title: Disrupted galectin-3 causes non-alcoholic fatty liver disease in male mice.
abstract: Galectin-3, a beta-galactoside-binding animal lectin, is a multifunctional protein. Previous studies have suggested that galectin-3 may play an important role in inflammatory responses. Non-alcoholic fatty liver disease (NAFLD) is increasingly recognized as a liver condition that may progress to end-stage liver disease and based on the known functions of galectin-3, it was hypothesized that galectin-3 might play a role in the development of NAFLD. Thus, this study investigated the role of galectin-3 in NAFLD by comparing galectin-3 knockout (gal3(-/-)) mice and wild-type (gal3(+/+)) mice. The livers of gal3(-/-) male mice at 6 months of age histologically displayed mild to severe fatty change. The liver weight per body weight ratio, serum alanine aminotransferase levels, liver triglyceride levels, and liver lipid peroxide in gal3(-/-) mice were significantly increased compared with those in gal3(+/+) mice. Furthermore, the hepatic protein levels of advanced glycation end-products (AGE), receptor for AGE (RAGE), and peroxisome proliferator-activated receptor gamma (PPARgamma) were increased in gal3(-/-) mice relative to gal3(+/+) mice. In conclusion, this study suggests that the absence of gal3 can cause clinico-pathological features in male mice similar to those of NAFLD.
authors.affiliation: Department of Pathology, Faculty of Medicine, University of Toyama, Toyama, Japan.
authors.forename: K
authors.initials: K
authors.lastname: Nomoto
authors.forename: K
authors.initials: K
authors.lastname: Tsuneyama
authors.forename: H O
authors.initials: HO
authors.lastname: Abdel Aziz
authors.forename: H
authors.initials: H
authors.lastname: Takahashi
authors.forename: Y
authors.initials: Y
authors.lastname: Murai
authors.forename: Z-G
authors.initials: ZG
authors.lastname: Cui
authors.forename: M
authors.initials: M
authors.lastname: Fujimoto
authors.forename: I
authors.initials: I
authors.lastname: Kato
authors.forename: K
authors.initials: K
authors.lastname: Hiraga
authors.forename: D K
authors.initials: DK
authors.lastname: Hsu
authors.forename: F-T
authors.initials: FT
authors.lastname: Liu
authors.forename: Y
authors.initials: Y
authors.lastname: Takano
mesh_terms: D000410:Alanine Transaminase / Q000097:blood; D000818:Animals; D001835:Body Weight; D005234:Fatty Liver / Q000378:metabolism / Q000473:pathology*; D037502:Galectin 3 / Q000032:analysis / Q000172:deficiency / Q000378:metabolism*; D017127:Glycation End Products, Advanced / Q000032:analysis; D007150:Immunohistochemistry / Q000379:methods; D008099:Liver / Q000378:metabolism / Q000473:pathology; D008297:Male; D008565:Membrane Proteins / Q000032:analysis; D051379:Mice; D018345:Mice, Knockout; D009929:Organ Size; D047495:PPAR gamma / Q000032:analysis; D000070780:Perilipin-2; D012333:RNA, Messenger / Q000032:analysis; D000067759:Receptor for Advanced Glycation End Products; D011971:Receptors, Immunologic / Q000032:analysis; D051780:Sterol Regulatory Element Binding Protein 1 / Q000032:analysis
chemical_list: D037502:Galectin 3; D017127:Glycation End Products, Advanced; D008565:Membrane Proteins; D047495:PPAR gamma; D000070780:Perilipin-2; D012333:RNA, Messenger; D000067759:Receptor for Advanced Glycation End Products; D011971:Receptors, Immunologic; C497388:Srebf1 protein, mouse; D051780:Sterol Regulatory Element Binding Protein 1; D000410:Alanine Transaminase