Format:
Online-Ressource
ISSN:
1615-9861
Content:
Glycosylation of proteins is one of the most important PTMs, with more than half of all human proteins estimated to be glycosylated. It is widely known that aberrant glycosylation has been implicated in many different diseases due to changes associated with biological function and protein folding. In cancer, there is increasing evidence pertaining to the role of glycosylation in tumour formation and metastasis. Alterations in cell surface glycosylation, particularly terminal motifs, can promote invasive behaviour of tumour cells that ultimately lead to the progression of cancer. While a majority of studies have investigated protein glycosylation changes in cancer cell lines and tumour tissue for individual cancers, the review presented here represents a comprehensive, in‐depth overview of literature on the structural changes of glycosylation and their associated synthetic enzymes in five different cancer types originating from the breast, colon, liver, skin and ovary. More importantly, this review focuses on key similarities and differences between these cancers that reflect the importance of structural changes of cell surface N‐ and O‐glycans, such as sialylation, fucosylation, degree of branching and the expression of specific glycosyltransferases for each cancer. It is envisioned that the understanding of these biologically relevant glycan alterations on cellular proteins will facilitate the discovery of novel glycan‐based biomarkers which could potentially serve as diagnostic and prognostic indicators of cancer.
In:
volume:14
In:
number:4-5
In:
year:2014
In:
pages:525-546
In:
extent:22
In:
Proteomics, Weinheim : Wiley VCH, [2001]-, 14, Heft 4-5 (2014), 525-546 (gesamt 22), 1615-9861
Language:
English
DOI:
10.1002/pmic.201300387
URN:
urn:nbn:de:101:1-2023011605582362415805
URL:
https://doi.org/10.1002/pmic.201300387
URL:
https://nbn-resolving.org/urn:nbn:de:101:1-2023011605582362415805
URL:
https://d-nb.info/1278255222/34
URL:
https://doi.org/10.1002/pmic.201300387
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