Reflections on MUC 1 glycoprotein: the hidden potential of isoforms in carcinogenesis
Mucin 1 ( MUC 1) has been described as the renaissance molecule due to the large set of functions it displays in both normal and neoplastic cells. This membrane‐tethered glycoprotein is overexpressed and aberrantly glycosylated in most epithelial cancers, being involved in several processes related...
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| Veröffentlicht in: | APMIS : acta pathologica, microbiologica et immunologica Scandinavica microbiologica et immunologica Scandinavica, 2016-11, Vol.124 (11), p.913-924 |
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| container_title | APMIS : acta pathologica, microbiologica et immunologica Scandinavica |
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| creator | Sousa, Andreia M. Grandgenett, Paul M. David, Leonor Almeida, Raquel Hollingsworth, Michael Anthony Santos‐Silva, Filipe |
| description | Mucin 1 (
MUC
1) has been described as the renaissance molecule due to the large set of functions it displays in both normal and neoplastic cells. This membrane‐tethered glycoprotein is overexpressed and aberrantly glycosylated in most epithelial cancers, being involved in several processes related with malignant phenotype acquisition. With a highly polymorphic structure, both in the polypeptide and glycan counterparts,
MUC
1 variability has been associated with susceptibility to several diseases, including cancer. Biochemical features and biological functions have been characterized upon the full‐length
MUC
1 protein, remaining to clarify the real impact on cell dynamics of the plethora of
MUC
1 isoforms. This review aims to encompass a detailed characterization of
MUC
1 role in carcinogenesis, highlighting recent findings in cell differentiation and uncovering new evidences of
MUC
1 isoforms involvement in malignant phenotype. |
| doi_str_mv | 10.1111/apm.12587 |
| format | Article |
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MUC
1) has been described as the renaissance molecule due to the large set of functions it displays in both normal and neoplastic cells. This membrane‐tethered glycoprotein is overexpressed and aberrantly glycosylated in most epithelial cancers, being involved in several processes related with malignant phenotype acquisition. With a highly polymorphic structure, both in the polypeptide and glycan counterparts,
MUC
1 variability has been associated with susceptibility to several diseases, including cancer. Biochemical features and biological functions have been characterized upon the full‐length
MUC
1 protein, remaining to clarify the real impact on cell dynamics of the plethora of
MUC
1 isoforms. This review aims to encompass a detailed characterization of
MUC
1 role in carcinogenesis, highlighting recent findings in cell differentiation and uncovering new evidences of
MUC
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MUC
1) has been described as the renaissance molecule due to the large set of functions it displays in both normal and neoplastic cells. This membrane‐tethered glycoprotein is overexpressed and aberrantly glycosylated in most epithelial cancers, being involved in several processes related with malignant phenotype acquisition. With a highly polymorphic structure, both in the polypeptide and glycan counterparts,
MUC
1 variability has been associated with susceptibility to several diseases, including cancer. Biochemical features and biological functions have been characterized upon the full‐length
MUC
1 protein, remaining to clarify the real impact on cell dynamics of the plethora of
MUC
1 isoforms. This review aims to encompass a detailed characterization of
MUC
1 role in carcinogenesis, highlighting recent findings in cell differentiation and uncovering new evidences of
MUC
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MUC
1) has been described as the renaissance molecule due to the large set of functions it displays in both normal and neoplastic cells. This membrane‐tethered glycoprotein is overexpressed and aberrantly glycosylated in most epithelial cancers, being involved in several processes related with malignant phenotype acquisition. With a highly polymorphic structure, both in the polypeptide and glycan counterparts,
MUC
1 variability has been associated with susceptibility to several diseases, including cancer. Biochemical features and biological functions have been characterized upon the full‐length
MUC
1 protein, remaining to clarify the real impact on cell dynamics of the plethora of
MUC
1 isoforms. This review aims to encompass a detailed characterization of
MUC
1 role in carcinogenesis, highlighting recent findings in cell differentiation and uncovering new evidences of
MUC
1 isoforms involvement in malignant phenotype.</abstract><doi>10.1111/apm.12587</doi><tpages>12</tpages></addata></record> |
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| ispartof | APMIS : acta pathologica, microbiologica et immunologica Scandinavica, 2016-11, Vol.124 (11), p.913-924 |
| issn | 0903-4641 1600-0463 |
| language | eng |
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| source | Access via Wiley Online Library |
| title | Reflections on MUC 1 glycoprotein: the hidden potential of isoforms in carcinogenesis |
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