Transcriptional regulation of rat liver protein disulphide-isomerase gene by insulin and in diabetes
- 15 April 1990
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 267 (2) , 317-323
- https://doi.org/10.1042/bj2670317
Abstract
The mRNA encoding for rat protein disulphide-isomerase (PDI) increases 3-fold in the liver of diabetic rats and is accompanied by similar changes at the protein level. Long treatment (for 3 days) of diabetic rats with insulin reverses this effect of diabetes both at the mRNA and protein levels. The higher expression of rat PDI mRNA in diabetes is due to an increase in the transcriptional rate of the gene, and insulin treatment of diabetic animals produces within 30 min a decrease in the level of transcription of PDI gene, as judged by nuclear run-on transcription experiments performed in vivo. These results clearly show a role for insulin in the regulation of transcription of the gene encoding this multifunctional protein in rat liver.This publication has 39 references indexed in Scilit:
- Insulin short-term control of rat liver α2-microglobulin gene transcriptionJournal of Biological Chemistry, 1989
- Protein disulfide isomerase: Multiple roles in the modification of nascent secretory proteinsCell, 1989
- Syncatalytic inactivation of prolyl 4-hydroxylase by synthetic peptides containing the unphysiologic amino acid 5-oxaproline.Journal of Biological Chemistry, 1988
- Insulin regulates expression of the human growth hormone gene in transfected cells.Journal of Biological Chemistry, 1988
- Defective co-translational formation of disulphide bonds in protein disulphide-isomerase-deficient microsomesNature, 1988
- Nucleotide sequence of rat liver iodothyronine 5′-monodeiodinase (5′MD): Its identity with the protein disulfide isomeraseBiochemical and Biophysical Research Communications, 1988
- Glycosylation site binding protein, a component of oligosaccharyl transferase, is highly similar to three other 57 kd luminal proteins of the ERCell, 1988
- Thyroid hormone down-regulates p55, a thyroid hormone-binding protein that is homologous to protein disulfide isomerase and the beta-subunit of prolyl-4-hydroxylase.Journal of Biological Chemistry, 1988
- Sequence of membrane-associated thyroid hormone binding protein from bovine liver: Its identity with protein disulphide isomeraseBiochemical and Biophysical Research Communications, 1987
- Sequence of protein disulphide isomerase and implications of its relationship to thioredoxinNature, 1985