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A role of fukutin, a gene responsible for Fukuyama type congenital muscular dystrophy, in cancer cells: a possible role to suppress cell proliferation
Author(s) -
Yamamoto Tomoko,
Kato Yoichiro,
Shibata Noriyuki,
Sawada Tatsuo,
Osawa Makiko,
Kobayashi Makio
Publication year - 2008
Publication title -
international journal of experimental pathology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.671
H-Index - 72
eISSN - 1365-2613
pISSN - 0959-9673
DOI - 10.1111/j.1365-2613.2008.00599.x
Subject(s) - microbiology and biotechnology , biology , golgi apparatus , dystroglycan , endoplasmic reticulum , cancer research , laminin , extracellular matrix
Summary Fukutin, a gene responsible for Fukuyama type congenital muscular dystrophy (FCMD), is presumably related to the glycosylation of α‐dystroglycan (α‐DG), involved in basement membrane formation. Hypoglycosylation of α‐DG plays a key role for the pathogenesis of FCMD. On the other hand, fukutin and α‐DG are also expressed in various non‐neuromuscular tissues. Recently, a role of α‐DG as a cancer suppressor has been proposed, because of a decrease of glycosylated α‐DG in cancers. In this study, function of fukutin was investigated in two cancer cell lines, focusing on whether fukutin is involved in the glycosylation of α‐DG in cancer cells and has any possible roles related to a cancer suppressor. Localization of fukutin and a result of laminin‐binding assay after RNA interference suggest that fukutin may be involved in the glycosylation of α‐DG in a small portion in these cancer cell lines. In Western blotting and immuno‐electron microscopy, localization of fukutin in the nucleus was suggested in addition to the Golgi apparatus and/or endoplasmic reticulum. Immunohistochemically, there were more Ki‐67‐positive cells and more nuclear staining of phosphorylated c‐jun after knockdown of fukutin in two cell lines. Fukutin appears to suppress cell proliferation through a system involving c‐jun, although it is unclear this process is related to α‐DG or not at present. The result may propose a possibility of another function of fukutin in addition to the glycosylation of α‐DG in cancer cells.