TY - JOUR
T1 - Pathobiological implications of mucin glycans in cancer
T2 - Sweet poison and novel targets
AU - Chugh, Seema
AU - Gnanapragassam, Vinayaga S.
AU - Jain, Maneesh
AU - Rachagani, Satyanarayana
AU - Ponnusamy, Moorthy P.
AU - Batra, Surinder K.
N1 - Publisher Copyright:
© 2015 Elsevier B.V.
PY - 2015/12/1
Y1 - 2015/12/1
N2 - 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.
AB - 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.
KW - Cancer
KW - Carbohydrate antigen
KW - Glycan
KW - Glycosyltransferase
KW - Mucin
KW - O-glycosylation
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U2 - 10.1016/j.bbcan.2015.08.003
DO - 10.1016/j.bbcan.2015.08.003
M3 - Review article
C2 - 26318196
AN - SCOPUS:84941285571
SN - 0304-419X
VL - 1856
SP - 211
EP - 225
JO - Biochimica et Biophysica Acta - Reviews on Cancer
JF - Biochimica et Biophysica Acta - Reviews on Cancer
IS - 2
ER -