title: Ischemia-responsive protein (irp94) is up-regulated by endoplasmic reticulum stress.
abstract: The expression of the ischemia-responsive protein (irp94) was enhanced by endoplasmic reticulum (ER) stress inducing drugs such as brefeldin A (BFA), calcium ionophor A23187, dithiothreitol (DTT) and tunicamycin in fisher rat thyroid epithelial cell line (FRTL-5 cells). In particular, irp94 mRNA expression was increased dose dependently by tunicamycin, and there was increased irp94 expression when the cells were incubated with the thyroid-stimulating hormone (TSH) together.
authors.affiliation: Department of Emergency Medicine, Chungnam National University Hospital, Taejon, Korea.
authors.forename: S W
authors.initials: SW
authors.lastname: Kim
authors.forename: I S
authors.initials: IS
authors.lastname: Yoo
authors.forename: H S
authors.initials: HS
authors.lastname: Koh
authors.forename: O Y
authors.initials: OY
authors.lastname: Kwon
mesh_terms: D000818:Animals; D002460:Cell Line; D017931:DNA Primers; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D005786:Gene Expression Regulation / Q000502:physiology*; D050957:HSP110 Heat-Shock Proteins; D018840:HSP70 Heat-Shock Proteins / Q000235:genetics*; D007511:Ischemia / Q000235:genetics; D020133:Reverse Transcriptase Polymerase Chain Reaction; D013312:Stress, Physiological / Q000378:metabolism; D013972:Thyrotropin / Q000494:pharmacology
chemical_list: D017931:DNA Primers; D050957:HSP110 Heat-Shock Proteins; D018840:HSP70 Heat-Shock Proteins; D013972:Thyrotropin