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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, Michael LU ; Balog, Crina I A; Kilsgård, Ola LU ; Hellmark, Thomas LU ; Bakoush, Omran LU ; Segelmark, Mårten LU ; Fernö, Mårten LU ; Olsson, Håkan LU ; Malmström, Johan LU and Wuhrer, Manfred, et al. (2012) In Biochimica et Biophysica Acta 1820(9). p.1366-1372
Abstract
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. METHODS: 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,... (More)
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. METHODS: 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. RESULTS: 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. CONCLUSION: 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. GENERAL 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. (Less)
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Contribution to journal
publication status
published
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Biochimica et Biophysica Acta
volume
1820
issue
9
pages
1366 - 1372
publisher
Elsevier
external identifiers
  • wos:000306444000008
  • pmid:22285770
  • scopus:84862899232
ISSN
0006-3002
DOI
10.1016/j.bbagen.2012.01.007
language
English
LU publication?
yes
id
6703c645-3d73-4248-aad1-07a30b710d6b (old id 2335953)
alternative location
http://www.ncbi.nlm.nih.gov/pubmed/22285770?dopt=Abstract
date added to LUP
2012-02-01 23:09:20
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2017-09-10 04:00:07
@article{6703c645-3d73-4248-aad1-07a30b710d6b,
  abstract     = {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. METHODS: 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. RESULTS: 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. CONCLUSION: 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. GENERAL 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.},
  author       = {Carlsson, Michael and Balog, Crina I A and Kilsgård, Ola and Hellmark, Thomas and Bakoush, Omran and Segelmark, Mårten and Fernö, Mårten and Olsson, Håkan and Malmström, Johan and Wuhrer, Manfred and Leffler, Hakon},
  issn         = {0006-3002},
  language     = {eng},
  number       = {9},
  pages        = {1366--1372},
  publisher    = {Elsevier},
  series       = {Biochimica et Biophysica Acta},
  title        = {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.},
  url          = {http://dx.doi.org/10.1016/j.bbagen.2012.01.007},
  volume       = {1820},
  year         = {2012},
}