نتایج جستجو برای: پروتئین glut4

تعداد نتایج: 20721  

Journal: :Brazilian journal of medical and biological research = Revista brasileira de pesquisas medicas e biologicas 2001
P M Seraphim M T Nunes U F Machado

GLUT4 protein expression in white adipose tissue (WAT) and skeletal muscle (SM) was investigated in 2-month-old, 12-month-old spontaneously obese or 12-month-old calorie-restricted lean Wistar rats, by considering different parameters of analysis, such as tissue and body weight, and total protein yield of the tissue. In WAT, an approximately 70% decrease was observed in plasma membrane and micr...

2013
Haijia Yu Shailendra S. Rathore Eric M. Davis Yan Ouyang Jingshi Shen

The glucose transporter GLUT4 plays a central role in maintaining body glucose homeostasis. On insulin stimulation, GLUT4-containing vesicles fuse with the plasma membrane, relocating GLUT4 from intracellular reservoirs to the cell surface to uptake excess blood glucose. The GLUT4 vesicle fusion reaction requires soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) as...

Journal: :European journal of endocrinology 1997
A Shimaya O Noshiro R Hirayama T Yoneta K Niigata H Shikama

Genetically obese Zucker rats exhibit mild hyperglycaemia and hyperinsulinaemia suggesting the existence of peripheral insulin resistance. We have examined the effects of YM268, an analogue of thiazolidinedione, on the content and translocation of a glucose transporter (GLUT4) in epididymal adipose tissue in 11-week-old obese and lean Zucker rats. The administration of YM268 at a dose of 10 mg/...

Journal: :Methods in enzymology 2012
Maleppillil Vavachan Vijayakumar Manoj Kumar Bhat

Insulin-stimulated glucose transporter 4 (GLUT4) translocation promoting glucose uptake is vital to glucose homeostasis and is a defined target of antidiabetic drug research. Existing functional assays to detect the process of GLUT4 translocation are hampered due to assay variability and low sensitivity, thus slowing down the progress towards the development of preferred alternative to insulin....

Journal: :The Journal of biological chemistry 2005
Mark Larance Georg Ramm Jacqueline Stöckli Ellen M van Dam Stephanie Winata Valerie Wasinger Fiona Simpson Michael Graham Jagath R Junutula Michael Guilhaus David E James

Insulin stimulates the translocation of the glucose transporter GLUT4 from intracellular vesicles to the plasma membrane. In the present study we have conducted a comprehensive proteomic analysis of affinity-purified GLUT4 vesicles from 3T3-L1 adipocytes to discover potential regulators of GLUT4 trafficking. In addition to previously identified components of GLUT4 storage vesicles including the...

2015
Hongxia Ren Taylor Y. Lu Timothy E. McGraw Domenico Accili

The central nervous system (CNS) uses glucose independent of insulin. Nonetheless, insulin receptors and insulin-responsive glucose transporters (Glut4) often colocalize in neurons (Glut4 neurons) in anatomically and functionally distinct areas of the CNS. The apparent heterogeneity of Glut4 neurons has thus far thwarted attempts to understand their function. To answer this question, we used Cr...

2013
Yu Chen Jennifer Lippincott-Schwartz

The glucose transporter, GLUT4, redistributes to the plasma membrane (PM) upon insulin stimulation, but also recycles through endosomal compartments. Different Rab proteins control these transport itineraries of GLUT4. However, the specific roles played by different Rab proteins in GLUT4 trafficking has been difficult to assess, primarily due to the complexity of endomembrane organization and t...

Journal: :American journal of physiology. Endocrinology and metabolism 2002
Maria G Buse Katherine A Robinson Bess A Marshall Richard C Hresko Mike M Mueckler

O-linked glycosylation on Ser/Thr with single N-acetylglucosamine (O-GlcNAcylation) is a reversible modification of many cytosolic/nuclear proteins, regulated in part by UDP-GlcNAc levels. Transgenic (T) mice that overexpress GLUT1 in muscle show increased basal muscle glucose transport that is resistant to insulin stimulation. Muscle UDP-GlcNAc levels are increased. To assess whether GLUT4 is ...

Journal: :Journal of cell science 1996
E Ralston T Ploug

There is little consensus on the nature of the storage compartment of the glucose transporter GLUT4, in non-stimulated cells of muscle and fat. More specifically, it is not known whether GLUT4 is localized to unique, specialized intracellular storage vesicles, or to vesicles that are part of the constitutive endosomal-lysosomal pathway. To address this question, we have investigated the localiz...

Journal: :Journal of Cell Science 2011

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