Lectins as possible tools for improved urinary bladder cancer management

Višnjar, Tanja; Romih, Rok; Zupančič, Daša

doi:10.1093/glycob/cwz001

Cited by 15 publications

(17 citation statements)

References 103 publications

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“… 19 Major sugar residues of the UPs are high mannose glycans, fucosylated complex glycans and N-linked complex glycans capped by sialic acid. 25 In normal urothelium specific glycoproteins like E-selectin, mucins 1, 2, 4, 6 and 7 and galectins are also expressed. 25 ACA and jacalin predominantly bind to galactosyl(β-1,3) N -acetilgalactosamine (Thomsen-Friedenreich antigen, Tn) and its sialylated form (sTn).…”

Section: Discussionmentioning

confidence: 99%

“… 25 In normal urothelium specific glycoproteins like E-selectin, mucins 1, 2, 4, 6 and 7 and galectins are also expressed. 25 ACA and jacalin predominantly bind to galactosyl(β-1,3) N -acetilgalactosamine (Thomsen-Friedenreich antigen, Tn) and its sialylated form (sTn). Although Tn and sTn are thought to not be present in the normal urothelium, 31 in our study ACA and jacalin labelled apical PM of umbrella cells.…”

Section: Discussionmentioning

confidence: 99%

“…The immunohistochemistry (IHC) is sometimes additionally done for detection of keratins, while lectin histochemistry (LHC) is not accepted as a diagnostic tool, despite several studies demonstrated that it could improve diagnosis of bladder cancer. [22][23][24][25] Correlation between protein and sugar residues expression and localization would offer additional information about carcinoma subtypes.…”

Section: Introductionmentioning

confidence: 99%

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Combined lectin- and immuno-histochemistry (CLIH) for applications in cell biology and cancer diagnosis: Analysis of human urothelial carcinomas

et al. 2020

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Lectin histochemistry (LHC) and immunohistochemistry (IHC), which demonstrate the composition and localisation of sugar residues and proteins in cell membranes, respectively, are generally used separately. Using these two methods, we previously demonstrated that malignant transformation of urothelial cells results in the alterations of protein glycosylation and reduced expression of urothelium-specific integral membrane proteins uroplakins (UPs). However, the correlation between these changes was not studied yet. To evaluate this correlation, we developed innovative method, which we named combined lectin- and immuno- histochemistry (CLIH). We used human biopsies of 6 normal urothelia and 9 papillary urothelial carcinomas, i.e. 3 papillary urothelial neoplasms of low malignant potential (PUNLMP), 3 non-invasive papillary urothelial carcinomas of low grade (pTa, l.g.), and 3 invasive papillary urothelial carcinomas of high grade (pT1, h.g.). We tested five different protocols (numbered 1-5) of CLIH on paraffin and cryo-semithin sections and compared them with LHC and IHC performed separately. Additionally, we carried out western and lectin blotting with antibodies against UPs and lectins Amaranthus caudatus agglutinin (ACA), Datura stramonium agglutinin (DSA), and jacalin, respectively. We showed that incubation with primary antibodies first, followed by the mixture of secondary antibodies and lectins is the most efficient CLIH method (protocol number 5). Additionally, 300 nm thick cryo-semithin sections enabled better resolution of co-localisation between sugar residues and proteins than 5 µm thick paraffin sections. In the normal urothelium, CLIH showed co-localisation of lectins ACA and jacalin with UPs in the apical plasma membrane (PM) of superficial umbrella cells. In papillary urothelial carcinomas, all three lectins (ACA, DSA and jacalin) labelled regions of apical PM, where they occasionally co-localised with UPs. Western and lectin blotting confirmed the differences between normal urothelium and papillary urothelial carcinomas. Our results show that CLIH, when used with various sets of lectins and antigens, is a useful, quick, and reliable method that could be applied for basic cell biology research as well as detailed subtyping of human urothelial carcinomas.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Combined lectin- and immuno-histochemistry (CLIH) for applications in cell biology and cancer diagnosis: Analysis of human urothelial carcinomas

et al. 2020

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“…On cancer cell lines, they exhibit antiproliferative properties [20,22], promote apoptosis and autophagy, and block angiogenesis [20,22]. Moreover, their ability to bind to carbohydrates could make them useful for the detection of subtle modifications of carbohydrate composition, which appears during cancer transformation [23]. However, although anticancer activity of terrestrial lectins has been summarized in several reviews [20,24,25], to our knowledge no comprehensive report highlighting uniquely the antineoplastic activity of marine lectins has been written.…”

Section: Introductionmentioning

confidence: 99%

Antitumor Potential of Marine and Freshwater Lectins

et al. 2019

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Often, even the most effective antineoplastic drugs currently used in clinic do not efficiently allow complete healing due to the related toxicity. The reason for the toxicity lies in the lack of selectivity for cancer cells of the vast majority of anticancer agents. Thus, the need for new potent anticancer compounds characterized by a better toxicological profile is compelling. Lectins belong to a particular class of non-immunogenic glycoproteins and have the characteristics to selectively bind specific sugar sequences on the surface of cells. This property is exploited to exclusively bind cancer cells and exert antitumor activity through the induction of different forms of regulated cell death and the inhibition of cancer cell proliferation. Thanks to the extraordinary biodiversity, marine environments represent a unique source of active natural compounds with anticancer potential. Several marine and freshwater organisms, ranging from the simplest alga to the most complex vertebrate, are amazingly enriched in these proteins. Remarkably, all studies gathered in this review show the impressive anticancer effect of each studied marine lectin combined with irrelevant toxicity in vitro and in vivo and pave the way to design clinical trials to assess the real antineoplastic potential of these promising proteins. It provides a concise and precise description of the experimental results, their interpretation as well as the experimental conclusions that can be drawn.

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“…It arises from the urothelial cell lining. [ 1 ] The main risk factor for BC is tobacco smoking. [ 2 ] At the time of diagnosis, approximately 75% of these have non-MIBC, with the remaining 25% having MIBCor metastatic disease.…”

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confidence: 99%