15-05-2016, 11:28 PM
The research doors are open huh?, chances are you'll find more related NBE/HrT in this thread as opposed to other places, I'll be adding my other research threads into this one, it might save you some time. You should look at stat5 protein, interleukin6, histone, carrier proteins, to name a few.
(06-03-2015, 03:19 AM)Lotus Wrote: present study we show that caveolin-1 binds directly to ERalpha. This is part of the first part, which is party of the second part, (is that how it goes?) anyways, subcellular localization of COX-2 and caveolin-1 was determined.
J Biol Chem. 2001 Sep 14;276(37):34975-82. Epub 2001 Jun 29.
Colocalization and interaction of cyclooxygenase-2 with caveolin-1 in human fibroblasts.
Abstract
Results from our previous study suggest that cyclooxygenase-2 (COX-2) induced by phorbol 12-myristate 13-acetate (PMA) may be localized to caveolae-like structures (Liou, J.-Y., Shyue, S.-K., Tsai, M.-J., Chung, C.-L., Chu, K.-Y., and Wu, K. K. (2000) J. Biol. Chem. 275, 15314-15320). In this study, we determined subcellular localization of COX-2 and caveolin-1 by confocal microscopy. COX-2 in human foreskin fibroblasts stimulated by PMA (100 nm) or interleukin-1beta (1 ng/ml) for 6 h was localized to plasma membrane in addition to endoplasmic reticulum and nuclear envelope. Caveolin-1 was localized to plasma membrane, and image overlay showed colocalization of COX-2 with caveolin-1. This was confirmed by the presence of COX-2 and caveolin-1 in the detergent-insoluble membrane fraction of cells stimulated by PMA. Immunoprecipitation showed complex formation of COX-2 with caveolin-1 in a time-dependent manner. A larger quantity of COX-2 was complexed with caveolin-1 in PMA-treated than in interleukin-1beta-treated cells. Purified COX-2 complexed with glutathione S-transferase-fused caveolin-1, which was not inhibited by the scaffolding domain peptide. Caveolin-1-bound COX-2 was catalytically active, and its activity was not inhibited by the scaffolding domain peptide. These results suggest that COX-2 induced by PMA and interleukin-1beta is colocalized with caveolin-1 in the segregated caveolae compartment. Because caveolae are rich in signaling molecules, this COX-2 compartment may play an important role in diverse pathophysiological processes.
PMID: 11432874 [PubMed - indexed for MEDLINE]