IIICS de novo glycosylated fibronectin as a marker for invasiveness in urothelial carcinoma of the urinary bladder (UBC)

Richter, Petra; Junker, Kerstin; Franz, Marcus; Berndt, Angela; Geyer, Christiane; Gajda, Mieczysław; Kosmehl, Hartwig; Berndt, Alexander; Wunderlich, Heiko

doi:10.1007/s00432-008-0390-6

Cited by 16 publications

(14 citation statements)

References 32 publications

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“…Although onfFN was discovered almost 30 years ago (68), until very recently, there had been no studies that describe its role in cancer biology. Over the last few years, the O -glycosylated onfFN has only been used for diagnostic purposes (104). …”

Section: Emt: the Glycan Connectionmentioning

confidence: 99%

Sweet and Sour: The Impact of Differential Glycosylation in Cancer Cells Undergoing Epithelialâ€“Mesenchymal Transition

Freire-de-Lima

2014

Front. Oncol.

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Glycosylation changes are a feature of disease states. One clear example is cancer cells, which commonly express glycans at atypical levels or with different structural attributes than those found in normal cells. Epithelial–mesenchymal transition (EMT) was initially recognized as an important step for morphogenesis during embryonic development, and is now shown to be one of the key steps promoting tumor metastasis. Cancer cells undergoing EMT are characterized by significant changes in glycosylation of the extracellular matrix (ECM) components and cell-surface glycoconjugates. Current scientific methodology enables all hallmarks of EMT to be monitored in vitro and this experimental model has been extensively used in oncology research during the last 10 years. Several studies have shown that cell-surface carbohydrates attached to proteins through the amino acids, serine, or threonine (O-glycans), are involved in tumor progression and metastasis, however, the impact of O-glycans on EMT is poorly understood. Recent studies have demonstrated that transforming growth factor-beta (TGF-β), a known EMT inducer, has the ability to promote the up-regulation of a site-specific O-glycosylation in the IIICS domain of human oncofetal fibronectin, a major ECM component expressed by cancer cells and embryonic tissues. Armed with the knowledge that cell-surface glycoconjugates play a major role in the maintenance of cell homeostasis and that EMT is closely associated with glycosylation changes, we may benefit from understanding how unusual glycans can govern the molecular pathways associated with cancer progression. This review initially focuses on some well-known changes found in O-glycans expressed by cancer cells, and then discusses how these alterations may modulate the EMT process.

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Section: Emt: the Glycan Connectionmentioning

confidence: 99%

Sweet and Sour: The Impact of Differential Glycosylation in Cancer Cells Undergoing Epithelialâ€“Mesenchymal Transition

Freire-de-Lima

2014

Front. Oncol.

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“…The quantitative evaluation of IIICS O-linked glycosylated FN is believed to be among the most effective markers for preterm delivery [14] and a valuable histological marker for the invasiveness of urothelial carcinoma of the urinary bladder [15]. The role of mucin-type O-glycan has not been elucidated.…”

Section: Introductionmentioning

confidence: 99%

Expression and potential biological role of α(1,2)fucosylated glycotopes on amniotic and seminal fibronectins

Kątnik-Prastowska¹,

Orczyk-Pawiłowicz²

2011

Biochemical Society Transactions

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The present paper describes concisely the expression and role of α(1,2)-linked fucose on some glycoconjugates as well as the detection, distribution and potential role of that glycotope on human soluble plasma and cellular fibronectins in addition to the expression on both normal and pathological amniotic fluid and seminal plasma fibronectins. The determination of α(1,2)fucosylated glycans is considered with respect to its usefulness as a potential clinically applicable biomarker in obstetrics to monitor pregnancy and in andrology to evaluate the ejaculate of infertile men and in vitro fertilization.

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“…Thus, we suggest an intravesicular proteolytic degradation of Tn-C by tumour-derived proteolytic enzymes. Comparable results have been presented recently for collagen type IV, laminin and Wbronectin in renal cell carcinoma (Sherief et al 2003) and also for de novo glycosylated Wbronectin in UBC (Richter et al 2008). In congruence, Papale et al (2007) recently showed that repeated freeze-thaw cycles and room temperature storage have only moderate eVects on protein proWling in urine by SELDI technology.…”

Section: Discussionmentioning

confidence: 55%

B and C domain containing tenascin-C: urinary markers for invasiveness of urothelial carcinoma of the urinary bladder?

Richter

Tost

Franz

et al. 2009

J Cancer Res Clin Oncol

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Purpose Surveillance of urothelial carcinoma of the urinary bladder (UBC) patients with respect to tumour recurrence and invasiveness is crucial for therapy and prognosis. Therefore, evaluation of non-invasive methods to monitor tumour progression is of high clinical interest. The study was aimed at investigating urinary concentrations of tenascin-C splicing domains for their value as tumour surveillance markers.

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IIICS de novo glycosylated fibronectin as a marker for invasiveness in urothelial carcinoma of the urinary bladder (UBC)

Cited by 16 publications

References 32 publications

Sweet and Sour: The Impact of Differential Glycosylation in Cancer Cells Undergoing Epithelialâ€“Mesenchymal Transition

Sweet and Sour: The Impact of Differential Glycosylation in Cancer Cells Undergoing Epithelialâ€“Mesenchymal Transition

Expression and potential biological role of α(1,2)fucosylated glycotopes on amniotic and seminal fibronectins

B and C domain containing tenascin-C: urinary markers for invasiveness of urothelial carcinoma of the urinary bladder?

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