The clinical utility of Lens culinaris agglutinin-reactive thyroglobulin ratio in serum for distinguishing benign from malignant conditions of the thyroid

Shimizu, Kayoko; Nakamura, Kenji; Kobatake, Shinzo; Satomura, Shinji; Maruyama, Mina; Kameko, Fumiko; Tajiri, Junichi; Kato, Ryoji

doi:10.1016/j.cca.2006.12.017

Cited by 18 publications

(8 citation statements)

References 25 publications

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“…In addition, several other assays have been developed to distinguish Tg produced by malignant and benign thyroid tissues, but they have not been applied for routine use (12). Until more reliable methods become available, we recommend that every laboratory should monitor TgAb interference of the used Tg method.…”

Section: Discussionmentioning

confidence: 99%

Serum thyroglobulin antibody levels within or near to the reference range may interfere with thyroglobulin measurement

et al. 2012

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High concentration of thyroglobulin antibodies (TgAb) is a major limiting factor of thyroglobulin measurements in patients with differentiated thyroid cancer. We investigated whether thyroglobulin antibody added to serum samples could interfere with the thyroglobulin assay. Thyroglobulin levels in serum samples with different concentrations of thyroglobulin were measured by electrochemiluminescence immunoassay before and after the addition of increasing concentrations of thyroglobulin antibody using the secondary calibrator solution of the thyroglobulin assay kit containing sheep thyroglobulin antibody to reach thyroglobulin antibody levels within or near to the reference range. Thyroglobulin and thyroglobulin antibody concentrations were also measured in 134 serum samples from 27 patients after thyroid ablation. There was a strong negative association (slope = -1.179) between thyroglobulin antibody and thyroglobulin concentrations in samples with added thyroglobulin antibody (beta = -0.86; P < 0.001). Changes in thyroglobulin concentrations were described mathematically as loss of thyroglobulin% = -0.2408 x Ln(thyroglobulin antibody IU/ml) + 0.1944. Thyroglobulin concentrations were significantly lower than those calculated from experiments with added thyroglobulin antibody in 26/134 samples from patients after thyroid ablation. We conclude that if the same TgAb interference exists in the presence of naturally occurring human TgAb, our observation may prove to be useful during follow-up of patients with differentiated thyroid cancer. However, further studies are needed to explore the clinical relevance of thyroglobulin antibody levels within or near to the reference range in monitoring these patients.

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Section: Discussionmentioning

confidence: 99%

Serum thyroglobulin antibody levels within or near to the reference range may interfere with thyroglobulin measurement

et al. 2012

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“…Structure elucidation of Tg glycosylation in cancer has not been performed to date but may be useful for thyroid cancer diagnostics. Preliminary studies showed that the interaction of lectin LCA with Tg from thyroid carcinoma was significantly lower than that in normal thyroid tissue and in patients with benign thyroid tumor [ 111 , 112 ]. The percentage of LCA-reactive Tg could discriminate between benign and malignant lesions [ 113 ].…”

Section: Clinically Approved Biomarkersmentioning

confidence: 99%

“…The percentage of LCA-reactive Tg could discriminate between benign and malignant lesions [ 113 ]. It was also found that the percentage of LCA-reactive Tg was significantly decreased in thyroid carcinoma patients who were positive for lymph node metastasis compared to thyroid carcinoma patients who were negative for lymph node metastasis [ 112 ].…”

Section: Clinically Approved Biomarkersmentioning

confidence: 99%

Glycosylation-Based Serum Biomarkers for Cancer Diagnostics and Prognostics

Kirwan

Utratna

O’Dwyer

et al. 2015

BioMed Research International

180

143

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Cancer is the second most common cause of death in developed countries with approximately 14 million newly diagnosed individuals and over 6 million cancer-related deaths in 2012. Many cancers are discovered at a more advanced stage but better survival rates are correlated with earlier detection. Current clinically approved cancer biomarkers are most effective when applied to patients with widespread cancer. Single biomarkers with satisfactory sensitivity and specificity have not been identified for the most common cancers and some biomarkers are ineffective for the detection of early stage cancers. Thus, novel biomarkers with better diagnostic and prognostic performance are required. Aberrant protein glycosylation is well known hallmark of cancer and represents a promising source of potential biomarkers. Glycoproteins enter circulation from tissues or blood cells through active secretion or leakage and patient serum is an attractive option as a source for biomarkers from a clinical and diagnostic perspective. A plethora of technical approaches have been developed to address the challenges of glycosylation structure detection and determination. This review summarises currently utilised glycoprotein biomarkers and novel glycosylation-based biomarkers from the serum glycoproteome under investigation as cancer diagnostics and for monitoring and prognostics and includes details of recent high throughput and other emerging glycoanalytical techniques.

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“…During malignant transformation, epithelial cells modulate the glycosylation profile of their secretion proteins and these post-translational changes may represent specific markers which may be useful diagnostic or prognostic tools. The composition of carbohydrate chains on thyroglobulin from thyroid carcinoma has been reported to differ from that in normal thyroid tissue (Maruyama et al, 1998;Shimizu et al, 2007a). Shimizu et al (2007b) investigated Lens culinaris agglutinin (LCA)-reactive thyroglobulin ratio in serum to evaluate its usefulness for distinguishing between thyroid carcinoma and benign thyroid tumor.…”

Section: Thyroglobulinmentioning

confidence: 99%

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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The clinical utility of Lens culinaris agglutinin-reactive thyroglobulin ratio in serum for distinguishing benign from malignant conditions of the thyroid

Cited by 18 publications

References 25 publications

Serum thyroglobulin antibody levels within or near to the reference range may interfere with thyroglobulin measurement

Serum thyroglobulin antibody levels within or near to the reference range may interfere with thyroglobulin measurement

Glycosylation-Based Serum Biomarkers for Cancer Diagnostics and Prognostics

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

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