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Expression of Helix pomatia Lectin Binding Glycoproteins in Women with Breast Cancer in Relationship to Their Mood Group Phenotypes

Welinder, Charlotte LU ; Jansson, Bo LU ; Fernö, Mårten LU ; Olsson, Håkan LU and Baldetorp, Bo LU (2009) In Journal of Proteome Research 8(2). p.782-786
Abstract
Aberrant glycosylation occurs in essentially all types of human cancers. A difference in glycopattern of proteins will result in a change of function of the proteins. The lectin from Helix pomatia (HPA) recognizes N-acetylgalactosaminylated glycoproteins and very consistent results over the increased binding of HPA in tissue sections are associated with metastasis progression and poor patient prognosis in a range of human adenocarcinomas. The induced modification of protein function after changed glycosylation is unknown, and as a part in characterizing the glycoproteins carrying the specific carbohydrates, we analyzed the major HPA binding proteins in sera from healthy women, women with primary breast cancer with no metastasis (bcmet-),... (More)
Aberrant glycosylation occurs in essentially all types of human cancers. A difference in glycopattern of proteins will result in a change of function of the proteins. The lectin from Helix pomatia (HPA) recognizes N-acetylgalactosaminylated glycoproteins and very consistent results over the increased binding of HPA in tissue sections are associated with metastasis progression and poor patient prognosis in a range of human adenocarcinomas. The induced modification of protein function after changed glycosylation is unknown, and as a part in characterizing the glycoproteins carrying the specific carbohydrates, we analyzed the major HPA binding proteins in sera from healthy women, women with primary breast cancer with no metastasis (bcmet-), and women with metastasizing breast cancer (bcmet+) using lectin affinity chromatography and lectin blotting. The binding ligands were further identified using mass spectrometry (MALDI-TOF MS) to confirm the captured glycoproteins. The major HPA binding proteins in serum were found to be IgA1, complement factor C3, von Willebrand factor (vWF), alpha-2-macroglobulin and IgM. This set of antigens is a panel of candidates for useful HPA related biomarkers in sera, but our results also emphasize the fact that the blood group phenotypes are of most importance when using the lectin HPA in recognition of cancer biomarkers in sera and plasma. The results emphasize that interpretation of an individual change in the glycosylation pattern of a specific tumor marker always needs to be analyzed in its right context. This study shows that the blood group phenotypes can have a major impact on the results when analyzing HPA lectin binding. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
blood, group, serum, breast cancer, GaINAc glycoproteins, Helix pomatia lectin, HPA
in
Journal of Proteome Research
volume
8
issue
2
pages
782 - 786
publisher
The American Chemical Society
external identifiers
  • wos:000263193300038
  • scopus:61849141247
ISSN
1535-3893
DOI
10.1021/pr800444b
language
English
LU publication?
yes
id
5750648f-cf7b-424e-bddf-33cae1b0b2a0 (old id 1374930)
date added to LUP
2009-05-08 14:01:28
date last changed
2017-07-23 03:57:27
@article{5750648f-cf7b-424e-bddf-33cae1b0b2a0,
  abstract     = {Aberrant glycosylation occurs in essentially all types of human cancers. A difference in glycopattern of proteins will result in a change of function of the proteins. The lectin from Helix pomatia (HPA) recognizes N-acetylgalactosaminylated glycoproteins and very consistent results over the increased binding of HPA in tissue sections are associated with metastasis progression and poor patient prognosis in a range of human adenocarcinomas. The induced modification of protein function after changed glycosylation is unknown, and as a part in characterizing the glycoproteins carrying the specific carbohydrates, we analyzed the major HPA binding proteins in sera from healthy women, women with primary breast cancer with no metastasis (bcmet-), and women with metastasizing breast cancer (bcmet+) using lectin affinity chromatography and lectin blotting. The binding ligands were further identified using mass spectrometry (MALDI-TOF MS) to confirm the captured glycoproteins. The major HPA binding proteins in serum were found to be IgA1, complement factor C3, von Willebrand factor (vWF), alpha-2-macroglobulin and IgM. This set of antigens is a panel of candidates for useful HPA related biomarkers in sera, but our results also emphasize the fact that the blood group phenotypes are of most importance when using the lectin HPA in recognition of cancer biomarkers in sera and plasma. The results emphasize that interpretation of an individual change in the glycosylation pattern of a specific tumor marker always needs to be analyzed in its right context. This study shows that the blood group phenotypes can have a major impact on the results when analyzing HPA lectin binding.},
  author       = {Welinder, Charlotte and Jansson, Bo and Fernö, Mårten and Olsson, Håkan and Baldetorp, Bo},
  issn         = {1535-3893},
  keyword      = {blood,group,serum,breast cancer,GaINAc glycoproteins,Helix pomatia lectin,HPA},
  language     = {eng},
  number       = {2},
  pages        = {782--786},
  publisher    = {The American Chemical Society},
  series       = {Journal of Proteome Research},
  title        = {Expression of Helix pomatia Lectin Binding Glycoproteins in Women with Breast Cancer in Relationship to Their Mood Group Phenotypes},
  url          = {http://dx.doi.org/10.1021/pr800444b},
  volume       = {8},
  year         = {2009},
}