Socioeconomic and Political Initiators of Pay Comparison (original) (raw)
Related papers
C-kit+ cardiac progenitors exhibit mesenchymal markers and preferential cardiovascular commitment
Cardiovascular research, 2011
The heart contains c-kit(+) progenitors that maintain cardiac homeostasis. Cardiac c-kit(+) cells are multipotent and give rise to myocardial, endothelial and smooth muscle cells, both in vitro and in vivo. C-kit(+) cells have been thoroughly investigated for their stem cell activity, susceptibility to stress conditions and ageing, as well as for their ability to repair the infarcted heart. Recently, expression of mesenchymal stem cell (MSC) markers and MSC differentiation potency have been reported in cardiac progenitor cells. Based on this evidence, we hypothesized that c-kit(+) cells may have phenotypic and functional features in common with cardiac MSCs. Culture of cells obtained from enzymatic dissociation of heart auricle fragments produced a fast-growing fibroblast-like population expressing mesenchymal markers. C-kit(+) cells co-expressing MSC markers were identified in this population, sorted by flow cytometry and cultured in the presence or the absence of unselected cardia...
Post-activation Turn-off of NF-kappa B-dependent Transcription Is Regulated by Acetylation of p65
Journal of Biological Chemistry, 2003
NF-κB represents a family of eukaryotic transcription factors participating in the regulation of various cellular genes involved in the immediate early processes of immune, acute-phase, and inflammatory responses. Cellular localization and consequently the transcriptional activity of NF-κB is tightly regulated by its partner IκBα. Here, we show that the p65 subunit of NF-κB is acetylated by both p300 and PCAF on lysines 122 and 123. Both HDAC2 and HDAC3 interact with p65 although only HDAC3 was able to deacetylate p65. Acetylation of p65 reduces its ability to bind κΒ-DNA. Finally, acetylation of p65 facilitated its removal from DNA and consequently its ΙκΒα-mediated export from the nucleus. We propose that acetylation of p65 plays a key role in ΙκΒα-mediated attenuation of NF-κΒ transcriptional activity which is an important process that restores the latent state in post-induced cells.
Journal of Biological Chemistry, 2005
Flotillin-1 is a lipid raft-associated protein that has been implicated in various cellular processes. We examine the subcellular distribution of flotillin-1 in different cell types, and find that localization is cell type-specific. Flotillin-1 relocates from a cytoplasmic compartment to the plasma membrane upon the differentiation of 3T3-L1 adipocytes. To delineate the structural determinants necessary for its localization, we generated a series of truncation mutants of flotillin-1. Wild-type flotillin-1 has two putative hydrophobic domains, and is localized to lipid raft microdomains at the plasma membrane. Flotillin-1 fragments lacking the N-terminal hydrophobic stretch are excluded from the lipid raft compartments, but remain at the plasma membrane. On the other hand, mutants with the second hydrophobic region deleted fail to traffic to the plasma membrane, but are instead found in intracellular granule-like structures. Flotillin-1 specifically interacts with the adapter protein CAP, the Src family kinase Fyn, and cortical F-actin in lipid raft microdomains in adipocytes. Furthermore, CAP and Fyn associate with different regions in the amino terminal sequences of flotillin-1. These results further our understanding for how flotillin-1 can function as a molecular link between lipid rafts of the plasma membrane and a multimeric signaling complex at the actin cytoskeleton.
Journal of Biological Chemistry, 2003
Troglitazone (TGZ) is a peroxisome proliferator-activated receptor γ (PPARγ) ligand, that has pro-apoptotic activity in human colon cancer. Although TGZ binds to PPARγ transcription factors as an agonist, emerging evidence suggests that TGZ acts independently of PPARγ in many functions, including apoptosis. Early growth response-1 (Egr-1) transcription factor has been linked to apoptosis and shown to be activated by extracellular signal-regulated kinase (ERK). We investigated whether TGZ-induced apoptosis may be related to EGR-1 induction since TGZ has been known to induce ERK activity. Our results show that Egr-1 is dramatically induced by TGZ, but not by other PPARγ ligands. TGZ affects Egr-1 induction at least by two mechanisms; TGZ increases Egr-1 promoter activity by two fold and prolongs Egr-1 mRNA stability by three fold. Inhibition of ERK phosphorylation in HCT-116 cells abolishes the Egr-1 induction by TGZ, suggesting its ERK dependent manner. Further, the TGZ-induced Egr-1 expression results in increased promoter activity using a reporter system containing 4 copies of Egr-1 binding sites, and TGZ induces Egr-1 binding activity to Egr-1 consensus sites as assessed by gel shift assay. In addition, TGZ induces ERK-dependent phosphorylation of PPARγ, resulting in the down-regulation of PPARγ activity. The fact that TGZ-induced apoptosis is accompanied by the biosynthesis of Egr-1 suggests that Egr-1 plays a pivotal role in TGZinduced apoptosis in HCT-116 cells. Our results suggest that Egr-1 induction is a unique property of TGZ compared to other PPARγ ligands, and is independent of PPARγ activation.