Glycoprotein Disease Markers and Single Protein-omics

Chandler, Kevin Brown; Goldman, Radoslav

doi:10.1074/mcp.r112.026930

Cited by 55 publications

(44 citation statements)

References 102 publications

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“…A growing body of evidence indicates that focusing on an aberrant glycan on a certain serum protein is a promising approach to the development of glycan‐related biomarkers . Prior to these studies, numerous studies demonstrated glycan alterations during carcinogenesis and tumor progression .…”

Section: Introductionmentioning

confidence: 99%

Large‐scale identification of secretome glycoproteins recognized by Wisteria floribunda agglutinin: A glycoproteomic approach to biomarker discovery

et al. 2015

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One of the promising approaches to the development of cancer diagnostic systems is quantification of a specific protein carrying cancerous glycans. Potential utility of Wisteria floribunda agglutinin (WFA) for such assays has been suggested for several cancer types. To develop such diagnostic systems, identification of WFA-recognized glycoproteins is essential. Here, we successfully identified 504 WFA-recognized glycoproteins from the secretome of HEK293T cells. Most of the identified proteins were likely soluble or single-pass transmembrane proteins, which may serve as specific proteins for the diagnosis using biological fluids. Our method may help to discover marker glycoproteins for various cancers generating WFA-recognized glycans.

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Section: Introductionmentioning

confidence: 99%

Large‐scale identification of secretome glycoproteins recognized by Wisteria floribunda agglutinin: A glycoproteomic approach to biomarker discovery

et al. 2015

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“…Analysis of plasma membrane proteins and their posttranslational modifications is critical for the effective identification of disease markers and targets for drug treatment [2,6,55]. Glycosylation is a well known posttranslational modification in many secreted proteins.…”

Section: Discussionmentioning

confidence: 99%

Rat liver sinusoidal surface N-linked glycoproteomic analysis by affinity enrichment and mass spectrometric identification

Gao

Miao

et al. 2015

Biochemistry Moscow

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Glycosylation in liver is one of the most biologically important protein modifications. It plays critical roles in many physiological and pathological processes by virtue of its unique location at the blood-tissue interface, including angiogenesis, liver cancer, cirrhosis, and fibrosis. To analyze glycosylation of plasma membrane proteins in liver sinusoidal endothelial cells (LSEC), N-glycopeptides of the LSEC surface were enriched using a filter-assisted sample preparation-based lectin affinity capture method and subsequently identified with mass spectrometry. In total, 225 unique N-glycosylation sites on 152 glycoproteins were identified, of which 119 (53%) sites had not previously been determined experimentally. Among the glycoproteins, 53% were classified as plasma membrane proteins and 47 (31%) as signaling proteins and receptors. Moreover, 23 cluster of differentiation antigens with 49 glycopeptides were detected within the membrane glycoproteins of the liver sinusoidal surface. Furthermore, bioinformatics analysis revealed that the majority of identified glycoproteins have an impact on processes of LSEC. Therefore, N-glycoproteomic analysis of the liver sinusoidal surface may provide useful information on liver regeneration and facilitate liver disease diagnosis.

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“…Due to their demonstrated involvement in molecular signalling, glycoproteins and glycolipids present on the cell surface of tumour cells and host response cells, glycans are potential good candidates to provide indications pertaining to cancer pathogenesis and prognosis, including the metastatic potential (Saldova et al., 2011). Recent studies point to glycosylation events that are different when comparing tumour cells to healthy cells and tissues (Chandler and Goldman, 2013; Potapenko et al., 2009), including differences in many N‐ and O‐glycans attached to cell surface proteins. Alterations in synthesis, modifications, transfer and degradation of glycans are all processes that affect glycosylation.…”

Section: Introductionmentioning

confidence: 99%

Serum N‐glycan analysis in breast cancer patients – Relation to tumour biology and clinical outcome

et al. 2015

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Glycosylation and related processes play important roles in cancer development and progression, including metastasis. Several studies have shown that N-glycans have potential diagnostic value as cancer serum biomarkers. We have explored the significance of the abundance of particular serum N-glycan structures as important features of breast tumour biology by studying the serum glycome and tumour transcriptome (mRNA and miRNA) of 104 breast cancer patients. Integration of these types of molecular data allows us to study the relationship between serum glycans and transcripts representing functional pathways, such as metabolic pathways or DNA damage response. We identified tri antennary trigalactosylated trisialylated glycans in serum as being associated with lower levels of tumour transcripts involved in focal adhesion and integrin-mediated cell adhesion. These glycan structures were also linked to poor prognosis in patients with ER negative tumours. High abundance of simple monoantennary glycan structures were associated with increased survival, particularly in the basal-like subgroup. The presence of circulating tumour cells was found to be significantly associated with several serum glycome structures like bi and triantennary, di- and trigalactosylated, di- and trisialylated. The link between tumour miRNA expression levels and N-glycan production is also examined.

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Glycoprotein Disease Markers and Single Protein-omics

Cited by 55 publications

References 102 publications

Large‐scale identification of secretome glycoproteins recognized by Wisteria floribunda agglutinin: A glycoproteomic approach to biomarker discovery

Large‐scale identification of secretome glycoproteins recognized by Wisteria floribunda agglutinin: A glycoproteomic approach to biomarker discovery

Rat liver sinusoidal surface N-linked glycoproteomic analysis by affinity enrichment and mass spectrometric identification

Serum N‐glycan analysis in breast cancer patients – Relation to tumour biology and clinical outcome

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