Organization of the gene for gelatin-binding protein (GBP28)

Saito, Kiyomi; Tobe, Takashi; Minoshima, Shinsei; Asakawa, Shuichi; Sumiya, Jun-ichi; Yoda, Madoka; Nakano, Yasuko; Shimizu, Nobuyoshi; Tomita, Motowo

doi:10.1016/s0378-1119(99)00041-4

Cited by 121 publications

(72 citation statements)

References 33 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Recently we determined the organization of the GBP28 gene, and to analyze the promoter region, we sequenced about 600 nucleotides in the 9 kb fragment of the 5 H¯a nking region. 18 Schaf¯er et al also recently reported the human adipocyte apM1 promoter. 19 In the promoter of GBP28 gene, no TATA box, but a classical CCAAT box, was identi®ed, which is associated with constitutively active housekeeping genes.…”

Section: Characterization Of Mouse Gbp28mentioning

confidence: 93%

Characterization of mouse GBP28 and its induction by exposure to cold

et al. 2001

View full text Add to dashboard Cite

OBJECTIVE:To investigate whether the expression of the novel adipose tissue-speci®c protein GBP28 in adipose tissue and serum are altered in mice under a variety of conditions. DESIGN: Mice were fed a high-fat diet for 4 weeks, fasted for 48 h or exposed at 4 C. SUBJECTS: C57BLa6J mouse, male, 4 ± 6 weeks old. MEASUREMENTS: GBP28 mRNA, GBP28 protein, blood glucose, insulin and fad pad weight of the mice. RESULTS: We ®rst con®rmed that the mouse has GBP28 and its characteristics are the same as human GBP28. Serum concentration and mRNA levels of GBP28 signi®cantly increased in the mice exposed to cold. CONCLUSION: GBP28 may play a role in homeostasis, regulating body temperature and basal metabolic rate in response to changing environmental conditions.

show abstract

Section: Characterization Of Mouse Gbp28mentioning

confidence: 93%

Characterization of mouse GBP28 and its induction by exposure to cold

et al. 2001

View full text Add to dashboard Cite

show abstract

“…We have also shown, in cultured mouse adipocytes, that rosiglitazone increased the steady-state mRNA of adiponectin (16). The proximal promoter region (1 kb) of the human adiponectin gene contains only a half-site of PPAR-␥ response element (AGGTCA between -610 and -605 relative to ATG start codon) (22,23). Its proximal promoter also contains several regulatory elements commonly observed in the promoters of genes expressed in adipose tissue.…”

Section: Statistical Analysesmentioning

confidence: 99%

Synthetic Peroxisome Proliferator-Activated Receptor-γ Agonist, Rosiglitazone, Increases Plasma Levels of Adiponectin in Type 2 Diabetic Patients

et al. 2002

View full text Add to dashboard Cite

OBJECTIVE—Adiponectin, a plasma protein exclusively synthesized and secreted by adipose tissue, has recently been shown to have anti-inflammatory, antiatherogenic properties in vitro and beneficial metabolic effects in animals. Lower plasma levels of adiponectin have been documented in human subjects with metabolic syndrome and coronary artery disease. We investigated whether the level of this putative protective adipocytokine could be increased by treatment with a peroxisome proliferator-activated receptor-γ (PPAR-γ) agonist in diabetic patients. RESEARCH DESIGN AND METHODS—Type 2 diabetic patients (30 in the treatment group and 34 in the placebo group) were recruited for a randomized double-blind placebo-controlled trial for 6 months with the PPAR-γ agonist rosiglitazone. Blood samples were collected and metabolic variables and adiponectin levels were determined in all patients before initiation of the study. RESULTS—In the rosiglitazone group, mean plasma adiponectin level was increased by more than twofold (P < 0.0005), whereas no change was observed in the placebo group. Multivariate linear regression analysis showed that whether rosiglitazone was used was the single variable significantly related to the changes of plasma adiponectin. The amount of variance in changes of plasma adiponectin level explained by the treatment was ∼24% (r2 = 0.24) after adjusting for age, sex, and changes in fasting plasma glucose, HbA1c, insulin resistance index, and BMI. CONCLUSIONS—Rosiglitazone increases plasma adiponectin levels in type 2 diabetic subjects. Whether this may contribute to the antihyperglycemic and putative antiatherogenic benefits of PPAR-γ agonists in type 2 diabetic patients warrants further investigation.

show abstract

Section: )mentioning

confidence: 99%

“…15) These two genes, which are composed of three exons and have a long first intron, are expressed specifically in adipose tissue. 15) Adiponectin and leptin control fuel homeostasis, body weight, and insulin sensitivity. In another recent study, amelioration of insulin resistance, pancreatic β-cell degranulation, and diabetes after crossing leptin-deficient mice with globular domain adiponectin trans-Vol 47 No 1 genic mice has been described, indicating that globular adiponectin and leptin may have overlapping functions.…”

Section: )mentioning

confidence: 99%

Impaired Expression of Cardiac Adiponectin in Leptin-Deficient Mice With Viral Myocarditis

Takahashi

Saegusa

et al. 2006

Int. Heart J.

View full text Add to dashboard Cite

SUMMARYA mouse model of encephalomyocarditis (EMC) virus-induced myocarditis was used to investigate the expression of adiponectin in damaged cardiomyocytes. We intraperitoneally injected EMC virus into leptin-deficient ob/ob (OB) mice and wild-type (WT) mice. OB mice were divided into two subgroups consisting of mice with no intervention and mice receiving leptin replacement starting simultaneously with viral inoculation. We determined differences in heart weight, cardiac histological score, numbers of infiltrating and apoptotic cells in the myocardium, expression levels of adiponectin and TNF-α mRNA in the heart, adiponectin immunoreactivity in myocytes, adiponectin and TNF-α concentrations in the heart, and immunoreactivity of adiponectin receptors in myocytes between OB mice and WT mice. There was significantly decreased adiponectin mRNA expression, immunoreactivity, and protein level in the heart, and reduced immunoreactivity of adiponectin receptor 1 in myocytes from OB mice on days 4 and 8 after viral inoculation as compared with those in WT mice, together with increased cardiac weight, severe inflammatory myocardial damage, and increased levels of cardiac TNF-α mRNA and protein. Replacement of leptin in OB mice inhibited the development of severe myocarditis through augmentation of adiponectin mRNA, immunoreactivity, and protein level, increased adiponectin receptor 1 immunoreactivity in myocytes, and suppressed levels of TNF-α mRNA and protein. These results suggest that impaired expression of cardiac adiponectin may contribute to the progression of viral myocarditis through enhanced expression of TNF-α under a leptin-deficient condition. (Int Heart J 2006; 47: 107-123) Key words: Adiponectin, Leptin deficiency, Viral myocarditis, Cardiomyocyte HEART failure is generally considered to begin with myocyte damage caused by a variety of pathological conditions that include ischemia, toxins, and myocardial infection. The heart compensates by dilatation and cellular hypertrophy, and eventually decompensates, resulting in heart failure. A proinflammatory cytokFrom the

show abstract

Organization of the gene for gelatin-binding protein (GBP28)

Cited by 121 publications

References 33 publications

Characterization of mouse GBP28 and its induction by exposure to cold

Characterization of mouse GBP28 and its induction by exposure to cold

Synthetic Peroxisome Proliferator-Activated Receptor-γ Agonist, Rosiglitazone, Increases Plasma Levels of Adiponectin in Type 2 Diabetic Patients

Impaired Expression of Cardiac Adiponectin in Leptin-Deficient Mice With Viral Myocarditis

Contact Info

Product

Resources

About