Sialic acid expression in autoimmune thyroiditis

Janega, Pavol; Černá, Andrea; Kholová, Ivana; Brabencová, Eva; Babál, Pavel

doi:10.1078/0065-1281-00676

Cited by 15 publications

(4 citation statements)

References 8 publications

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“…Lectin histochemical staining of SA in tissue specimens of four human thyroid carcinomas showed that cancer transformation of thyroid follicular epithelial cells to PTC and FTC is associated with an increase of sialylation [ 105 , 106 ]. Changes in sialylation in thyroid diseases involve the Tg molecule.…”

Section: Glycosylation In Thyroid Pathologymentioning

confidence: 99%

Glycosylation in the Thyroid Gland: Vital Aspects of Glycoprotein Function in Thyrocyte Physiology and Thyroid Disorders

Ząbczyńska

Kozłowska

Pocheć

2018

IJMS

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The key proteins responsible for hormone synthesis in the thyroid are glycosylated. Oligosaccharides strongly affect the function of glycosylated proteins. Both thyroid-stimulating hormone (TSH) secreted by the pituitary gland and TSH receptors on the surface of thyrocytes contain N-glycans, which are crucial to their proper activity. Thyroglobulin (Tg), the protein backbone for synthesis of thyroid hormones, is a heavily N-glycosylated protein, containing 20 putative N-glycosylated sites. N-oligosaccharides play a role in Tg transport into the follicular lumen, where thyroid hormones are produced, and into thyrocytes, where hyposialylated Tg is degraded. N-glycans of the cell membrane transporters sodium/iodide symporter and pendrin are necessary for iodide transport. Some changes in glycosylation result in abnormal activity of the thyroid and alteration of the metabolic clearance rate of hormones. Alteration of glycan structures is a pathological process related to the progression of chronic diseases such as thyroid cancers and autoimmunity. Thyroid carcinogenesis is accompanied by changes in sialylation and fucosylation, β1,6-branching of glycans, the content and structure of poly-LacNAc chains, as well as O-GlcNAcylation, while in thyroid autoimmunity the main processes affected are sialylation and fucosylation. The glycobiology of the thyroid gland is an intensively studied field of research, providing new data helpful in understanding the role of the sugar component in thyroid protein biology and disorders.

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Section: Glycosylation In Thyroid Pathologymentioning

confidence: 99%

Glycosylation in the Thyroid Gland: Vital Aspects of Glycoprotein Function in Thyrocyte Physiology and Thyroid Disorders

Ząbczyńska

Kozłowska

Pocheć

2018

IJMS

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“…The level of different types of serum glycoproteins are maintained within a narrow range in health [10], but is elevated in many pathological conditions viz. tuberculosis [11], autoimmune disease [12], cardiovascular disease [13,14], diabetes mellitus [15], cancer of cervix [16], uterus [17] and breasts [18], and arthritis [19]. Thus, it is of great interest to identify and validate serum glycoproteins whose change in levels may provide new insight into cancer progression and may have utility as potential markers for cancer diagnosis.…”

Section: Introductionmentioning

confidence: 99%

Serum Levels of Glycoproteins are Elevated in Patients with Ovarian Cancer

et al. 2013

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Identification of reliable biomarkers for detection and staging of cancer and monitoring the outcome of anticancer therapy has been considered to be of high importance. We aimed to estimate the levels of serum glycoproteins, protein bound-hexose, protein bound hexosamine, protein bound fucose, protein bound sialic acid and protein bound carbohydrate in 32 ovarian cancer patients and compared them with the levels that found in 25 normal subjects. As compared to the normal subjects, all the four fractions of glycoproteins level were significantly elevated in ovarian cancer patients (p \ 0.05). Chemotherapy in these patients significantly decreased the levels of serum glycoproteins (p \ 0.05). Thus, high levels of serum glycoproteins in ovarian cancer patients could be due to abnormal protein glycosylation indicating malignant transformation of the cells.

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“…The glycosylation of Tg is necessary for the proper functioning and immunoreactivity of Tg [ 43 , 44 ]. Moreover, the neoplastic transformation of thyroid follicular cells to PTC and follicular thyroid carcinoma (FTC) is associated with an increase in sialylation [ 19 , 45 , 46 ]. Glycosylation is also the main processes affected in thyroid autoimmunity [ 19 ] and could represent the “trait d’union” to understand the processes leading to coexistence of serum TgAb, lymphocytic infiltrates, and PLNF in non-neoplastic thyroid gland, as evidenced in our study.…”

Section: Discussionmentioning

confidence: 99%

Serum Anti-Thyroglobulin Autoantibodies Are Specific in Predicting the Presence of Papillary-like Nuclear Features and Lymphocytic Infiltrate in the Thyroid Gland

et al. 2023

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(1) Background: Previous studies have reported a correlation between serum anti-Thyroglobulin-antibodies (TgAb) and papillary thyroid carcinoma. The aim of our study was to evaluate whether serum TgAb and anti-thyroid-peroxidase antibody (TPO) positivity was also related to pre-neoplastic histological changes such as papillary-like nuclear features (PLNF) and with the presence of lymphocytic infiltrate (LI) in thyroid surgical specimens. (2) Methods: The study was retrospectively carried out on 70 consecutively recruited patients who underwent thyroidectomy for benign process and whose TgAb and TPOAb values were retrieved from clinical records. Histological sections of thyroid surgical samples were revised, looking for PLNF and lymphocytic infiltrate. HBME1 expression was assessed by immunohistochemistry. (3) Results: Our results showed a significant association between TgAb, PLNF, and lymphocytic infiltrate. The presence of TgAb was highly specific, but less sensitive, in predicting the presence of PLNF (sensitivity = 0.6, specificity = 0.9; positive predictive value (PPV) = 0.88; negative predictive value (NPV) = 0.63). TgAb positivity showed a good association with the presence of lymphocytic infiltrate (sensitivity = 0.62, specificity = 0.9; PPV = 0.88 and NPV = 0.68). HBME1 immunoreactivity was observed in the colloid of follicles showing PLNF and/or closely associated with LI. (4) Conclusions: The presence of PLNF and LI is associated with serum TgAb positivity. The presence of TgAb and of LI could be triggered by an altered thyroglobulin contained in the HBME1-positive colloid, and could be a first defense mechanism against PLNF that probably represent early dysplastic changes in thyrocytes.

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Sialic acid expression in autoimmune thyroiditis

Cited by 15 publications

References 8 publications

Glycosylation in the Thyroid Gland: Vital Aspects of Glycoprotein Function in Thyrocyte Physiology and Thyroid Disorders

Glycosylation in the Thyroid Gland: Vital Aspects of Glycoprotein Function in Thyrocyte Physiology and Thyroid Disorders

Serum Levels of Glycoproteins are Elevated in Patients with Ovarian Cancer

Serum Anti-Thyroglobulin Autoantibodies Are Specific in Predicting the Presence of Papillary-like Nuclear Features and Lymphocytic Infiltrate in the Thyroid Gland

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