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Updated: Oct 14, 2025

Glucose Uptake Measurement and Response to Insulin Stimulation in In Vitro Cultured Human Primary Myotubes
Published on: June 25, 2017
Regulation of glucose responsive protein (GRP) gene expression by insulin
J Lee Franklin1,2, Margaret O Amsler3, Joseph L Messina4,5
1Department of Pathology, Division of Pathobiology and Molecular Medicine, University of Alabama at Birmingham, 1670 University Blvd., Volker Hall G019, Birmingham, AL, 35294-0019, USA.
Abstract:
While screening for insulin-induced genes, we identified two members of a family of stress-induced genes referred to as glucose-regulated proteins (GRPs). GRPs are members of the stress-responsive superfamily of genes which also includes heat shock proteins (HSPs). The GRP proteins are not normally heat-inducible, but are overproduced when cells are starved of glucose. The two major GRP proteins, GRP78 and GRP94, are highly conserved among vertebrates. We have found that physiological concentrations of insulin stimulate the transcription of GRP78 and GRP94 in rat H4IIE hepatoma cells. The regulation of GRP78 transcription was rapid, with the first induction within minutes, and a further induction after several hours, and both occurred in the presence of glucose. GRP78 transcription was more greatly induced by insulin in the presence of SB202190, a specific p38-MAPK inhibitor. Transcription of GRP94 was also induced, but only after several hours. Calcimycin (A23187) and anisomycin were used to induce endoplasmic reticulum (ER)/cellular stress, and both induced GRP78 and GRP94 transcription.
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