Relation between raised concentrations of fucose, sialic acid, and acute phase proteins in serum from patients with cancer: choosing suitable serum glycoprotein markers.

Turner, G. A.; Skillen, A. W.; Buamah, Paul K.; Guthrie, David; Welsh, James S.; Harrison, J. R.; Kowalski, Alicia M.

doi:10.1136/jcp.38.5.588

Cited by 67 publications

(46 citation statements)

References 14 publications

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“…This is mainly due to changes in their production by hepatocytes triggered by cytokines secreted by macrophages and monocytes at inflammatory sites [23]. Elevated levels of acute phase proteins have also been found in cancer [24], in which the hepatocyte stimulating cytokines are most likely produced by the tumour microenvironment [25]. However, the source of acute phase proteins might also be peripheral; both cancer cells and non-hepatic normal cells, e.g.…”

Section: Discussionmentioning

confidence: 99%

Different fractions of human serum glycoproteins bind galectin-1 or galectin-8, and their ratio may provide a refined biomarker for pathophysiological conditions in cancer and inflammatory disease

Carlsson

Balog

Kilsgård

et al. 2012

Biochimica et Biophysica Acta (BBA) - General Subjects

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Background: Changes in glycosylation of serum proteins are common, and various glycoforms are being explored as biomarkers in cancer and inflammation. We recently showed that glycoforms detected by endogenous galectins not only provide potential biomarkers, but also have different functions when they encounter galectins in tissue cells. Now we have explored the use of a combination of two galectins with different specificities, to further increase biomarker sensitivity and specificity. less thanbrgreater than less thanbrgreater thanMethods: Sera from 14 women with metastatic breast cancer, 12 healthy controls, 14 patients with IgA-nephritis (IgAN), and 12 patients with other glomerulonephritis were fractionated by affinity chromatography on immobilized human galectin-1 or galectin-8N, and the protein amounts of the bound and unbound fractions for each galectin were determined. less thanbrgreater than less thanbrgreater thanResults: Each galectin bound largely different fractions of the serum glycoproteins, including different glycoforms of haptoglobin. In the cancer sera, the level of galectin-1 bound glycoproteins was higher and galectin-8N bound glycoproteins lower compared to the other patients groups, whereas in IgAN sera the level of galectin-8N bound glycoproteins were higher. less thanbrgreater than less thanbrgreater thanConclusion: The ratio of galectin-1 bound/galectin-8N bound glycoproteins showed high discriminatory power between cancer patients and healthy, with AUC of 0.98 in ROC analysis, and thus provides an interesting novel cancer biomarker candidate. less thanbrgreater than less thanbrgreater thanGeneral significance: The galectin-binding ability of a glycoprotein is not only a promising biomarker candidate but may also have a specific function when the glycoprotein encounters the galectin in tissue cells, and thus be related to the pathophysiological state of the patient. This article is part of a Special Issue entitled Glycoproteomics.

Funding Agencies|Swedish Research Council (Vetenskapsradet)||Region Skane||Swedish Cancer Society||Lund University Hospital Foundation||Swedish Research Council|2008-3356|Swedish Foundation for Swedish Research|FFL4|Crafoord Foundation||Swedish Healthcare System||

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Section: Discussionmentioning

confidence: 99%

Different fractions of human serum glycoproteins bind galectin-1 or galectin-8, and their ratio may provide a refined biomarker for pathophysiological conditions in cancer and inflammatory disease

Carlsson

Balog

Kilsgård

et al. 2012

Biochimica et Biophysica Acta (BBA) - General Subjects

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“…Haptoglobin is an 'acute-phase protein' (25) that displays a rapid increase in response to inflammation, injury, wound healing, cancer and many other pathobiological processes, similarly to fibrinogen, ceruloplasmin, ·-1 acid glycoprotein and C-reactive protein (CRP) (15,26). The increase of haptoglobin with aberrant glycosylation, probed by various lectins, has been a target of cancer diagnosis for many years (14)(15)(16)(17).…”

Section: Discussionmentioning

confidence: 99%

N-glycosylation status of β-haptoglobin in sera of patients with prostate cancer vs. benign prostate diseases

Hakomori¹

2009

Int J Oncol

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Abstract. N-glycosylation status of purified ß-haptoglobin separated from sera of patients with prostate cancer was studied in comparison to that of sera from patients with benign prostate diseases, or normal subjects. Two different approaches, as summarized below, one based on binding of lectins and antibodies to ß-haptoglobin, the other on mass spectrometry of released N-linked glycans from ß-haptoglobin, were performed. Some of the results were useful for distinction of prostate cancer vs. benign prostate diseases. i) Binding of Phaseolus vulgaris-L lectin (PHA-L), defining the GlcNAcß6Man·6Man side chain present in tri-or tetraantennary N-linked glycans, to ß-haptoglobin was higher for cases of prostate cancer and high-grade prostate intraepithelial neoplasia than for benign diseases. Binding of Aleuria aurantia lectin (AAL) defining Fuc·3-, ·4-, or ·6-GlcNAc, or monoclonal antibody directed to sialyl-Le x , to ß-haptoglobin was also higher for some of the cancer cases than for benign diseases. Many other lectins and antibodies showed no binding to ß-haptoglobin, or showed no significant difference between cancer vs. benign diseases. ii) Mass spectrometric analysis of N-linked glycans of ß-haptoglobin released by Peptide N-glycosidase-F showed enhanced expression of monosialyl tri-antennary structures in prostate cancer cases. Thus, binding of PHA-L to affinity-purified ß-haptoglobin from sera of patients could lead to development of useful tools for differential diagnosis of prostate cancer vs. benign prostate diseases.

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“…Early studies [44][45] observed an increase in the sialic acid content of cancer AGP glycans compared to normal controls. A more recent study by Hashimoto et al [46] on AGP branching and fucosylation in cancer concluded that changes in microheterogeneity could be used as a marker of carcinoma progression and prognosis.…”

Section: Introductionmentioning

confidence: 99%

Alpha-1-Acid Glycoprotein (AGP) as a Potential Biomarker for Breast Cancer

Smith¹,

Behan²,

Matthews-Smith³

et al. 2012

Glycosylation

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Relation between raised concentrations of fucose, sialic acid, and acute phase proteins in serum from patients with cancer: choosing suitable serum glycoprotein markers.

Cited by 67 publications

References 14 publications

Different fractions of human serum glycoproteins bind galectin-1 or galectin-8, and their ratio may provide a refined biomarker for pathophysiological conditions in cancer and inflammatory disease

Different fractions of human serum glycoproteins bind galectin-1 or galectin-8, and their ratio may provide a refined biomarker for pathophysiological conditions in cancer and inflammatory disease

N-glycosylation status of β-haptoglobin in sera of patients with prostate cancer vs. benign prostate diseases

Alpha-1-Acid Glycoprotein (AGP) as a Potential Biomarker for Breast Cancer

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