Viscaceae Lectins

Franz, Hartmut

doi:10.1007/978-3-662-11060-7_2

Cited by 16 publications

(4 citation statements)

References 25 publications

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“…Twenty eight cytokine genes were upregulated by VCA (including IL-1α, IL-1β, IL-6, IL-8, IFN-γ, and TNF-α), and five of the genes were upregulated more than 10-fold. The above observations are consistent with the previous studies (Frantz, 1989;Beuth et al, 1994;Riberéau-Gayon et al, 1996) which showed that low non-toxic concentrations of mistletoe lectin can stimulate animal or human macrophages/monocytes. Taken together, these data suggest that a specific network of chemokine genes is activated by VCA, and that this activation is accompanied by a similar activation of the cytokine network.…”

Section: Discussionsupporting

confidence: 93%

Effect of Korean Mistletoe Lectin on Gene Expression Profile in Human T Lymphocytes: A Microarray Study

Lyu¹,

Park

2010

Biomolecules and Therapeutics

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-Korean mistletoe has a variety of biological effects, such as immunoadjuvant activities. This study investigates the effects of Korean mistletoe lectin (Viscum album L. var. coloratum agglutinin, VCA) on human T lymphocytes to determine whether VCA acts as an immunomodulator. Purified human T-lymphocytes were cultured with VCA and RNA from each point was analyzed using Affymetrix human genome chips containing 22,500 probe sets which represents more than 18,000 transcripts derived from 14,500 human genes. As a result, there was a striking upregulation of genes coding for chemokines. Seventeen genes out of 50 coding for proteins with chemokine activity were upregulated including CXCL9 and IL-8 which are related to the treatment of cancer. In addition, 28 cytokine genes were upregulated including IL-1, IL-6, IL-8, IFN-γ, and TNF-α. Taken together, the data suggest that Korean mistletoe lectin, in parallel with European mistletoe, has an ability to modulate human T cell function.

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Section: Discussionsupporting

confidence: 93%

Effect of Korean Mistletoe Lectin on Gene Expression Profile in Human T Lymphocytes: A Microarray Study

Lyu¹,

Park

2010

Biomolecules and Therapeutics

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“…In a series of papers it has been demonstrated that the main lectin from European mistletoe (mistletoe lectin I, MLI) belongs to the so-called toxic lectins besides ricin, abrin, modeccin and PCL, the lectin from Phoradendron californicum (for review see [6,9]. These lectins all consist of an A and a B chain.…”

Section: Introductionmentioning

confidence: 98%

Induction of tumor necrosis factor expression by a lectin fromViscum album

Männel

Becker

Gundt

et al. 1991

Cancer Immunol Immunother

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A purified lectin (MLI) from Viscum album was used to test whether peripheral monocytes from human blood can be activated for the production of tumour necrosis factor (TNF). Cytotoxic activity was detected in the supernatant of MLI-stimulated monocyte cultures. This cytotoxic activity was completely inhibited by monoclonal antibodies to TNF alpha. Small amounts of soluble TNF protein were measured in a TNF alpha-specific enzyme-linked immunospecific assay system. Strong expression of TNF alpha mRNA was induced in human monocytes as well as in macrophage cultures from C3H/HeJ mice having a low response to endotoxin after 2 h of stimulation. Both chains of the MLI were found to induce TNF mRNA equally well in human monocytes. In macrophages of endotoxin-low-responder mice the toxic A chain was a better inducer of TNF mRNA than the galactose-specific lectin B chain. Thus, MLI has immunomodulating effects in activating monocytes/macrophages for inflammatory responses.

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“…Both chains are derived from a single precursor by the post-translational excision of a linker sequence between the (N-terminal) A-domain and the (C-terminal) B-domain and are held together by a disulphide bridge. Mistletoe lectin I (MLI) is a dimer of two [A-s-s-B] pairs and exhibits a preferential specificity towards galactose [4][5][6][7]. In contrast, lectin II (MLII) and lectin III (MLIII) are monomeric type 2 RIP exhibiting specificity towards galactose/N-acetylgalactosamine and N-acetylgalactosamine, respectively [1,2].…”

Section: Introductionmentioning

confidence: 99%

Isolation and partial characterization of a small chitin‐binding lectin from mistletoe (Viscum album)

et al. 1996

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In this report we present evidence that mistletoe contains besides the three above-mentioned type 2 RIP/lectins also a small agglutinin, which on the basis of its structure and specificity can be classified in the group of chitin-binding plant lectins composed of hevein domains [9]. The discovery of the novel agglutinin not only demonstrates that mistletoe contains two groups of totally different lectins, but also raises the question of whether this new lectin possibly contributes either positively or negatively to the therapeutic effects of mistletoe preparations. Since a similar chitin-binding lectin from the rhizomes of stinging nettle (Urtica dioica) is a potent superantigen in mice [10], the latter question is certainly relevant.

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Viscaceae Lectins

Cited by 16 publications

References 25 publications

Effect of Korean Mistletoe Lectin on Gene Expression Profile in Human T Lymphocytes: A Microarray Study

Effect of Korean Mistletoe Lectin on Gene Expression Profile in Human T Lymphocytes: A Microarray Study

Induction of tumor necrosis factor expression by a lectin fromViscum album

Isolation and partial characterization of a small chitin‐binding lectin from mistletoe (Viscum album)

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