<i>Vicia faba</i> agglutinin, the lectin present in broad beans, stimulates differentiation of undifferentiated colon cancer cells

Jordinson, M; El‐Hariry, Iman; Calnan, Denis P.; Calam, J.; Pignatelli, Massimo

doi:10.1136/gut.44.5.709

Cited by 59 publications

(33 citation statements)

References 31 publications

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“…A large number of studies with PNA indicate that this lectin acts in a cell type specific manner, often promoting proliferation and sometimes producing a toxic effect (Lee 1988;Caldero et al, 1989;McGarrity et al, 1991;Boland et al, 1992;Ryder et al, 1992;Chen et al, 1994;Kiss et al, 1997;Lorea et al, 1997;Jordinson et al, 1998;Yu et al, 2001;Singh et al, 2001;2006;Ohba et al, 2003;Cai et al, 2005). Valentiner et al (2003) in a model study showed that different lectins exerted different effects at specific concentrations on different breast cancer cell lines.…”

Section: Discussionmentioning

confidence: 99%

“…In the study reported here, we examine two lectins that are reported to be largely non-toxic to cells -Dolichos biflorus agglutinin (DBA) and Arachis hypogaea /peanut agglutinin (PNA) (Ryder et al, 1992;Chen et al, 1994;Camby et al, 1997;Kiss et al, 1997;Jordinson et al, 1998;Ohba et al, 2003;Valentiner et al, 2003;Singh et al, 2006) -using a human colon cancer (CCL-220) and a human non-cancer colon CRL-1459) cell line, as in our previous studies (Khurrum et al, 2002;Heinrich et al, 2005;Welty et al, 2006). We did not want to use toxic lectins that kill cells quickly.…”

Section: Introductionmentioning

confidence: 99%

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Lectin binding and effects in culture on human cancer and non-cancer cell lines: Examination of issues of interest in drug design strategies

2007

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SummaryBy using a non-cancer and a cancer cell line originally from the same tissue (colon), coupled with testing lectins for cell binding and for their effects on these cell lines in culture, this study decribes a simple multiparameter approach that has revealed some interesting results that could be useful in drug development strategies.Two human cell lines, CCL-220/Colo320DM (human colon cancer cells, tumorigenic in nude mice) and CRL-1459/CCD-18Co (non-malignant human colon cells) were tested for their ability to bind to agarose microbeads derivatized with two lectins, peanut agglutinin (Arachis hypogaea agglutinin, PNA) and Dolichos biflorus agglutinin (DBA), and the effects of these lectins were assessed in culture using the MTT assay.Both cell lines bound to DBA-derivatized microbeads, and binding was inhibited by N-acetyl-Dgalactosamine, but not by L-fucose. Neither cell line bound to PNA-derivatized microbeads. Despite the lack of lectin binding using the rapid microbead method, PNA was mitogenic in culture at some time points and its mitogenic effect displayed a reverse-dose response. This was also seen with effects of DBA on cells in culture.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Lectin binding and effects in culture on human cancer and non-cancer cell lines: Examination of issues of interest in drug design strategies

2007

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“…Overexpression of Ep-CAM is linked to differentiation and cell proliferation (Jordinson et al, 1999), although the molecular mechanism is still poorly understood. In vitro, its overexpression has been shown to be directly linked to stimulation of the cell cycle and proliferation by upregulating c-myc and cyclin A/E .…”

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confidence: 99%

Frequent high-level expression of the immunotherapeutic target Ep-CAM in colon, stomach, prostate and lung cancers

et al. 2006

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Epithelial cell adhesion molecule (Ep-CAM; CD326) is used as a target by many immunotherapeutic approaches, but little data are available about Ep-CAM expression in major human malignancies with respect to level, frequency, tumour stage, grade, histologic tumour type and impact on survival. We analysed by immunohistochemical staining tissue microarrays with 4046 primary human carcinoma samples from colon, stomach, prostate and lung cancers for both frequency and intensity of Ep-CAM expression under highly standardised conditions. A total of 3360 samples were analysable. High-level Ep-CAM expression was observed in 97.7% (n ¼ 1186) of colon, 90.7% of gastric (n ¼ 473), and 87.2% of prostate cancers (n ¼ 414), and in 63.9% of lung cancers (n ¼ 1287). No detectable Ep-CAM staining was found with only 0.4% of colon, 2.5% of gastric, 1.9% of prostate cancers, and 13.5% of lung cancers. The only significant correlation of Ep-CAM expression with tumour grading was observed in colon cancer where high-level Ep-CAM expression on grade 3 tumours was down to 92.1% (Po0.0001). Adenosquamous and squamous carcinomas of the lung had a lower percentage of high-level Ep-CAM expression compared to adenocarcinomas with 35.4 and 53.6%, respectively, and with 45.5 and 17.3% of tumours being Ep-CAM negative. With the exception of moderately differentiated colon carcinoma, where patients not expressing Ep-CAM on their tumours showed an inferior survival (P ¼ 0.0014), correlation of Ep-CAM expression with survival did not reach statistical significance for any of the other cancer indications and subgroups. In conclusion, the data strongly support the notion that Ep-CAM is a prime target for immunotherapies in major human malignancies. This is because the most common human cancers show (i) a low frequency of Ep-CAM-negative tumours, (ii) a high frequency of Ep-CAM expression on cells of a given tumour, and (iii) for most cancers, an insignificant influence of tumour staging, grading and histology on Ep-CAM expression.

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“…~ ~sm for _ti 'w~__ altermior~ is not yet unde~oocl, it was suggested that might he responsible for the ch~n~ obr~nced on the e~/dln:)cyte surface. In case of GanGer breast cases there may be increase in galactose epitopes as Studies ~ated with cell membrane changes and lec0n agglutination stmu~d that binding sites differ in different stages (10). In our study although cases at different stages were present, stage wise analysis was not carried out.…”

Section: Results and Di~u8810nmentioning

confidence: 68%

Differential erythrocyte agglutination pattern in normal and cancer patients with Synadenium grantii root (Hook f) lectin

Durgawale

Shukla

Sontakke

et al. 2001

Indian J Clin Biochem

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In the present study the property of lecUn agglutination in blood on normal and different canGer patients has been observed. The purified SynadenlumgranUimot I~'tin was non blood group specific and its utility as s diagnostic tool in mlignancy was studied. Hemagglutinstion (units/ml) of red blood ceils of different types of cancer was compared with the normal control's red blood cells. Out of 113 totil cancer patients, only a group of 29 breast cancer patients showed significant increase in ;;t,-e value (P<0.06) compared to normal control.

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Vicia faba agglutinin, the lectin present in broad beans, stimulates differentiation of undifferentiated colon cancer cells

Abstract: (Gut 1999;44:709-714)

Cited by 59 publications

References 31 publications

Lectin binding and effects in culture on human cancer and non-cancer cell lines: Examination of issues of interest in drug design strategies

Lectin binding and effects in culture on human cancer and non-cancer cell lines: Examination of issues of interest in drug design strategies

Frequent high-level expression of the immunotherapeutic target Ep-CAM in colon, stomach, prostate and lung cancers

Differential erythrocyte agglutination pattern in normal and cancer patients with Synadenium grantii root (Hook f) lectin

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