PubMed · 7901570
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A G Casson. 1993-11-13. Laparoscopic appendicectomy.. https://pubmed.ncbi.nlm.nih.gov/7901570/
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The G12 subfamily of heterotrimeric G proteins, comprised of the alpha-subunits Galpha12 and Galpha13, has been implicated as a signaling component in cellular processes ranging from cytoskeletal changes to cell growth and oncogenesis. In an attempt to elucidate specific roles of this subfamily in cell regulation, we sought to identify molecular targets of Galpha12. Here we show a specific interaction between the G12 subfamily and the cytoplasmic tails of several members of the cadherin family of cell-surface adhesion proteins. Galpha12 or Galpha13 binding causes dissociation of the transcriptional activator beta-catenin from cadherins. Furthermore, in cells lacking the adenomatous polyposis coli protein required for beta-catenin degradation, expression of mutationally activated Galpha12 or Galpha13 causes an increase in beta-catenin-mediated transcriptional activation. These findings provide a potential molecular mechanism for the previously reported cellular transforming ability of the G12 subfamily and reveal a link between heterotrimeric G proteins and cellular processes controlling growth and differentiation.
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Heme oxygenase (HO-1) is the rate-limiting enzyme in heme catabolism. HO-1, a stress protein, has been suggested to be involved in defense mechanisms against agents that may induce oxidative stress. It has been proposed that renal HO gene expression regulates important hemoprotein(s) such as cytochrome P450 and may be essential to maintain homeostasis in the kidney. Because accurate assessment of HO-1 mRNA in normal and disease states in kidney were not available due to the limited number of cells, we developed a system to quantitate human HO-1 mRNA in samples limited in cell number and/or mRNA copies. Total RNA from human kidney was used to establish this technique; it was reverse-transcribed and then amplified by polymerase chain reaction (PCR) in a tube also containing an internal standard obtained by deleting 50 bp from the original human HO-1 gene. This allowed us to use the same primers for both the sample and internal standard. After amplification, templates were resolved by acrylamide gel electrophoresis and quantitated either by densitometry or radioactivity counted from the bands excised from the gel. When the internal standard is present in the reaction mixture, the ratio of amplified sample vs. the standard template is proportional to the amount of sample RNA, and it is therefore possible to calculate the number of specific mRNA molecules. We have used this approach to quantitate the number of HO-1 mRNA molecules in adenocarcinoma cells. Results show that reverse transcription (RT)/PCR methods were able to determine the number of HO-1 mRNA copies in biopsy samples of human adenocarcinoma cells.