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FASEB J. 2014 Oct;28(10):4183-99. doi: 10.1096/fj.14-257352. Epub 2014 Jul 2.

MUC16: molecular analysis and its functional implications in benign and malignant conditions.

Author information

1
Department of Biochemistry and Molecular Biology.
2
Department of Biochemistry and Molecular Biology, Fred and Pamela Buffett Cancer Center, Eppley Institute for Research in Cancer and Allied Diseases, and Department of Pathology and Microbiology, University of Nebraska Medical Center, Omaha, Nebraska, USA sbatra@unmc.edu.

Abstract

MUC16 is a high-molecular-weight glycoprotein that is expressed by the various epithelial cell surfaces of the human body to protect the cell layer from a myriad of insults. It is the largest mucin known to date, with an ∼22,152 aa sequence. Structurally, MUC16 is characterized into 3 distinct domains: the amino terminal, the tandem repeat, and the carboxyl terminal domain, with each domain having unique attributes. The extracellular portion of MUC16 is shed into the bloodstream and serves as a biomarker for diagnosing and monitoring patients with cancer; however, its functional role in cancer is yet to be elucidated. Several factors contribute to this challenge, which include the large protein size; the extensive glycosylation that the protein undergoes, which confers functional heterogeneity; lack of specific antibodies that detect the unique domains of MUC16; and the existence of splicing variants. Despite these limitations, MUC16 has been established as a molecule of significant application in cancer. Hence, in this review, we discuss the various aspects of MUC16, which include its discovery, structure, and biological significance both in benign and malignant conditions with an attempt to dissect its functional relevance.

KEYWORDS:

MUC16; animal model; cancer; domain structure

PMID:
25002120
DOI:
10.1096/fj.14-257352
[Indexed for MEDLINE]

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