Zobrazeno 1 - 10
of 58
pro vyhledávání: '"C. Randell Brown"'
Publikováno v:
Alcoholism, clinical and experimental research. 41(5)
Background Excessive alcohol (EtOH) consumption causes an imbalance in protein metabolism. EtOH impairs protein synthesis in C2C12 myoblasts via a FoxO1-AMPK-TSC2-mTORC1 pathway and also induces protein degradation. As the underlying regulatory signa
Publikováno v:
American Journal of Physiology-Cell Physiology. 302:C1557-C1565
Leucine (Leu) and insulin both stimulate muscle protein synthesis, albeit at least in part via separate signaling pathways. While alcohol (EtOH) suppresses insulin-stimulated protein synthesis in cultured myocytes, its ability to disrupt Leu signalin
Publikováno v:
Journal of Biological Chemistry. 285:1516-1528
When glucose is added to yeast cells that are starved for 3 days, fructose-1,6-bisphosphatase (FBPase) and malate dehydrogenase 2 are degraded in the vacuole via the vacuole import and degradation (Vid) pathway. In this study, we examined the distrib
Autor:
Hui Ling Chiang, C. Randell Brown
Publikováno v:
Communicative & Integrative Biology. 2:177-183
In Saccharomyces cerevisiae, glucose starvation induces key gluconeogenic enzymes such as fructose-1,6-bisphosphatase (FBPase), malate dehydrogenase (MDH2) and phosphoenolpyruvate carboxykinase, while glucose addition inactivates these enzymes. Signi
Publikováno v:
Journal of Biological Chemistry. 282:3702-3712
Ethanol decreases protein synthesis in cells, although the underlying regulatory mechanisms of this process are not fully established. In the present study incubation of C2C12 myocytes with 100 mm EtOH decreased protein synthesis while markedly incre
Publikováno v:
Alcoholism: Clinical and Experimental Research. 30:1297-1307
Background: Alcohol and the antiretroviral drug indinavir (Ind) decrease protein synthesis in skeletal muscle under in vivo and in vitro conditions. The goal of the present study was to identify signaling mechanisms responsible for the inhibitory eff
Publikováno v:
Autophagy. 1:146-156
The key gluconeogenic enzyme fructose-1,6-bisphosphatase (FBPase) is induced during glucose starvation. After the addition of glucose, inactivated FBPase is selectively targeted to Vid (vacuolar import and degradation) vesicles and then to the vacuol
Publikováno v:
Journal of Biological Chemistry. 279:49138-49150
The key gluconeogenic enzyme fructose-1,6-bisphosphatase (FBPase) is subjected to catabolite inactivation and degradation when glucose-starved cells are replenished with fresh glucose. In various studies, the proteasome and the vacuole have each been
Publikováno v:
American Journal of Physiology-Cell Physiology. 287:C1482-C1492
Anti-retroviral therapy promotes clinical, immunologic, and virologic improvement in human immunodeficiency virus-infected patients. Whereas this therapy adversely affects carbohydrate and lipid metabolism, the effects of anti-retroviral drugs on mus
Autor:
Christopher P. Elco, Hui Ling Chiang, C. Randell Brown, Graham Guo Chiuan Hung, Jameson A. McCann
Publikováno v:
Journal of Cell Science. 115:655-666
Fructose-1,6-bisphosphatase (FBPase), an important enzyme in the gluconeogenic pathway in Saccharomyces cerevisiae , is expressed when cells are grown in media containing a poor carbon source. Following glucose replenishment, FBPase is targeted from