The extracellular matrix in cancer progression: Role of hyalectan proteoglycans and ADAMTS enzymes

Binder, Marley J.; McCoombe, Scott; Williams, Elizabeth D.; McCulloch, Daniel R.; Ward, Alister C.

doi:10.1016/j.canlet.2016.11.001

Cited by 65 publications

(51 citation statements)

References 181 publications

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“…Owing to unclear substrate specificity of OpeRATOR for O‐linked glycans, the site‐specific O‐linked glycosylation by glycans in addition to Core 1 glycans merits future investigation. VCAN and ACAN are known proteoglycans that have long sugar chains in normal condition (Binder et al , ). The extensive addition of short core 1 O‐linked glycans to these two proteins would be expected to enhance their mucin‐type properties such as resistance to enzymatic digestion and improved stiffness, and this in turn may alter their biological and biomechanical properties producing some remodeling of the tumor microenvironment (Kufe, ).…”

Section: Resultsmentioning

confidence: 99%

Mapping the O‐glycoproteome using site‐specific extraction of O‐linked glycopeptides (EXoO)

Yang

et al. 2018

Molecular Systems Biology

128

181

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Protein glycosylation is one of the most abundant post‐translational modifications. However, detailed analysis of O‐linked glycosylation, a major type of protein glycosylation, has been severely impeded by the scarcity of suitable methodologies. Here, a chemoenzymatic method is introduced for the site‐specific extraction of O‐linked glycopeptides (EXoO), which enabled the mapping of over 3,000 O‐linked glycosylation sites and definition of their glycans on over 1,000 proteins in human kidney tissues, T cells, and serum. This large‐scale localization of O‐linked glycosylation sites demonstrated that EXoO is an effective method for defining the site‐specific O‐linked glycoproteome in different types of sample. Detailed structural analysis of the sites identified revealed conserved motifs and topological orientations facing extracellular space, the cell surface, the lumen of the Golgi, and the endoplasmic reticulum (ER). EXoO was also able to reveal significant differences in the O‐linked glycoproteome of tumor and normal kidney tissues pointing to its broader use in clinical diagnostics and therapeutics.

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Section: Resultsmentioning

confidence: 99%

Mapping the O‐glycoproteome using site‐specific extraction of O‐linked glycopeptides (EXoO)

Yang

et al. 2018

Molecular Systems Biology

128

181

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“…3C red asterisk in lower panel). VCAN and ACAN are known proteoglycans that have long sugar chains in normal condition 29 . The extensive addition of short core 1 O-linked glycans to these two proteins would be expected to enhance their mucin-type properties such as resistance to enzymatic digestion and improved stiffness and this in turn may alter their biological and biomechanical properties producing some remodelling of the tumor microenvironment 30 .…”

Section: Resultsmentioning

confidence: 99%

Mapping In Vivo O-Glycoproteome Using Site-specific Extraction of O-linked glycopeptides (EXoO)

Yang

et al. 2018

Preprint

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24 Protein glycosylation is one of the most abundant post-translational modifications. However, 25 detailed analysis of in vivo O-linked glycosylation, a major type of protein glycosylation, has 26 been severely impeded by the scarcity of suitable methodologies. Here, we present a 27 chemoenzymatic method for the site-specific extraction of O-linked glycopeptides (EXoO), 28 which enabled the unambiguous mapping of over 3,000 O-linked glycosylation sites and 29 definition of their glycans on over 1,000 proteins in human kidney tissues, T cells and serum. 30 This large-scale localization of O-linked glycosylation sites nearly doubles the number of 31 previously identified sites, demonstrating that EXoO is the most effective method to-date for 32 defining the site-specific O-linked glycoproteome in different types of sample. Detailed 33 structural analysis of the sites identified revealed conserved motifs and topological orientations 34 facing extracellular space, the cell surface, the lumen of the ER and the Golgi. EXoO was also 35 able to reveal significant differences in the in vivo O-linked glycoproteome of tumor and normal 36 kidney tissues pointing to its broader use in clinical diagnostics and therapeutics. 37 38

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“…На основании существования этой двойной активности на N-и С-концах молекулы был предложен термин «галектан», акроним для гиалурон-и лектин-связывающих ПГ [1]. Функционирование галектанов регулируется путем протеолитического расщепления металлопротеиназами семейства ADAMTS (дезинтег-рин и металлопротеиназа с фрагментом тромбоспон-дина) [24,25].…”

Section: обзорные статьиunclassified

Proteoglycans in normal physiology and carcinogenesis

Суховских¹,

Григорьева²

2018

Usp. mol. onkol

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The extracellular matrix in cancer progression: Role of hyalectan proteoglycans and ADAMTS enzymes

Cited by 65 publications

References 181 publications

Mapping the O‐glycoproteome using site‐specific extraction of O‐linked glycopeptides (EXoO)

Mapping the O‐glycoproteome using site‐specific extraction of O‐linked glycopeptides (EXoO)

Mapping In Vivo O-Glycoproteome Using Site-specific Extraction of O-linked glycopeptides (EXoO)

Proteoglycans in normal physiology and carcinogenesis

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