title: Pathobiological implications of mucin glycans in cancer: Sweet poison and novel targets.
abstract: Mucins 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.
authors: Department of Biochemistry and Molecular Biology, University of Nebraska Medical Center, Omaha, NE 68198-5870, USA.
authors: Seema
authors: S
authors: Chugh
authors: Department of Biochemistry and Molecular Biology, University of Nebraska Medical Center, Omaha, NE 68198-5870, USA.
authors: Vinayaga S
authors: VS
authors: Gnanapragassam
authors: Department of Biochemistry and Molecular Biology, University of Nebraska Medical Center, Omaha, NE 68198-5870, USA; Fred and Pamela Buffett Cancer Center, Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, Omaha, NE 68198-5870, USA.
authors: Maneesh
authors: M
authors: Jain
authors: Department of Biochemistry and Molecular Biology, University of Nebraska Medical Center, Omaha, NE 68198-5870, USA.
authors: Satyanarayana
authors: S
authors: Rachagani
authors: Department of Biochemistry and Molecular Biology, University of Nebraska Medical Center, Omaha, NE 68198-5870, USA; Fred and Pamela Buffett Cancer Center, Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, Omaha, NE 68198-5870, USA.
authors: Moorthy P
authors: MP
authors: Ponnusamy
authors: Department of Biochemistry and Molecular Biology, University of Nebraska Medical Center, Omaha, NE 68198-5870, USA; Fred and Pamela Buffett Cancer Center, Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, Omaha, NE 68198-5870, USA; Department of Pathology and Microbiology, University of Nebraska Medical Center, Omaha, NE 68198-5870, USA. Electronic address: sbatra@unmc.edu.
authors: Surinder K
authors: SK
authors: Batra
mesh_terms: D000818:Animals; D014408:Biomarkers, Tumor / Q000378:metabolism*; D006801:Humans; D008954:Models, Biological; D025202:Molecular Diagnostic Techniques / Q000379:methods*; D058990:Molecular Targeted Therapy / Q000379:methods*; D009077:Mucins / Q000378:metabolism*; D009369:Neoplasms / Q000175:diagnosis / Q000378:metabolism* / Q000628:therapy*; D011134:Polysaccharides / Q000378:metabolism
chemical_list: D014408:Biomarkers, Tumor; D009077:Mucins; D011134:Polysaccharides
keywords: Cancer; Carbohydrate antigen; Glycan; Glycosyltransferase; Mucin; O-glycosylation