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

The FASEB JournalVolume 28, Issue 10 p. 4183-4199 ReviewFree to Read MUC16: molecular analysis and its functional implications in benign and malignant conditions Dhanya Haridas, Dhanya Haridas Department of Biochemistry and Molecular Biology, University of Nebraska Medical Center, Omaha, Nebraska, USASearch for more papers by this authorMoorthy P. Ponnusamy, Moorthy P. Ponnusamy Department of Biochemistry and Molecular Biology, University of Nebraska Medical Center, Omaha, Nebraska, USASearch for more papers by this authorSeema Chugh, Seema Chugh Department of Biochemistry and Molecular Biology, University of Nebraska Medical Center, Omaha, Nebraska, USASearch for more papers by this authorImayavaramban Lakshmanan, Imayavaramban Lakshmanan Department of Biochemistry and Molecular Biology, University of Nebraska Medical Center, Omaha, Nebraska, USASearch for more papers by this authorParthasarathy Seshacharyulu, Parthasarathy Seshacharyulu Department of Biochemistry and Molecular Biology, University of Nebraska Medical Center, Omaha, Nebraska, USASearch for more papers by this authorSurinder K. Batra, Corresponding Author Surinder K. Batra [email protected] Department of Biochemistry and Molecular Biology, University of Nebraska Medical Center, Omaha, Nebraska, USA Fred and Pamela Buffett Cancer Center, Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, Omaha, Nebraska, USA Department of Pathology and Microbiology, University of Nebraska Medical Center, Omaha, Nebraska, USACorrespondence: Department of Biochemistry and Molecular Biology, Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, Omaha, Nebraska, 68198-5870, USA. E-mail: [email protected]Search for more papers by this author Dhanya Haridas, Dhanya Haridas Department of Biochemistry and Molecular Biology, University of Nebraska Medical Center, Omaha, Nebraska, USASearch for more papers by this authorMoorthy P. Ponnusamy, Moorthy P. Ponnusamy Department of Biochemistry and Molecular Biology, University of Nebraska Medical Center, Omaha, Nebraska, USASearch for more papers by this authorSeema Chugh, Seema Chugh Department of Biochemistry and Molecular Biology, University of Nebraska Medical Center, Omaha, Nebraska, USASearch for more papers by this authorImayavaramban Lakshmanan, Imayavaramban Lakshmanan Department of Biochemistry and Molecular Biology, University of Nebraska Medical Center, Omaha, Nebraska, USASearch for more papers by this authorParthasarathy Seshacharyulu, Parthasarathy Seshacharyulu Department of Biochemistry and Molecular Biology, University of Nebraska Medical Center, Omaha, Nebraska, USASearch for more papers by this authorSurinder K. Batra, Corresponding Author Surinder K. Batra [email protected] Department of Biochemistry and Molecular Biology, University of Nebraska Medical Center, Omaha, Nebraska, USA Fred and Pamela Buffett Cancer Center, Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, Omaha, Nebraska, USA Department of Pathology and Microbiology, University of Nebraska Medical Center, Omaha, Nebraska, USACorrespondence: Department of Biochemistry and Molecular Biology, Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, Omaha, Nebraska, 68198-5870, USA. E-mail: [email protected]Search for more papers by this author First published: 02 July 2014 https://doi.org/10.1096/fj.14-257352Citations: 6Read the full textAboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinkedInRedditWechat 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.— Haridas, D., Ponnusamy, M. P., Chugh, S., Lakshmanan, I., Seshacharyulu, P., and Batra, S. K., MUC16: molecular analysis and its functional implications in benign and malignant conditions. FASEB J. 28, 4183-4199 (2014). www.fasebj.org Citing Literature Volume28, Issue10October 2014Pages 4183-4199 RelatedInformation