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.
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.
  
  
  CONCLUSIONS
  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.
  
  
  CONCLUSIONS
  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.
authors.affiliation: Section MIG (Microbiology, Immunology, Glycobiology), Department of Laboratory Medicine, Lund University, Lund, Sweden. michael.carlsson@med.lu.se
authors.forename: Michael C
authors.initials: MC
authors.lastname: Carlsson
authors.forename: Crina I A
authors.initials: CI
authors.lastname: Balog
authors.forename: Ola
authors.initials: O
authors.lastname: Kilsgård
authors.forename: Thomas
authors.initials: T
authors.lastname: Hellmark
authors.forename: Omran
authors.initials: O
authors.lastname: Bakoush
authors.forename: Mårten
authors.initials: M
authors.lastname: Segelmark
authors.forename: Mårten
authors.initials: M
authors.lastname: Fernö
authors.forename: Håkan
authors.initials: H
authors.lastname: Olsson
authors.forename: Johan
authors.initials: J
authors.lastname: Malmström
authors.forename: Manfred
authors.initials: M
authors.lastname: Wuhrer
authors.forename: Hakon
authors.initials: H
authors.lastname: Leffler
mesh_terms: D015415:Biomarkers / Q000097:blood / Q000378:metabolism; D001798:Blood Proteins / Q000378:metabolism*; D001943:Breast Neoplasms / Q000097:blood / Q000175:diagnosis / Q000473:pathology; D002277:Carcinoma / Q000097:blood / Q000175:diagnosis / Q000473:pathology; D016022:Case-Control Studies; D002846:Chromatography, Affinity; D005260:Female; D037483:Galectin 1 / Q000378:metabolism*; D037161:Galectins / Q000378:metabolism*; D006023:Glycoproteins / Q000097:blood / Q000378:metabolism*; D006801:Humans; D007249:Inflammation / Q000175:diagnosis* / Q000378:metabolism / Q000473:pathology; D009362:Neoplasm Metastasis; D009369:Neoplasms / Q000175:diagnosis* / Q000378:metabolism / Q000473:pathology; D011485:Protein Binding / Q000502:physiology; D044967:Serum / Q000737:chemistry / Q000378:metabolism*
chemical_list: D015415:Biomarkers; D001798:Blood Proteins; D037483:Galectin 1; D037161:Galectins; D006023:Glycoproteins; C091991:LGALS8 protein, human