Journal
ANNUAL REVIEW OF PATHOLOGY: MECHANISMS OF DISEASE, VOL 10
Volume 10, Issue -, Pages 473-510Publisher
ANNUAL REVIEWS
DOI: 10.1146/annurev-pathol-012414-040438
Keywords
glycoprotein; glycosylation; glycans; oligosaccharides; cancer; transformation; biomarkers; immunohistochemistry
Categories
Funding
- NATIONAL CANCER INSTITUTE [U01CA168930] Funding Source: NIH RePORTER
- NATIONAL HEART, LUNG, AND BLOOD INSTITUTE [P01HL085607] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R24GM098791, P41GM103694] Funding Source: NIH RePORTER
- OFFICE OF THE DIRECTOR, NATIONAL INSTITUTES OF HEALTH [DP5OD019892] Funding Source: NIH RePORTER
- NCI NIH HHS [U01 CA168930, U01CA168930] Funding Source: Medline
- NHLBI NIH HHS [P01HL085607, P01 HL085607] Funding Source: Medline
- NIGMS NIH HHS [P41GM103694, R24 GM098791, R24GM 098791, P41 GM103694] Funding Source: Medline
- NIH HHS [DP5OD019892, DP5 OD019892] Funding Source: Medline
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Neoplastic transformation results in a wide variety of cellular alterations that impact the growth, survival, and general behavior of affected tissue. Although genetic alterations underpin the development of neoplastic disease, epigenetic changes can exert an equally significant effect on neoplastic transformation. Among neoplasia-associated epigenetic alterations, changes in cellular glycosylation have recently received attention as a key component of neoplastic progression. Alterations in glycosylation appear to not only directly impact cell growth and survival but also facilitate tumor-induced immunomodulation and eventual metastasis. Many of these changes may support neoplastic progression, and unique alterations in tumor-associated glycosylation may also serve as a distinct feature of cancer cells and therefore provide novel diagnostic and even therapeutic targets.
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