The effect of plant lectins on the survival and malignant behaviors of thyroid cancer cells

Abstract

Altered or aberrant glycosylation is a common phenomenon in cancer cells and it originates from changes in the expression of the enzymes, glycosyltransferase, and glycosidase which up-regulate in response to some oncogenes in the glycan synthesis pathway. In this present study, it has been aimed to determine the alteration of sialic acid and fucose expressions in the cell surface of human thyroid carcinoma cells and investigate the changes in tumorigenic and malignant characters after treating them with specific plant lectins. Our study showed that the cell surface glycan chains of anaplastic 8305C, follicular FTC-133, and papillary K1 thyroid carcinoma cells were rich in α-2,6, α-2,3, sialic acid, and α-1,6 fucose residues. When the cells were treated with specific doses of Maackia amurensis lectin II (MAL), Sambucus nigra agglutinin (SNA), and Aleuria aurantia lectin (AAL) which have specific binding capacity for the detected glycan residues, respectively their cancerous traits changed dramatically. Remarkable findings obtained from MAL treatment leading to necrosis in 8505C cells without any toxicity for normal thyroid epithelial cells but it had proliferative effect on K1 and FCT-133 cells. Besides, MAL and SNA treatment decreased the mobility of 8505C and K1 cells. MAL and SNA lectins dramatically reduced the endothelial affinity of the cells and AAL significantly attenuated that of 8050C and K1 cells but not FTC-133. These results suggest that altered cell surface glycosylation in thyroid cancer seems to be a strong candidate for developing new therapeutic strategies.

Lectin Treatment Affects Malignant Characteristics of TPC-1 Papillary Thyroid Cancer Cells

“…However, it has been demonstrated that AAL treatment increases the mobility of 8505C cells. It has been also shown that MAL-II and SNA treatment to FTC-133 follicular thyroid cancer cells increases cell mobility (29). Our findings have been pointed out that MAL-II, SNA and AAL lectin treatment significantly increase cell mobility on TPC-1 papillary cancer cells.…”

Increase of MAL-II Binding Alpha2,3-Sialylated Glycan Is Associated with 5-FU Resistance and Short Survival of Cholangiocarcinoma Patients

“…It plays many roles in normal physiology, for example, neural differentiation [6], tissue regeneration [7,8], and resistance to influenza virus infection [9,10]. The increase of sialylation and sialylated-glycans were associated with development and progression of human diseases including cancer [10][11][12][13][14][15]. Sialylation plays important roles in tumor metastasis of many types of cancer such as colon [16], thyroid [14], and melanoma [17].…”

“…The increase of sialylation and sialylated-glycans were associated with development and progression of human diseases including cancer [10][11][12][13][14][15]. Sialylation plays important roles in tumor metastasis of many types of cancer such as colon [16], thyroid [14], and melanoma [17]. In addition, sialylation is involved in chemoresistance of ovarian [18,19], gastric [20], and colon [21] cancers.…”

“…Sialic binding lectins, such as Maackia amurensis lectin-II (MAL-II, α2,3-sialylated glycan binding lectin) and Sambucus nigra agglutinin (SNA, α2,6-sialylated glycan binding lectin), have been used for detecting and studying biological roles of sialylated-glycans in human diseases [9,11,12,14,15,17,[22][23][24][25].…”

MicroRNA‑30a suppresses papillary thyroid cancer cell proliferation, migration and invasion by directly targeting E2F7

“…The incidence of thyroid cancer (TC) is the highest among endocrine malignancies (1)(2)(3)(4), with ~62,450 new diagnoses and ~1,950 TC mortalities in 2015 alone (5). Furthermore, the incidence of TC has increased rapidly in recent years and as such has attracted more scientific attention; the age-adjusted incidence of TC is estimated to be 9.1 per 100,000 females and 2.9 per 100,000 males in developed countries (6)(7)(8)(9).…”