. extracts three chitin-binding lectin isoforms, cbML1, cbML2, and cbML3, were isolated and their primary structure determined. All three cbML isoforms are composed of two protein chains of 48 or 49 amino acid residues, linked by an intermolecular disulfide bond. The sequence of each single cbML chain is characterized by a relatively high number of cysteine and glycine residues, 9 and 6, respectively, and contains four intramolecular disulfide bridges. On the basis of the combined interpretation of sequencing and MALDI MS data, the following results for the three cbML isoforms were obtained: the first one consists of two identical truncated polypeptide chains (1--48), the second is a heterodimer, containing one truncated (1--48) and one full-length chain (1--49), and the third is composed of two full length chains (1--49). The cbML sequence shows 55% identity to hevein, a single-chain chitin-binding protein of 43 amino acids, one of the most predominant proteins in natural rubber latex. On the basis of the NMR data on hevein from Hevea brasiliensis the three-dimensional structure of cbML3 was modelled. The 26 sequence changes between cbML3 and hevein were accommodated with only little perturbation in the main chain folding. A comparison of the primary structures of cbML3 and hevein is shown and the effects of the sequence changes are discussed. Differences have been identified in the loop region of the molecule and the potential interface region of cbML3 supporting the dimer formation. The high-affinity chitin-binding site seems to be highly conserved.

Amino Acid Sequence↗
PubMed1995

Interaction of mistletoe toxic lectin-I with sialoglycoproteins.

The binding properties of mistletoe toxic lectin-I (ML-I) with sialo-N- and O-glycans were investigated by quantitative precipitin and precipitin inhibition assays. Human alpha 1-acid glycoprotein reacted strongly with ML-I, precipitating over 82% of the lectin nitrogen tested, while the precipitability of its asialo product decreased by 30%. Native fetuin precipitated 50% of the ML-I added, and its reactivity was reduced by 20% after desialylation. On the contrary, the poor reactivity of rat sublingual sialoglycoprotein with ML-I increased substantially after removal of sialic acid and completely precipitated the lectin added. The glycoprotein-lectin interactions were inhibited by NeuAc alpha 2-->3/alpha 2-->6Gal beta 1-->4Glc and/or Gal beta 1-->4Glc (NAc) residues. From the above results, it is concluded that ML-I is specific for sialic acid. However, sialic acid of some O-glycans also acts as masking molecule as the precipitability of rat sublingual and bovine submandibular glycoproteins with ML-I increased after desialylation.

Animals↗
PubMed1998

Complete amino acid sequence of the B chain of mistletoe lectin I.

The primary structure of the B chain of mistletoe lectin I, the component of a commercially available extract from Viscum album exhibiting immunomodulatory capacity, was established based on amino acid sequence analysis of the protein and peptides derived from its enzymatic digestion. It is composed of 264 residues, including seven cysteine residues and three N-linked carbohydrate chains. The amino acid sequence of MLB shows a high homology with those from other structurally related galactoside-specific lectins such as ricin and abrin with 169 and 146 identities, respectively. These results are of crucial importance in order to understand the biological activity of ML-1.

Abrin↗
PubMed1998

Primary structure and molecular modeling of mistletoe lectin I from Viscum album.

The first three-dimensional structure of the ribosome inactivating protein mistletoe lectin I (ML-I) from Viscum album has been modeled on the basis of the X-ray structure of castor bean ricin from Ricinus communis. The relative high sequence homology and conserved secondary structure enabled accurate modeling. The 196 sequence changes between ML-I and ricin could be accomodated with only little pertubation in the main chain folding. A close comparison of the primary structures of ML-I and ricin is given and the effects of the sequence changes are elucidated on the basis of the modeled three-dimensional structure. Differences have been identified in the vicinity of the active site, in the high affinity galactose binding site and in the interface between the A and B chains, which might account for the reduced cytotoxicity of ML-I.

Amino Acid Sequence↗
PubMed1999

Crystal structure of mistletoe lectin I from Viscum album.

The crystal structure of the ribosome-inactivating protein (RIP) mistletoe lectin I (ML-I) from Viscum album has been solved by molecular replacement techniques. The structure has been refined to a crystallographic R-factor of 24.5% using X-ray diffraction data to 2.8 A resolution. The heterodimeric 63-kDa protein consists of a toxic A subunit which exhibits RNA-glycosidase activity and a galactose-specific lectin B subunit. The overall protein fold is similar to that of ricin from Ricinus communis; however, unlike ricin, ML-I is already medically applied as a component of a commercially available misteltoe extract with immunostimulating potency and for the treatment of human cancer. The three-dimensional structure reported here revealed structural details of this pharmaceutically important protein. The comparison to the structure of ricin gives more insights into the functional mechanism of this protein, provides structural details for further protein engineering studies, and may lead to the development of more effective therapeutic RIPs.

Abrin↗
PubMed1999

Site-specific mutagenesis of mistletoe lectin: the role of RIP activity in apoptosis.

Recombinant mistletoe lectin (rML) belongs to the class of type II ribosome-inactivating proteins (RIP) composed of a catalytically active A-chain with rRNA N-glycosidase activity and a B-chain with carbohydrate binding properties. To investigate the contribution of the enzymatic activity of the rML A-chain to the observed cytotoxic and apoptotic effects, an rMLA E166Q R169Q molecule was developed by means of site-specific mutagenesis. Following heterologous expression, the activity of mutant rMLA was measured in a cell-free assay for rRNA-N-glycosidase activity. Moreover, after generation of heterodimer, the activities of mutant rML E166Q R169Q and rML wild type were determined in a cytotoxicity and apoptosis assay. Although the reduction of activity as measured in the cell-free RIP assay was more pronounced (factor 237) than in both cellular assays (factors 20-22), the data clearly indicate a close correlation between cytotoxicity, apoptosis, and the enzymatic activity of the rML A-chain. Thus, RIP activity is an essential feature of rML and therefore a prerequisite for its biological function as an anticancer agent.

Apoptosis↗
PubMed1993

Crystallization of the ribosome inactivating protein ML1 from Viscum album (mistletoe) complexed with beta-D-galactose.

A ribosome inactivating protein (ML1) from the mistletoe plant (Viscum album) has been crystallized. The crystals, grown in the presence of beta-D-galactose, are hexagonal, space group P6(1)22 or P6(5)22, a = b = 111.0 A, c = 309.3 A with 24 molecules per unit cell (assuming 33% solvent by weight). The protein of molecular mass 63 kDa is a heterodimer consisting of two chains, A and B, joined by a disulfide bond. The A-chain, 29 kDa, inhibits protein synthesis by depurinating an adenine residue (A4324) in a highly conserved RNA loop of the 28 S ribosomal subunit. The toxicity of the protein is mediated by the B-chain, 34 kDa, which has lectin activity, interacting with sugar residues of glycoproteins and glycolipids on the surface of target cells.

Crystallography, X-Ray↗