Evaluation of a new method for the diagnosis of alterations of Lens culinaris agglutinin binding of thyroglobulin molecules in thyroid carcinoma

Kanai, Toshiharu; Amakawa, Masao; Kato, Ryoji; Shimizu, Kayoko; Nakamura, Kenji; Ito, Kenichi; Hama, Yoshihisa; Fujimori, Minoru; Amano, Jun

doi:10.1515/cclm.2009.277

Cited by 13 publications

(4 citation statements)

References 21 publications

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“…Moreover, in cases of thyroid carcinoma with lymph node metastasis, Lens culinaris agglutinin-reactive Tg ratios were significantly decreased compared to patients with thyroid carcinoma without metastasis. Further studies confirm usefulness of the determination of LCA-reactive Tg ratios using an enzyme-linked immunosorbent assay for distinguishing between benign and malignant lesions (Kanai et al, 2009).…”

Section: Thyroglobulinmentioning

confidence: 53%

Glycosylation and Glycoproteins in Thyroid Cancer: A Potential Role for Diagnostics

Krześlak¹,

Jóźwiak²,

Lipińska³

2012

Updates in the Understanding and Management of Thyroid Cancer

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Glycosylation is the most common and the most diverse form of co-and post-translational modifications. An analysis of the Swiss-PROT database has led to the estimation that more than 50% of all proteins are glycosylated. Genes coding proteins involved in all types of oligosaccharides biosynthesis represent 0.5 to 1% of the translated genome (Dennis et al., 1999). Glycoproteins are found ubiquitously in an organism either as soluble (intracellular or extracellular) or as membrane bound molecules. There is a great structural variety of glycoproteins based on the type, length and linkage of a carbohydrate components as well as the degree of saturation of potential glycosylation sites on the protein itself. Carbohydrates can have a significant influence on the physicochemical properties of glycoproteins, affecting their folding, solubility, aggregation and degradation. Furthermore, glycan chains in glycoproteins play key roles in many biological processes such as embryonic development, immune response and cell-cell interactions in which sugar-sugar or sugar-protein specific recognition is involved (Wei & Li , 2009). Altered glycosylation is an universal feature of cancer cells, and certain glycan structures and glycoproteins are well-known tumor markers. These include for example glycoproteins such as carcinoembryonic antigen (CEA), commonly used as a marker of colorectal cancer, prostate-specific antigen (PSA) and CA-125 used in the diagnosis of ovarian cancer (Drake et al., 2010). High expression of some glycosyl epitopes for example sialyl Lewis a, sialyl Lewis x, Lewis y, promotes invasion and metastasis. Antibodies against Lewis antigens are used for evaluation of specimens from breast, bladder, colorectal, esophageal and lung carcinomas (Drake et al., 2010). Glycans can regulate different aspects of tumor progression, including proliferation, invasion and metastasis. Cancer-related changes in glycosylation can reflect disease specific alterations in glycan biosynthetic pathways. These include variations in the expression and activity of glycosyltransferases, enzymes that add monosaccharides to acceptors, i.e. proteins or growing carbohydrate chains and glycosidases which catalyze the hydrolysis of the glycosidic linkage to release sugars. There are three most common categories of protein glycosylation 1) N-glycosylation, where glycans are attached to asparagine residues in a consensus sequence N-X-S/T via N-acetylglucosamine (GlcNAc) residue; 2) O-glycosylation, where glycans are attached to serine or threonine via N-acetylgalactosamine (GalNAc) residue (mucin type glycosylation);

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Section: Thyroglobulinmentioning

confidence: 53%

Glycosylation and Glycoproteins in Thyroid Cancer: A Potential Role for Diagnostics

Krześlak¹,

Jóźwiak²,

Lipińska³

2012

Updates in the Understanding and Management of Thyroid Cancer

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“…Kanai et al [ 132 ] similarly analyzed the ratios of LCA-reactive Tg to total Tg from the sera of healthy individuals and patients with thyroid cancers utilizing an enzyme-linked immunofluorescence assay (ELISA) for the detection of Tg, which has a much higher sensitivity for the detection of Tg at low serum concentrations. This study demonstrated a reduction in the LCA-reactive-to-total-Tg ratio in patients with thyroid malignancies compared to healthy controls, regardless of total Tg serum concentration.…”

Section: Glycosylationmentioning

confidence: 99%

Posttranslational Modifications in Thyroid Cancer: Implications for Pathogenesis, Diagnosis, Classification, and Treatment

Broekhuis

James

Cummings

et al. 2022

Cancers

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There is evidence that posttranslational modifications, including phosphorylation, acetylation, methylation, ubiquitination, sumoylation, glycosylation, and succinylation, may be involved in thyroid cancer. We review recent reports supporting a role of posttranslational modifications in the tumorigenesis of thyroid cancer, sensitivity to radioiodine and other types of treatment, the identification of molecular treatment targets, and the development of molecular markers that may become useful as diagnostic tools. An increased understanding of posttranslational modifications may be an important supplement to the determination of alterations in gene expression that has gained increasing prominence in recent years.

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“…Furthermore, the fucosylated α fetoprotein-L3 (AFTL3) isoform shows higher specificity in HCC diagnosis in comparison with total AFT and worsens prognosis [48]. The lectin LCA also interacts with serum thyroglobulin (Tg), a biomarker of thyroid cancer, distinguishing between noncancerous and malignant diseases [49]. Moreover, LCA and Aleuria aurantia lectin (AAL) bind to fucosylated prostate-specific antigen (PSA), a commonly employed early diagnostic marker of prostate cancer [50,51].…”

Section: Lectins As Potential Diagnostic Toolsmentioning

confidence: 99%

Plant-Derived Lectins as Potential Cancer Therapeutics and Diagnostic Tools

Mazalovska

Kouokam

2020

BioMed Research International

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Cancer remains a global health challenge, with high morbidity and mortality, despite the recent advances in diagnosis and treatment. Multiple compounds assessed as novel potential anticancer drugs derive from natural sources, including microorganisms, plants, and animals. Lectins, a group of highly diverse proteins of nonimmune origin with carbohydrate-binding abilities, have been detected in virtually all kingdoms of life. These proteins can interact with free and/or cell surface oligosaccharides and might differentially bind cancer cells, since malignant transformation is tightly associated with altered cell surface glycans. Therefore, lectins could represent a valuable tool for cancer diagnosis and be developed as anticancer therapeutics. Indeed, several plant lectins exert cytotoxic effects mainly by inducing apoptotic and autophagic pathways in malignant cells. This review summarizes the current knowledge regarding the basis for the use of lectins in cancer diagnosis and therapy, providing a few examples of plant-derived carbohydrate-binding proteins with demonstrated antitumor effects.

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Evaluation of a new method for the diagnosis of alterations of Lens culinaris agglutinin binding of thyroglobulin molecules in thyroid carcinoma

Cited by 13 publications

References 21 publications

Glycosylation and Glycoproteins in Thyroid Cancer: A Potential Role for Diagnostics

Glycosylation and Glycoproteins in Thyroid Cancer: A Potential Role for Diagnostics

Posttranslational Modifications in Thyroid Cancer: Implications for Pathogenesis, Diagnosis, Classification, and Treatment

Plant-Derived Lectins as Potential Cancer Therapeutics and Diagnostic Tools

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