Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0038187 (starvation)
 24,951 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A cDNA of 3.2 kb, encoding a putative G protein-coupled receptor and hence called bRGR1, has been isolated from a cDNA library generated from the bovine renal epithelial cell line NBL-1. This cDNA consisted of 41 base pairs of 5'-untranslated sequence, an open reading frame of 1083 base pairs, and a 2.07 kb fragment of 3'-untranslated sequence that includes a poly(dA) tail. The coding sequence predicts a protein of 361 residues. The ligand of the bRGR1 protein may be of low molecular weight, as deduced from the analysis of the predicted primary structure of the receptor protein and the comparison with other subtypes of the G protein-coupled receptor family. The amounts of bRGR1 mRNA significantly increase when NBL-1 cells are cultured in an amino acid-depleted medium. This effect can not be caused by a decrease in protein synthesis because cycloheximide did not mimic the increase in bRGR1 mRNA levels triggered by amino acid starvation. These data suggest that bRGR1 may be an amino acid-regulated gene.
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PMID:Molecular cloning of a bovine renal G-protein coupled receptor gene (bRGR): regulation of bRGR mRNA levels by amino acid availability. 929 61

Five or more orthophosphates bound together by high-energy phosphoanhydride bonds are highly ubiquitous inorganic molecules called polyphosphate. Polyphosphate acts as a signaling molecule eliciting a number of responses in eukaryotic cells, but the mechanisms mediating these effects are poorly understood. Proliferating Dictyostelium discoideum cells accumulate extracellular polyphosphate. At extracellular concentrations similar to those observed in stationary phase cells, polyphosphate inhibits proteasome activity and proliferation, and induces aggregation. Here we identify GrlD as a putative G protein-coupled receptor that mediates binding of extracellular polyphosphate to the cell surface. Cells lacking GrlD do not respond to polyphosphate-induced proteasome inhibition, aggregation, or proliferation inhibition. Polyphosphate also elicits differential effects on cell-substratum adhesion and cytoskeletal F-actin levels based on nutrient availability, and these effects were also mediated by GrlD. Starving cells also accumulate extracellular polyphosphate. Starved cells treated with exopolyphosphatase failed to aggregate effectively, suggesting that polyphosphate also acts as a signaling molecule during starvation-induced development of Dictyostelium. Together, these results suggest that a eukaryotic cell uses a G protein-coupled receptor to mediate the sensing and response to extracellular polyphosphate.
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PMID:The putative G protein-coupled receptor GrlD mediates extracellular polyphosphate sensing in Dictyostelium discoideum. 3078 40