Glycans: potential therapeutic targets for cholangiocarcinoma and their therapeutic and diagnostic implications

Silsirivanit, Atit

doi:10.1080/14728222.2021.1861250

Cited by 8 publications

(9 citation statements)

References 15 publications

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“…Alteration of glycosylation has been shown to be involved in tumor growth, metastasis and therapeutic resistance [ 16 , 17 ]. Several specific glycans are applicable as markers for diagnosis, monitoring and prognostic prediction of many cancer types [ 18 , 19 ]. In CCA, several CCA-associated glycans are involved in tumor progression and are suggested to be the targets for CCA treatment [ 19 ].…”

Section: Discussionmentioning

confidence: 99%

“…Several specific glycans are applicable as markers for diagnosis, monitoring and prognostic prediction of many cancer types [ 18 , 19 ]. In CCA, several CCA-associated glycans are involved in tumor progression and are suggested to be the targets for CCA treatment [ 19 ]. Indramanee et al used histochemistry of 14 commercially available lectins to detect alteration of glycans in patient CCA tissues, and found that almost all lectins tested gave positive signals with normal bile duct, HP/DP and CCA, including hepatocytes and stromal cells [ 3 ].…”

Section: Discussionmentioning

confidence: 99%

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A Novel Serum Glycobiomarker for Diagnosis and Prognosis of Cholangiocarcinoma Detected by Butea monosperma Agglutinin

et al. 2021

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Plant lectins are widely used in medical glycosciences and glycotechnology. Many lectin-based techniques have been applied for the detection of disease-associated glycans and glycoconjugates. In this study, Butea monosperma agglutinin (BMA), a lectin purified from seeds of the medicinal plant Butea monosperma, was used for the detection of cholangiocarcinoma (CCA)-associated glycans. Expression of BMA-binding N-acetyl galactosamine/galactose (GalNAc/Gal)-associated glycan (BMAG) in CCA tissues was determined using BMA lectin histochemistry; the results showed that BMAG was undetectable in normal bile ducts and drastically increased in preneoplastic bile ducts and CCA. The study in hamsters showed that an increase of BMAG was associated with carcinogenesis of CCA. Using an in-house double BMA sandwich enzyme-linked lectin assay, BMAG was highly detected in the sera of CCA patients. The level of serum BMAG in CCA patients (N = 83) was significantly higher than non-CCA controls (N = 287) and it was applicable for diagnosis of CCA with 55.4% sensitivity, 81.9% specificity, and 76.0% accuracy. A high level of serum BMAG (≥82.5 AU/mL) was associated with unfavorable survival of CCA patients; this information suggested the potential of serum BMAG as a poor prognostic indicator of CCA. In summary, BMAG was aberrantly expressed in preneoplastic bile ducts and CCA, it was also highly detected in patient serum which potentially used as a marker for diagnosis and prognostic prediction of CCA.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

A Novel Serum Glycobiomarker for Diagnosis and Prognosis of Cholangiocarcinoma Detected by Butea monosperma Agglutinin

et al. 2021

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“…These aberrantly expressed glycans are possibly used as a biomarker or a target for the treatment of cancers. Many tumor-associated glycans were demonstrated to play essential roles in tumor development, progression, and therapeutic resistance [2,5].…”

Section: Introductionmentioning

confidence: 99%

Glycan and Glycosylation as a Target for Treatment of Glioblastoma

Silsirivanit¹

2023

Glioblastoma - Current Evidence

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Glycosylation is an important post-translational modification regulating many cellular processes. In cancer, aberrant glycosylation leads to the expression of tumor-associated glycans that are possibly used as therapeutic targets or biomarkers for diagnosis, monitoring, and prognostic prediction. The cumulative evidence suggested the significance of alteration of glycosylation in glioblastoma (GBM). Aberrant glycosylation presents truncated or uncommon glycans on glycoproteins, glycolipids, and other glycoconjugates. These aberrant glycans consequently promote the tumor development, metastasis, and therapeutic resistance. The glycosylation changes occurred in either cancer cells or the tumor microenvironment. GBM-associated glycans and their corresponding enzymes are proposed to be a target for GBM treatment. Several tools, such as lectin and inhibitors, are possibly applied to target the tumor-associated glycans and glycosylation for the treatment of GBM. This chapter provides information insight into glycosylation changes and their roles in the development and progression of GBM. The perspectives on targeting glycans and glycosylation for the treatment of GBM are enclosed.

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“…CCA is characterized by an aberration of genetics, epigenetics, and post-translation modification [1]. Dysregulation of glycosylation has a significant role in the development and progression of CCA [3,4]. Aberrant glycosylations in CCA (e.g., mucin MUC5AC, MUC1, CCA-CA, carbohydrate antigen 19-9 (CA19-9), and CA-S27) have been used as proxies for CCA diagnosis as their altered expressions are correlated with the progression of CCA [4].…”

Section: Introductionmentioning

confidence: 99%

“…Dysregulation of glycosylation has a significant role in the development and progression of CCA [3,4]. Aberrant glycosylations in CCA (e.g., mucin MUC5AC, MUC1, CCA-CA, carbohydrate antigen 19-9 (CA19-9), and CA-S27) have been used as proxies for CCA diagnosis as their altered expressions are correlated with the progression of CCA [4]. Mucins MUC1 and MUC5AC are strongly expressed in CCA and are related to the more aggressive phenotypes [5,6].…”

Section: Introductionmentioning

confidence: 99%

Down-Regulation of C1GALT1 Enhances the Progression of Cholangiocarcinoma through Activation of AKT/ERK Signaling Pathways

Khiaowichit

Talabnin

Dechsukhum

et al. 2022

Life

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Alteration of mucin-type O-glycosylation is implicated in tumor progression and metastasis of cholangiocarcinoma (CCA). Core 1 β1-3 Galactosyltransferase (C1GALT1) is a primary enzyme that regulates the elongation of core 1-derived mucin-type O-glycans. Dysregulation of C1GALT1 has been documented in multiple cancers and is associated with aberrant core 1 O-glycosylation and cancer aggressiveness; however, the expression of C1GALT1 and its role in CCA progression remains unknown. Our study demonstrated that C1GALT1 was downregulated in CCA tissues at both the mRNA and protein levels. The biological function of C1GALT1 using siRNA demonstrated that suppression of C1GALT1 in the CCA cell lines (KKU-055 and KKU-100) increased CCA progression, evidenced by: (i) Induction of CCA cell proliferation and 5-fluorouracil resistance in a dose-dependent manner; (ii) up-regulation of growth-related genes, ABC transporter genes, and anti-apoptotic proteins; and (iii) an increase in the activation/phosphorylation of AKT and ERK in silencing C1GALT1 cells. We demonstrated that silencing C1GALT1 in CCA cell lines was associated with immature core 1 O-glycosylation, demonstrated by high expression of VVL-binding glycans and down-regulation of other main O-linked glycosyltransferases β1,3-N-acetylglucosaminyltransferase 6 (B3GNT6) and ST6 N-Acetylgalactosaminide Alpha-2,6-Sialyltransferase 1 (ST6GALNAC1) in C1GALT1 knockdown. Our findings demonstrate that down-regulation of C1GALT1 in CCA increases the expression of immature core 1 O-glycan, enhancing CCA progression, including growth and 5-fluorouracil resistance via the activation of the AKT/ERK signaling pathway.

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Glycans: potential therapeutic targets for cholangiocarcinoma and their therapeutic and diagnostic implications

Cited by 8 publications

References 15 publications

A Novel Serum Glycobiomarker for Diagnosis and Prognosis of Cholangiocarcinoma Detected by Butea monosperma Agglutinin

A Novel Serum Glycobiomarker for Diagnosis and Prognosis of Cholangiocarcinoma Detected by Butea monosperma Agglutinin

Glycan and Glycosylation as a Target for Treatment of Glioblastoma

Down-Regulation of C1GALT1 Enhances the Progression of Cholangiocarcinoma through Activation of AKT/ERK Signaling Pathways

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