Zobrazeno 1 - 10
of 32
pro vyhledávání: '"Lelita T. Braiterman"'
Autor:
Lelita T. Braiterman, Nesrin M. Hasan, Samuel Jayakanthan, Svetlana Lutsenko, Vinzenz M. Unger
Publikováno v:
Journal of Biological Chemistry. 292:18760-18774
ATP7B is a copper-transporting P1B-type ATPase (Cu-ATPase) with an essential role in human physiology. Mutations in ATP7B cause the potentially fatal Wilson disease, and changes in ATP7B expression are observed in several cancers. Despite its physiol
Autor:
Svetlana Lutsenko, Sergiy Nokhrin, Lelita T. Braiterman, Jameson R. Bothe, Marco Tonelli, Oleg Y. Dmitriev, Nan Yang, Corey H. Yu, Natalia V. Dolgova
Publikováno v:
Journal of Biological Chemistry. 292:18169-18177
The human transporter ATP7B delivers copper to the biosynthetic pathways and maintains copper homeostasis in the liver. Mutations in ATP7B cause the potentially fatal hepatoneurological disorder Wilson disease. The activity and intracellular localiza
Autor:
Ling Yi, Haojun Yang, Lelita T. Braiterman, Martina Ralle, Stephen G. Kaler, Michael P. Murphy, Ashima Bhattacharjee, Tony R. Capps, Ya-Wen Lu, Arianrhod Conrad-Antoville, Emily Robinson, Megan Duffy, Svetlana Lutsenko, Michael J. Wolfgang
Publikováno v:
The Journal of Biological Chemistry
Copper-transporting ATPase ATP7A is essential for mammalian copper homeostasis. Loss of ATP7A activity is associated with fatal Menkes disease and various other pathologies. In cells, ATP7A inactivation disrupts copper transport from the cytosol into
Publikováno v:
Journal of Biological Chemistry. 290:8803-8819
The Wilson disease protein ATP7B exhibits copper-dependent trafficking. In high copper, ATP7B exits the trans-Golgi network and moves to the apical domain of hepatocytes where it facilitates elimination of excess copper through the bile. Copper level
Publikováno v:
American Journal of Physiology-Gastrointestinal and Liver Physiology. 301:G69-G81
ATP7A and ATP7B are copper-transporting P-type ATPases that are essential to eukaryotic copper homeostasis and must traffic between intracellular compartments to carry out their functions. Previously, we identified a nine-amino acid sequence (F37–E
Autor:
Lelita T. Braiterman, Yan Guo, Ann L. Hubbard, Svetlana Lutsenko, Lydia K. Nyasae, Rodrigo Bustos
Publikováno v:
American Journal of Physiology-Gastrointestinal and Liver Physiology. 296:G433-G444
ATP7B is a copper-transporting P-type ATPase present predominantly in liver. In basal copper, hepatic ATP7B is in a post-trans-Golgi network (TGN) compartment where it loads cytoplasmic Cu(I) onto newly synthesized ceruloplasmin. When copper levels r
Autor:
David C. Johns, Sean Heffernan, Lydia K. Nyasae, Arun Sharma, Allison McNickle, Ann L. Hubbard, Alfred P. See, Mira Herman, Ulhas P. Naik, Lelita T. Braiterman, Rebeca Yutzy
Publikováno v:
American Journal of Physiology-Gastrointestinal and Liver Physiology. 294:G576-G588
Junctional adhesion molecule (JAM) is involved in tight junction (TJ) formation in epithelial cells. Three JAMs (A, B, and C) are expressed in rat hepatocytes, but only rat JAM-A is present in polarized WIF-B cells, a rat-human hepatic line. We used
Publikováno v:
American Journal of Physiology-Gastrointestinal and Liver Physiology. 292:G1181-G1194
We report for the first time on the copper-dependent behavior of endogenous ATP7A in two types of polarized intestinal epithelia, rat enterocytes in vivo and filter-grown Caco-2 cells, an accepted in vitro model of human small intestine. We used high
Publikováno v:
Journal of Cellular Biochemistry. 99:647-664
Scribble (Scrib) is a large multi-domain cytoplasmic protein that was first identified through its requirement for the establishment of epithelial polarity. We tested the hypotheses that Scrib asssociates with the basolateral membrane via multiple do
Publikováno v:
Cell Biochemistry and Biophysics. 32:333-337
X-linked adrenoleukodystrophy (X-ALD) is characterized biochemically by elevated levels of saturated very long-chain fatty acids (VLCFAs) in plasma and tissues. In X-ALD, peroxisomal very-long-chain acyl-CoA synthetase (VLCS) fails to activate VLCFAs