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Mucin glycoproteins in neoplasia (1996)

Kim, Young S. ; Gum, James ; Brockhausen, Inka

Springer

Glycoconjugate journal 13 (1996), S. 693-707

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ISSN: 1573-4986

Keywords: mucin glycoproteins ; mucin genes ; carbohydrate antigens ; cancer ; metastasis

Source: Springer Online Journal Archives 1860-2000

Topics: Chemistry and Pharmacology

Notes: Abstract Mucins are high molecular weight glycoproteins that are heavily glycosylated with many oligosaccharide side chains linked O-glycosidically to the protein backbone. With the recent application of molecular biological methods, the structures of apomucins and regulation of mucin genes are beginning to be understood. At least nine human mucin genes have been identified to date. Although a complete protein sequence is known for only three human mucins (MUC1, MUC2, and MUC7), common motifs have been identified in many mucins. The pattern of tissue and cell-specific expression of these mucin genes are emerging, suggesting a distinct role for each member of this diverse mucin gene family. In epithelial cancers, many of the phenotypic markers for pre-malignant and malignant cells have been found on the carbohydrate and peptide moieties of mucin glycoproteins. The expression of carbohydrate antigens appears to be due to modification of peripheral carbohydrate structures and the exposure of inner core region carbohydrates. The expression of some of the sialylated carbohydrate antigens appears to correlate with poor prognosis and increased metastatic potential in some cancers. The exposure of peptide backbone structures of mucin glycoproteins in malignancies appears to be due to abnormal glycosylation during biosynthesis. Dysregulation of tissue and cell-specific expression of mucin genes also occurs in epithelial cancers. At present, the role of mucin glycoproteins in various stages of epithelial cell carcinogenesis (including the preneoplastic state and metastasis), in cancer diagnosis and immunotherapy is under investigation.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF00702333

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Altered glycosylation of mucin glycoproteins in colonic neoplasia (1992)

Kim, Young S.

New York, N.Y. : Wiley-Blackwell

Journal of Cellular Biochemistry 50 (1992), S. 91-96

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ISSN: 0730-2312

Keywords: carbohydrate antigens ; chemoprevention ; colorectal cancer antigens ; intermediate biomarker ; mucin glycoproteins ; Life and Medical Sciences ; Cell & Developmental Biology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology , Chemistry and Pharmacology , Medicine

Notes: Considerable alteration of cellular carbohydrates such as glycolipids and glycoproteins occurs in colonic neoplasia. Some of these changes are also observed at certain embryonic stages of differentiation and are, therefore, considered onco-developmental changes. In colon cancer cells, many of the phenotypic markers for malignancy have been found on carbohydrate moieties, and some have been found on the peptide portion of mucin glycoproteins. The changes in carbohydrate antigens include altered expression of core region carbohydrates, extension of backbone structures and modification of peripheral carbohydrate structures that may arise due to abnormal glycosylation processes. Altered glycosylation may also result in the exposure of the peptide moiety of the mucin glycoprotein. Therefore, these altered mucin glycoprotein structures may serve as tumor markers. Howerver, it remains to be determined whether they will be useful as intermediate endpoint markers.

Additional Material: 1 Ill.