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Plant Lectins: Targeting Programmed Cell Death Pathways As Antitumor Agents

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Plant Lectins: Targeting Programmed Cell Death Pathways As Antitumor Agents See discussions, stats, and author profiles for this publication at: http://www.researchgate.net/publication/51529797 Plant lectins: targeting programmed cell death pathways as antitumor agents. Int J Biochem Cell Biol ARTICLE in THE INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY · JULY 2011 Impact Factor: 4.05 · DOI: 10.1016/j.biocel.2011.07.004 · Source: PubMed CITATIONS READS 56 232 6 AUTHORS, INCLUDING: Chengcheng Zhou Shun Yao Sichuan University Shanghai Institutes for Biological Sciences 2 PUBLICATIONS 61 CITATIONS 6 PUBLICATIONS 82 CITATIONS SEE PROFILE SEE PROFILE Available from: Chengcheng Zhou Retrieved on: 26 November 2015 This article appeared in a journal published by Elsevier. The attached copy is furnished to the author for internal non-commercial research and education use, including for instruction at the authors institution and sharing with colleagues. Other uses, including reproduction and distribution, or selling or licensing copies, or posting to personal, institutional or third party websites are prohibited. In most cases authors are permitted to post their version of the article (e.g. in Word or Tex form) to their personal website or institutional repository. Authors requiring further information regarding Elsevier’s archiving and manuscript policies are encouraged to visit: http://www.elsevier.com/copyright Author's personal copy The International Journal of Biochemistry & Cell Biology 43 (2011) 1442–1449 Contents lists available at ScienceDirect The International Journal of Biochemistry & Cell Biology jo urnal homepage: www.elsevier.com/locate/biocel Review Plant lectins: Targeting programmed cell death pathways as antitumor agents 1 1 1 ∗ ∗ Lei-lei Fu , Cheng-cheng Zhou , Shun Yao , Jia-ying Yu, Bo Liu , Jin-ku Bao School of Life Sciences & State Key Laboratory of Biotherapy and Cancer Center, West China Hospital, West China Medical School, Sichuan University, Chengdu 610041, China a r t i c l e i n f o a b s t r a c t Article history: Lectins, a group of highly diverse, carbohydrate-binding proteins of non-immune origin that are ubiq- Received 7 June 2011 uitously distributed in plants, animals and fungi, are well-characterized to have numerous links a wide Received in revised form 11 July 2011 range of pathological processes, most notably cancer. In this review, we present a brief outline of the Accepted 12 July 2011 representative plant lectins including Ricin-B family, proteins with legume lectin domains and GNA fam- Available online 20 July 2011 ily that can induce cancer cell death via targeting programmed cell death pathways. Amongst these above-mentioned lectins, we demonstrate that mistletoe lectins (MLs), Ricin, Concanavalin A (ConA) and Keywords: Polygonatum cyrtonema lectin (PCL) can lead to cancer cell programmed death via targeting apoptotic Plant lectin Cancer pathways. In addition, we show that ConA and PCL can also result in cancer cell programmed death by targeting autophagic pathways. Moreover, we summarize the possible anti-cancer therapeutic implica- Programmed cell death (PCD) Apoptosis tions of plant lectins such as ConA, Phaseolus vulgaris lectin (PHA) and MLs that have been utilized at Autophagy different stages of preclinical and clinical trials. Together, these findings can provide a comprehensive perspective for further elucidating the roles of plant lectins that may target programmed cell death path- ways in cancer pathogenesis and therapeutics. And, this research may, in turn, ultimately help cancer biologists and clinicians to exploit lectins as potential novel antitumor drugs in the future. © 2011 Elsevier Ltd. All rights reserved. Contents 1. Introduction . 1443 2. Molecular mechanisms of Ricin-B family-induced apoptosis . 1443 2.1. Mistletoe lectins . 1443 2.2. Other Ricin-B family lectins . 1444 3. Molecular mechanisms of proteins with legume lectin domains-induced apoptosis or autophagy . 1445 3.1. Concanavalin A . 1445 3.2. Other proteins with legume lectin domains . 1445 4. Molecular mechanisms of Galanthus nivalis agglutinin (GNA) family-induced apoptosis and/or autophagy . 1446 4.1. Polygonatum cyrtonema lectin . 1446 4.2. Other GNA-related lectins . 1447 5. Possible therapeutic implications of plant lectins in cancer . 1447 6. Concluding remarks and future directions . 1448 Acknowledgments . 1448 References . 1448 Abbreviations: ABA, garicus bisporus agglutinin; Apaf-1, apoptosis-associated factor-1; APC, adenomatous polyposis coli; APO-1, apoptosis antigen-1; CM-I, Chinese mistletoe lectin-I; ConA, Concanavalin A; EEA, Euonymus europaeus agglutinin; ERK, extracellular signal-regulated kinase; FADD, Fas-associated protein with death domain; GNA, Galanthus nivalis agglutinin; JNK, c-Jun N-terminal kinase; KML, Korean mistletoe lectin; LNL, Liparis noversa lectin; LysM, lysin motif; MAPK, mitogen-activated protein kinase; MLs, mistletoe lectins; PCD, programmed cell death; MMP, mitochondrial membrane potential; NMR, nuclear magnetic resonance; OJL, Ophiopogon japonicus lectin; PCL, Polygonatum cyrtonema lectin; PHA, Phaseolus vulgaris lectin; PI3K, phosphatidylinositol 3 kinase; POL, Polygonatum odoratum lectin; RBA, rice bran agglutinin; RIPs II, type II ribosome-inactivating proteins; ROS, reactive oxygen species; SAPK, stress-activated protein kinase; SFL, Sophora flavescens lectin; TNF-␣, tumor necrosis factor-␣; TRAIL, TNF-related apoptosis inducing ligand; XIAP, X-linked inhibitor of apoptosis protein. ∗ Corresponding authors. Tel.: +86 28 85411914; fax: +86 28 85411914. E-mail addresses: [email protected] (B. Liu), [email protected] (J.-k. Bao). 1 These authors contributed equally to this work. 1357-2725/$ – see front matter © 2011 Elsevier Ltd. All rights reserved. doi:10.1016/j.biocel.2011.07.004 Author's personal copy L.-l. Fu et al. / The International Journal of Biochemistry & Cell Biology 43 (2011) 1442–1449 1443 1. Introduction mistletoes, which has received much attention for their anti- proliferative and apoptosis-inducing mechanisms in cancer cells Lectins, a group of highly diverse non-immune origin pro- (Seifert et al., 2008) (Fig. 2A). So far, MLs have been divided into teins ubiquitously distributed in plants, animals and fungi, contain three distinct types, namely, ML-I, ML-II and ML-III. They are het- at least one non-catalytic domain which enables them to selec- erodimeric glycoproteins that consist of an A-chain comprising tively recognize and reversibly bind to specific free sugars or three conserved individual domains and a B-chain containing two glycans present on glycoproteins and glycolipids without alter- domains with the similar configuration (Thies et al., 2005). In the ing the structure of carbohydrate (Van Damme et al., 1998). Plant three types of MLs, sugar-binding specificity of B-chain may play lectins are divided into 12 different families according to their an important role in determining selective cytotoxicity for cancer different carbohydrate-binding specificities, such as (1) Agaricus cells via interacting with certain sugar-chains or sugar-containing bisporus agglutinin homologs, (2) Amaranthins, (3) Class V chitinase receptors on the cell surface, while A-chain inhibits protein syn- homologs with lectin activity, (4) Cyanovirin family, (5) EEA fam- thesis intracellularly via interacting with 28S ribosome, indicating ily, (6) GNA family, (7) proteins with hevein domains, (8) Jacalins, that the cellular cytotoxicity of MLs may require both the A- and (9) proteins with legume lectin domains, (10) LysM domain, (11) B-chains (Hoessli and Ahmad, 2008). Recently, accumulating data Nictaba family (formerly Cucurbitaceae phloem lectins), (12) Ricin- have demonstrated that MLs (mainly referring to ML-I and ML-II) B family (Van Damme et al., 2008) (see in Table 1). Amongst possess anti-proliferative activities toward various types of can- the above-mentioned lectin families, Ricin-B family, proteins with cer cells (e.g., human acute lymphoblastic leukemia cells, human legume lectin domains and GNA family have been widely reported hepatocarcinoma cells, human A549 lung cancer cells and human to have a number of links to many pathological processes, such as myeloleukemic U937 cells) (Fulda and Debatin, 2006; Hoessli and cancer (Liu et al., 2010a). Ahmad, 2008). On one hand, some plant lectins were previously used as sim- Moreover, ML-I was shown to possess more sensitivity to apo- ␣ ple tumor recognition tools to differentiate malignant tumors from ptosis induction by TNF- , which further suggests the cooperation benign and the degree of glycosylation associated with metastasis between ML-I and TNF-family death receptors in determining can- (Mody et al., 1995). In the recent years, they have been developed cer cell death (Pryme et al., 2006; Hoessli and Ahmad, 2008). for utilization as sophisticated microarray for better recognizing In addition, ML-I was found to induce apoptosis by activating malignant tumors in diagnosis and prognosis of cancer (Gupta et al., caspase-8 via the extrinsic apoptotic pathway, but independent 2010). On the other hand, these lectins have been well-known to of death receptor pathway in Jurkat leukemic T cells (Bantel possess antitumor activities, via targeting programmed cell death et al., 1999). Interestingly, ML-I was shown to potentiate the (PCD), which is a cell-intrinsic mechanism for eliminating harm- effects of chemotherapeutic drugs such as etoposide, further ful cells and maintaining homeostasis, including apoptosis and supporting the possibility of ML-I utilized for cancer therapy autophagy
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