4.6 Review

Pathobiological implications of mucin glycans in cancer: Sweet poison and novel targets

Journal

BIOCHIMICA ET BIOPHYSICA ACTA-REVIEWS ON CANCER
Volume 1856, Issue 2, Pages 211-225

Publisher

ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbcan.2015.08.003

Keywords

Mucin; Glycan; Cancer; O-glycosylation; Carbohydrate antigen; Glycosyltransferase

Funding

  1. National Institutes of Health [UO1 CA111294, P50 CA127297, U54 CA163120, RO1 CA183459, RO1 CA195586, K22 CA175260, P20 GM103480]

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Macins are large glycoproteins expressed on the epithelia that provide a protective barrier against harsh insults from toxins and pathogenic microbes. These glycoproteins are classified primarily as being secreted and membrane-bound; both forms are involved in pathophysiological functions including inflammation and cancer. The high molecular weight of mucins is attributed to their large polypeptide backbone that is extensively covered by glycan moieties that modulate the function of mucins and, hence, play an important role in physiological functions. Deregulation of glycosylation machinery during malignant transformation results in altered mucin glycosylation. This review describes the functional implications and pathobiological significance of altered mucin glycosylation in cancer. Further, this review delineates various factors such as glycosyltransferases and tumor microenvironment that contribute to dysregulation of mucin glycosylation during cancer. Finally, this review discusses the scope of mucin glycan epitopes as potential diagnostic and therapeutic targets. (C) 2015 Elsevier B.V. All rights reserved.

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