Glycosylation as a regulator of site-specific metastasis.
Bone metastasis
Brain metastasis
Glycosyltransferase
Lung metastasis
Lymph node metastasis
Organotropism
Sialylation
Journal
Cancer metastasis reviews
ISSN: 1573-7233
Titre abrégé: Cancer Metastasis Rev
Pays: Netherlands
ID NLM: 8605731
Informations de publication
Date de publication:
03 2022
03 2022
Historique:
received:
13
09
2021
accepted:
20
12
2021
pubmed:
31
12
2021
medline:
3
5
2022
entrez:
30
12
2021
Statut:
ppublish
Résumé
Metastasis is considered to be responsible for 90% of cancer-related deaths. Although it is clinically evident that metastatic patterns vary by primary tumor type, the molecular mechanisms underlying the site-specific nature of metastasis are an area of active investigation. One mechanism that has emerged as an important player in this process is glycosylation, or the addition of sugar moieties onto protein and lipid substrates. Glycosylation is the most common post-translational modification, occurring on more than 50% of translated proteins. Many of those proteins are either secreted or expressed on the cell membrane, thereby making glycosylation an important mediator of cell-cell interactions, including tumor-microenvironment interactions. It has been recently discovered that alteration of glycosylation patterns influences cancer metastasis, both globally and in a site-specific manner. This review will summarize the current knowledge regarding the role of glycosylation in the tropism of cancer cells for several common metastatic sites, including the bone, lung, brain, and lymph nodes.
Identifiants
pubmed: 34967926
doi: 10.1007/s10555-021-10015-1
pii: 10.1007/s10555-021-10015-1
pmc: PMC8930623
mid: NIHMS1768251
doi:
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
107-129Subventions
Organisme : NCI NIH HHS
ID : F31 CA265070
Pays : United States
Organisme : NCI NIH HHS
ID : T32 CA009592
Pays : United States
Informations de copyright
© 2021. The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature.
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