Zobrazeno 1 - 10
of 78
pro vyhledávání: '"Otto Fröhlich"'
Publikováno v:
The FASEB Journal. 27:4100-4107
The UT-A1 urea transporter plays an important role in the urinary concentration mechanism. However, the molecular mechanisms regarding UT-A1 trafficking, endocytosis, and degradation are still unclear. In this study, we identified the small GTPase Ra
Publikováno v:
American Journal of Physiology-Cell Physiology. 302:C1012-C1018
The cytoskeleton participates in many aspects of transporter protein regulation. In this study, by using yeast two-hybrid screening, we identified the cytoskeletal protein actin as a binding partner with the UT-A1 urea transporter. This suggests that
Publikováno v:
The FASEB Journal. 25:4531-4539
The UT-A1 urea transporter is a glycoprotein with two different glycosylated forms of 97 and 117 kDa. In this study, we found the 117-kDa UT-A1 preferentially resides in lipid rafts, suggesting that the glycosylation status may interfere with UT-A1 l
Autor:
Hui Cai, Guangping Chen, Haidong Huang, Jieqiu Zhuang, Xiuyan Feng, Jeff M. Sands, Janet D. Klein, Otto Fröhlich
Publikováno v:
American Journal of Physiology-Renal Physiology. 299:F1389-F1395
Dynamin is a large GTPase involved in several distinct modes of cell endocytosis. In this study, we examined the possible role of dynamin in UT-A1 internalization. The direct relationship of UT-A1 and dynamin was identified by coimmunoprecipitation.
Autor:
Rickta Mallick, Jeff M. Sands, Thomas Weimbs, Janet D. Klein, Abinash C. Mistry, Otto Fröhlich
Publikováno v:
American Journal of Physiology-Renal Physiology. 297:F292-F300
Proper targeting of the aquaporin-2 (AQP2) water channel to the collecting duct apical plasma membrane is critical for the urine concentrating mechanism and body water homeostasis. However, the trafficking mechanisms that recruit AQP2 to the plasma m
Publikováno v:
American Journal of Physiology-Cell Physiology. 286:C1264-C1270
Progress in understanding the cell biology of urea transporter proteins has been hampered by the lack of an appropriate cell culture system. The goal of this study was to create a polarized epithelial cell line that stably expresses the largest of th
Publikováno v:
Biology of Reproduction. 69:294-300
The expression pattern of EP2 variants was examined in the rhesus monkey (Macaca mulatta). Using reverse transcriptase-polymerase chain reaction and rapid amplification of complementary cDNA protocols, 11 message variants were identified in rhesus ep
Publikováno v:
Biology of Reproduction. 65:575-580
In primates, expression of the EP2 gene is androgen-dependent and epididymis-specific. EP2 mRNA expression was investigated in caput, corpus, and cauda regions of rat epididymis and in 15 other rat tissues. Polymerase chain reaction and Northern anal
Publikováno v:
Biology of Reproduction. 64:1072-1079
The EP2 gene codes for at least nine message variants that are all specifically expressed in the epididymis. These variants putatively encode small secretory proteins that differ in their Nand C-termini, resulting in proteins that can have little or