Journal
GLYCOBIOLOGY
Volume 23, Issue 11, Pages 1240-1249Publisher
OXFORD UNIV PRESS INC
DOI: 10.1093/glycob/cwt060
Keywords
breast cancer; glycoproteins; glycosylation sites; mass spectrometry; proteomics
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Funding
- National Institutes of Health [P20MD000544, R15CA164929]
- National Science Foundation [CHE-0619163]
- Division Of Chemistry
- Direct For Mathematical & Physical Scien [1228656] Funding Source: National Science Foundation
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Breast cancer cell lines express fewer transmembrane and secreted glycoproteins than nonmalignant ones. The objective of these experiments was to characterize the changes in the expression of several hundred glycoproteins quantitatively. Secreted and cell-surface glycoproteins were isolated using a glycoprotein capture protocol and then identified by tandem mass spectrometry. Glycoproteins expressed by a group of cell lines originating from malignant tumors of the breast were compared with those expressed by a nonmalignant set. The average number of spectral counts (proportional to relative protein abundance) and the total number of glycopeptides in the malignant samples were reduced to about two-thirds of the level in the nonmalignant samples. Most glycoproteins were expressed at a different level in the malignant samples, with nearly as many increasing as decreasing. The glycoproteins with reduced expression accounted for a larger change in spectral counts, and hence for the net loss of spectral counts in the malignant lines. Similar results were found when the glycoproteins were studied via identified glycosylation sites only, or through identified sites together with non-glycopeptides. The overall reduction is largely due to the loss of integrins, laminins and other proteins that form or interact with the basement membrane.
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