The expression and functional analysis of the sialyl-T antigen in prostate cancer

Bai, Ruifeng; Luan, Xue; Robbe-Masselot, Catherine; Brockhausen, Inka; Gao, Yin

doi:10.1007/s10719-020-09927-x

Cited by 25 publications

(18 citation statements)

References 36 publications

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“…Downregulation of ST3Gal-I reduces the tumor size in xenograft mouse model. [30] Comprehensive proteomic approaches of FUT8 overexpressing PCa cells.…”

Section: Glycosylationmentioning

confidence: 99%

“…The glycoproteomic approach to prostate cancer yielded several other publications (Table 1) that show the diversity of processes in prostate cancer that implicate glycosylation. [30]; cell adhesion [99]; N-linked glycans: in vitro proliferation, migration, invasion [101].…”

Section: Glycosylationmentioning

confidence: 99%

“…Current methods that are available do not offer satisfying solution to this issue. Therefore, glycans were suggested to be considered as a supplement to the current tools to diagnose prostate cancer rapidly, and to precisely determine tumor O-linked glycans: in vitro proliferation, migration, apoptosis; tumor size in mouse model [30]; cell adhesion [99];…”

Section: Fucosementioning

confidence: 99%

“…O-linked glycans: in vitro proliferation, migration, apoptosis; tumor size in mouse model [30]; cell adhesion [99]; N-linked glycans: in vitro proliferation, migration, invasion [101].…”

Section: Sialylationmentioning

confidence: 99%

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Post-Translational Modifications That Drive Prostate Cancer Progression

Samaržija

2021

Biomolecules

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While a protein primary structure is determined by genetic code, its specific functional form is mostly achieved in a dynamic interplay that includes actions of many enzymes involved in post-translational modifications. This versatile repertoire is widely used by cells to direct their response to external stimuli, regulate transcription and protein localization and to keep proteostasis. Herein, post-translational modifications with evident potency to drive prostate cancer are explored. A comprehensive list of proteome-wide and single protein post-translational modifications and their involvement in phenotypic outcomes is presented. Specifically, the data on phosphorylation, glycosylation, ubiquitination, SUMOylation, acetylation, and lipidation in prostate cancer and the enzymes involved are collected. This type of knowledge is especially valuable in cases when cancer cells do not differ in the expression or mutational status of a protein, but its differential activity is regulated on the level of post-translational modifications. Since their driving roles in prostate cancer, post-translational modifications are widely studied in attempts to advance prostate cancer treatment. Current strategies that exploit the potential of post-translational modifications in prostate cancer therapy are presented.

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“…Downregulation of ST3Gal-I reduces the tumor size in xenograft mouse model. [30] Comprehensive proteomic approaches of FUT8 overexpressing PCa cells.…”

Section: Glycosylationmentioning

confidence: 99%

Section: Glycosylationmentioning

confidence: 99%

Section: Fucosementioning

confidence: 99%

“…O-linked glycans: in vitro proliferation, migration, apoptosis; tumor size in mouse model [30]; cell adhesion [99]; N-linked glycans: in vitro proliferation, migration, invasion [101].…”

Section: Sialylationmentioning

confidence: 99%

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Post-Translational Modifications That Drive Prostate Cancer Progression

Samaržija

2021

Biomolecules

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“…Further research focused on examination of ST3Gal-I function in PC-3 cells; ST3Gal-I silencing studies indicated that ST3Gal-I is correlated with migration, proliferation and apoptosis of PC-3 cells. Subsequently, in vivo studies showed that decreased ST3Gal-I expression was associated with a reduction in tumor size in a xenograft mouse model, demonstrating that sialyl-T antigen could be considered as a biomarker for the prognosis of prostate cancer metastasis (Table 3) [124].…”

Section: Truncated O-glycansmentioning

confidence: 99%

Glycosylation: Rising Potential for Prostate Cancer Evaluation

Kałuża

Szczykutowicz

Ferens-Sieczkowska

2021

Cancers

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Prostate cancer is the second most commonly diagnosed cancer among men. Alterations in protein glycosylation are confirmed to be a reliable hallmark of cancer. Prostate-specific antigen is the biomarker that is used most frequently for prostate cancer detection, although its lack of sensitivity and specificity results in many unnecessary biopsies. A wide range of glycosylation alterations in prostate cancer cells, including increased sialylation and fucosylation, can modify protein function and play a crucial role in many important biological processes in cancer, including cell signalling, adhesion, migration, and cellular metabolism. In this review, we summarize studies evaluating the prostate cancer associated glycosylation related alterations in sialylation, mainly α2,3-sialylation, core fucosylation, branched N-glycans, LacdiNAc group and presence of truncated O-glycans (sTn, sT antigen). Finally, we discuss the great potential to make use of glycans as diagnostic and prognostic biomarkers for prostate cancer.

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Alcohol induces α2‐6sialo mucin O‐glycans that kill U937 macrophages mediated by sialic acid‐binding immunoglobulin‐like lectin 7 (Siglec 7)

Cheng,

Hothpet,

Bhat

et al. 2024

FEBS Open Bio

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Alcohol misuse increases infections and cancer fatalities, but mechanisms underlying its toxicity are ill‐defined. We show that alcohol treatment of human tracheobronchial epithelial cells leads to inactivation of giantin‐mediated Golgi targeting of glycosylation enzymes. Loss of core 2 N‐acetylglucosaminyltransferase 1, which uses only giantin for Golgi targeting, coupled with shifted targeting of other glycosylation enzymes to Golgi matrix protein 130‐Golgi reassembly stacking protein 65, the site normally used by core 1 enzyme, results in loss of sialyl Lewis x and increase of sialyl Lewis a and α2‐6sialo mucin O‐glycans. The α2‐6sialo mucin O‐glycans induced by alcohol cause death of U937 macrophages mediated by sialic acid‐binding immunoglobulin‐like lectin 7. These results provide a mechanistic insight into the cause of the toxic effects of alcohol and might contribute to the development of therapies to alleviate its toxicity.

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The expression and functional analysis of the sialyl-T antigen in prostate cancer

Cited by 25 publications

References 36 publications

Post-Translational Modifications That Drive Prostate Cancer Progression

Post-Translational Modifications That Drive Prostate Cancer Progression

Glycosylation: Rising Potential for Prostate Cancer Evaluation

Alcohol induces α2‐6sialo mucin O‐glycans that kill U937 macrophages mediated by sialic acid‐binding immunoglobulin‐like lectin 7 (Siglec 7)

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