Biomaterial Database

Hyperosmotic urea increases transcription and synthesis of Egr-1 in murine inner medullary collecting duct (mIMCD3) cells. 1994

D M Cohen, and W W Chin, and S R Gullans

Renal Division, Brigham and Women's Hospital, Boston, Massachusetts 02115.

It was previously shown that when cells of renal epithelial origin are exposed to hyperosmotic urea in concentrations unique to the renal medulla, abundance of mRNA encoding the immediate-early gene product Egr-1 is up-regulated. This phenomenon appears restricted to cells of renal epithelial origin. In the present study, the newly isolated murine renal inner medullary cell line mIMCD3 was used to determine whether the urea-induced increase in Egr-1 mRNA abundance is associated with increased expression of functional protein product, and whether this increase is transcriptionally mediated. In Western analysis, urea (200 mM) increased Egr-1 immunoreactivity 3-fold relative to sham-treated cells. [35S]Methionine pulse-labeling followed by immunoprecipitation confirmed that this increased immunoreactivity was associated with increased de novo Egr-1 protein synthesis. Electrophoretic mobility shift assay demonstrated that urea treatment induced a commensurate increase in specific DNA binding activity for the Egr-1 consensus sequence. In addition, the increase in Egr-1 mRNA expression accompanying urea treatment was a consequence of enhanced transcription, as determined by nuclear run-off assay. Taken together, these data indicate that hyperosmotic urea increases both Egr-1 transcription and new protein synthesis in renal epithelial cells in culture, and that this newly synthesized Egr-1 is a functional DNA-binding protein. To our knowledge, this is the first example of urea-inducible gene transcription. In addition, Egr-1 represents the first eukaryotic transcription factor transcriptionally activated by a hyperosmotic stressor.

UI	MeSH Term	Description	Entries
D007679	Kidney Medulla	The internal portion of the kidney, consisting of striated conical masses, the renal pyramids, whose bases are adjacent to the cortex and whose apices form prominent papillae projecting into the lumen of the minor calyces.	Kidney Papilla,Kidney Medullas,Kidney Papillas,Medulla, Kidney,Medullas, Kidney,Papilla, Kidney,Papillas, Kidney
D007685	Kidney Tubules, Collecting	Straight tubes commencing in the radiate part of the kidney cortex where they receive the curved ends of the distal convoluted tubules. In the medulla the collecting tubules of each pyramid converge to join a central tube (duct of Bellini) which opens on the summit of the papilla.	Kidney Collecting Ducts,Kidney Collecting Duct,Collecting Duct, Kidney,Collecting Ducts, Kidney
D009841	Oligonucleotides	Polymers made up of a few (2-20) nucleotides. In molecular genetics, they refer to a short sequence synthesized to match a region where a mutation is known to occur, and then used as a probe (OLIGONUCLEOTIDE PROBES). (Dorland, 28th ed)	Oligonucleotide
D009997	Osmotic Pressure	The pressure required to prevent the passage of solvent through a semipermeable membrane that separates a pure solvent from a solution of the solvent and solute or that separates different concentrations of a solution. It is proportional to the osmolality of the solution.	Osmotic Shock,Hypertonic Shock,Hypertonic Stress,Hypotonic Shock,Hypotonic Stress,Osmotic Stress,Hypertonic Shocks,Hypertonic Stresses,Hypotonic Shocks,Hypotonic Stresses,Osmotic Pressures,Osmotic Shocks,Osmotic Stresses,Pressure, Osmotic,Pressures, Osmotic,Shock, Hypertonic,Shock, Hypotonic,Shock, Osmotic,Shocks, Hypertonic,Shocks, Hypotonic,Shocks, Osmotic,Stress, Hypertonic,Stress, Hypotonic,Stress, Osmotic,Stresses, Hypertonic,Stresses, Hypotonic,Stresses, Osmotic
D011485	Protein Binding	The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.	Plasma Protein Binding Capacity,Binding, Protein
D002460	Cell Line	Established cell cultures that have the potential to propagate indefinitely.	Cell Lines,Line, Cell,Lines, Cell
D004268	DNA-Binding Proteins	Proteins which bind to DNA. The family includes proteins which bind to both double- and single-stranded DNA and also includes specific DNA binding proteins in serum which can be used as markers for malignant diseases.	DNA Helix Destabilizing Proteins,DNA-Binding Protein,Single-Stranded DNA Binding Proteins,DNA Binding Protein,DNA Single-Stranded Binding Protein,SS DNA BP,Single-Stranded DNA-Binding Protein,Binding Protein, DNA,DNA Binding Proteins,DNA Single Stranded Binding Protein,DNA-Binding Protein, Single-Stranded,Protein, DNA-Binding,Single Stranded DNA Binding Protein,Single Stranded DNA Binding Proteins
D005786	Gene Expression Regulation	Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control (induction or repression) of gene action at the level of transcription or translation.	Gene Action Regulation,Regulation of Gene Expression,Expression Regulation, Gene,Regulation, Gene Action,Regulation, Gene Expression
D000818	Animals	Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.	Animal,Metazoa,Animalia
D001665	Binding Sites	The parts of a macromolecule that directly participate in its specific combination with another molecule.	Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining