In vitro influence of lectins and neoglycoconjugates on the growth of three human sarcoma cell lines

Remmelink, Myriam; Darro, Francis; Decaestecker, Christine; Decker, Robert De; Bovin, Nicolai V.; Gebhart, Michaël; Kaltner, Herbert; Gabius, Hans‐Joachim; Kiss, Róbert; Salmon, Isabelle; Danguy, André

doi:10.1007/s004320050274

Cited by 18 publications

(9 citation statements)

References 38 publications

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“…In uterine leiomyosarcomas, galectin-1 levels were significantly low, consistent with earlier reports showing that galectin-1 staining was high in leiomyoma, but weak in leiomyosarcoma and myometrium [45]. Because treatment of human sarcoma cells, SK-UT-1 and SK-LMS-1 with galectin-1 inhibited cell proliferation [46], low levels of galectin-1 in uterine leiomyosarcoma may contribute to the tumor growth. Future studies of galectin-1 in uterine leiomyosarcoma would provide a better understanding of BDNF-TrkB signaling mediated-cell growth.…”

Section: Discussionsupporting

confidence: 89%

Inhibition of Uterine Sarcoma Cell Growth through Suppression of Endogenous Tyrosine Kinase B Signaling

et al. 2012

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Uterine leiomyosarcoma is an aggressive tumor typically found at advanced stages due to difficulties with early diagnosis. Because uterine leiomyosarcoma is resistant to conventional radiation and chemotherapy, the development of more potent medical therapeutics is anticipated. Using quantitative real-time RT-PCR and immunostaining, we found the expression of brain-derived neurotrophic factor (BDNF) and neurotropin-4/5, together with their receptor, tyrosine kinase B (TrkB), in different uterine sarcoma cell lines and primary tumor samples from uterine leiomyosarcoma patients. We noted that levels of BDNF were more abundant than those of neurotropin-4/5. Moreover, the expression of TrkB and its ligands was elevated in a multidrug-resistant cell line and samples obtained from patients with leiomyosarcoma. In cultured uterine sarcoma cells, inhibition of endogenous TrkB signaling by treatment with either the soluble TrkB ectodomain or the Trk receptor inhibitor, K252a, suppressed cell proliferation and increased apoptosis based on cell viability and proliferation, in situ terminal deoxynucleotidyl transferase-mediated 2′-deoxyuridine 5′-triphosphate nick end-labeling and caspase-3/7 assays, whereas an inactive plasma membrane nonpermeable K252b was ineffective. Correspondingly, treatment with exogenous BDNF increased cell proliferation. In in vivo studies in athymic nude mice bearing multidrug-resistant uterine sarcoma cell tumors, we demonstrate suppression of tumor growth by treatment with K252a, but not K252b, as reflected by decreased cell proliferation and increased levels of apoptosis and caspase-3/7 activities without obvious side effects. Our findings indicated that endogenous signaling of the TrkB pathway contributed to uterine sarcoma cell growth, and inhibition of TrkB signaling in these tumors could provide a novel medical therapy for patients with uterine sarcomas.

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Section: Discussionsupporting

confidence: 89%

Inhibition of Uterine Sarcoma Cell Growth through Suppression of Endogenous Tyrosine Kinase B Signaling

et al. 2012

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“…Besides, chemically modified form of Con A when administered to mice with melanoma, it augmented the anticancer ability of peripheral lymphocytes against tumor cells (Ueno et al, 2000). Similarly, PHA derived from raw kidney beans when incorporated in diet, inhibited the proliferation of murine non Hodgkin lymphoma tumor (Liu et al, 2010;Remmelink et al, 1999). On parallel lines, WGA treatment has shown to increase life expectancy of mice through modulation of host immune response (Liu et al, 2010).…”

Section: Use Of Lectins In Clinical Settingsmentioning

confidence: 98%

Structure-function and application of plant lectins in disease biology and immunity

Mishra

Behura

Mawatwal

et al. 2019

Food and Chemical Toxicology

142

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A B S T R A C TLectins are proteins with a high degree of stereospecificity to recognize various sugar structures and form reversible linkages upon interaction with glyco-conjugate complexes. These are abundantly found in plants, animals and many other species and are known to agglutinate various blood groups of erythrocytes. Further, due to the unique carbohydrate recognition property, lectins have been extensively used in many biological functions that make use of protein-carbohydrate recognition like detection, isolation and characterization of glycoconjugates, histochemistry of cells and tissues, tumor cell recognition and many more. In this review, we have summarized the immunomodulatory effects of plant lectins and their effects against diseases, including antimicrobial action. We found that many plant lectins mediate its microbicidal activity by triggering host immune responses that result in the release of several cytokines followed by activation of effector mechanism. Moreover, certain lectins also enhance the phagocytic activity of macrophages during microbial infections. Lectins along with heat killed microbes can act as vaccine to provide long term protection from deadly microbes. Hence, lectin based therapy can be used as a better substitute to fight microbial diseases efficiently in future.

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“…to figure out whether galectin-1 is a negative growth regulator mediated by its carbohydrate binding activity. Presented at the cell surface and acting via its carbohydrate binding capacity, galectin-1 (or its avian homologue CG-16) is mitogenic for murine Thy-1-negative spleen or lymph node cells, mammalian vascular and hu- man Hs729 cells, and SK-UT-1 osteosarcoma cells (52)(53)(54)(55)(56). In contrast, overexpression of galectin-1 during glucocorticoid-dependent induction of apoptosis in human T-cell CEM C7 leukemia cells and its carbohydrate-dependent proapoptotic activity on activated T-cells show that the responses to lectin binding are cell type-specific (57)(58)(59)(60).…”

Section: Discussionmentioning

confidence: 99%

Negative Regulation of Neuroblastoma Cell Growth by Carbohydrate-dependent Surface Binding of Galectin-1 and Functional Divergence from Galectin-3

Kopitz¹,

Reitzenstein²,

André³

et al. 2001

Journal of Biological Chemistry

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260

192

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The cell density-dependent growth inhibition of human SK-N-MC neuroblastoma cells is initiated by increased ganglioside sialidase activity leading to elevated cell surface presentation of ganglioside GM1, a ligand of galectin-1. We herein show that the extent of the cell surface expression of the galectin coincides with marked increases of the sialidase activity. Reverse transcriptase-polymerase chain reaction analysis excludes a regulation at the transcriptional level. Exposure of cells to purified galectin-1 reveals its carbohydrate-dependent activity to reduce cell proliferation. Assays to detect DNA fragmentation biochemically and cytometrically and to block caspases render it unlikely that galectin-1 acts as a classical proapoptotic factor on these cells. Because the chimeric galectin-3 shares binding sites and binding parameters with galectin-1 for these cells, we tested whether this galectin will elicit the same response as the homodimeric cross-linking galectin-1. Evidently, galectin-3 fails to affect cell growth by itself but interferes with galectin-1 upon coincubation. Its proteolytically truncated variant, the C-terminal lectin domain with impaired capacity to form aggregates when surface bound, has only weak binding properties. Thus, the way in which the galectin-1 interacts topologically with an apparently common set of ligands relative to galectin-3 is crucial for eliciting post-binding events. We conclude that galectin-1 is a probable effector in the sialidase-dependent growth control in this system. Moreover, the experiments with galectin-3 reveal functional divergence, most probably based on different topologies of presentation of homologous carbohydratebinding sites.

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In vitro influence of lectins and neoglycoconjugates on the growth of three human sarcoma cell lines

Cited by 18 publications

References 38 publications

Inhibition of Uterine Sarcoma Cell Growth through Suppression of Endogenous Tyrosine Kinase B Signaling

Inhibition of Uterine Sarcoma Cell Growth through Suppression of Endogenous Tyrosine Kinase B Signaling

Structure-function and application of plant lectins in disease biology and immunity

Negative Regulation of Neuroblastoma Cell Growth by Carbohydrate-dependent Surface Binding of Galectin-1 and Functional Divergence from Galectin-3

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