This study was designed to evaluate whether the nurses' assessment of postoperative pain can be an alternative to patients' self-reporting. We examined 187 patients receiving postoperative intravenous patient-controlled analgesia. The nurses assessed the patients' pain with three pain indices (therapeutic efficacy, pain intensity, and facial pain expression) 8 hr after operation. The patients recorded their resting and movement pain using 100-mm visual analog scales immediately following the nurses' assessment. There was an acceptable correlation between overall pain measurement assessed by patients and that assessed by nurses (canonical correlation coefficient=0.72, p=0.0001). The resting pain was more reliably reflected than the movement pain in overall measurement assessed both by nurses and by patients. Among the three pain indices assessed by nurses, the pain intensity most reliably reflected the patients' self-reports. The pain intensity assessed with a simple verbal descriptor scale therefore is believed to be an effective alternative to the patients' self-reports of postoperative pain at rest. However, it mirrored the patients' self-reports during movement less reliably. Therapeutic efficacy and facial pain expression indices were not effective alternatives to patients' self-reporting.
Analgesia, Patient-Controlled ; Facial Expression ; Human ; Nursing Assessment/*methods/standards ; Pain Measurement ; Pain, Postoperative/*nursing ; Perioperative Nursing/*methods ; Reproducibility of Results

2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) can induce drug transporter genes such as the ATP-binding cassette G member 2 (ABCG2), which contributes to multidrug resistance. We investigated the effect of TCDD pretreatment on drug transporters induction from cancer cells of various origins. Cell viabilities after treatment of cisplatin were measured to evaluate acquiring cisplatin resistance by TCDD. Acquring cisplatin resistance was found only in cisplatin senstivie cancer cells including gastric SNU601, colon LS180, brain CRT-MG and lymphoma Jurkat cells which showed a significant increase in cell viability after combined treatment with TCDD and cisplatin. High increase of ABCG2 gene expression was found in SNU601 and LS180 cells with a mild increase in the expression of the ABCC3, ABCC5,and SLC29A2 genes in SNU601 cells, and of major vault protein (MVP) in LS180 cells. The AhR inhibitor kaempferol suppressed the upregulation of ABCG2 expression and reversed the TCDD-induced increase in cell viability in LS180 cells. However, in CRT-MG cells, other transporter genes including ABCC1, ABCC5, ABCA3, ABCA2, ABCB4, ABCG1, and SLC29A1 were up-regulated. These findings suggested the acquiring cisplatin resistance by TCDD associated with cancer cell-type-specific induction of drug transporters.
ATP-Binding Cassette Transporters/genetics/*metabolism ; Cell Line, Tumor ; Cell Survival/drug effects ; Cisplatin/*pharmacology ; Drug Resistance, Neoplasm/drug effects ; Equilibrative-Nucleoside Transporter 2/genetics/metabolism ; Humans ; Jurkat Cells ; K562 Cells ; Kaempferols/pharmacology ; Multidrug Resistance-Associated Proteins/genetics/metabolism ; Neoplasm Proteins/genetics/*metabolism ; RNA, Messenger/metabolism ; Receptors, Aryl Hydrocarbon/metabolism ; Tetrachlorodibenzodioxin/*pharmacology ; Up-Regulation/*drug effects ; Vault Ribonucleoprotein Particles/genetics/metabolism

2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) can induce drug transporter genes such as the ATP-binding cassette G member 2 (ABCG2), which contributes to multidrug resistance. We investigated the effect of TCDD pretreatment on drug transporters induction from cancer cells of various origins. Cell viabilities after treatment of cisplatin were measured to evaluate acquiring cisplatin resistance by TCDD. Acquring cisplatin resistance was found only in cisplatin senstivie cancer cells including gastric SNU601, colon LS180, brain CRT-MG and lymphoma Jurkat cells which showed a significant increase in cell viability after combined treatment with TCDD and cisplatin. High increase of ABCG2 gene expression was found in SNU601 and LS180 cells with a mild increase in the expression of the ABCC3, ABCC5,and SLC29A2 genes in SNU601 cells, and of major vault protein (MVP) in LS180 cells. The AhR inhibitor kaempferol suppressed the upregulation of ABCG2 expression and reversed the TCDD-induced increase in cell viability in LS180 cells. However, in CRT-MG cells, other transporter genes including ABCC1, ABCC5, ABCA3, ABCA2, ABCB4, ABCG1, and SLC29A1 were up-regulated. These findings suggested the acquiring cisplatin resistance by TCDD associated with cancer cell-type-specific induction of drug transporters.
ATP-Binding Cassette Transporters/genetics/*metabolism ; Cell Line, Tumor ; Cell Survival/drug effects ; Cisplatin/*pharmacology ; Drug Resistance, Neoplasm/drug effects ; Equilibrative-Nucleoside Transporter 2/genetics/metabolism ; Humans ; Jurkat Cells ; K562 Cells ; Kaempferols/pharmacology ; Multidrug Resistance-Associated Proteins/genetics/metabolism ; Neoplasm Proteins/genetics/*metabolism ; RNA, Messenger/metabolism ; Receptors, Aryl Hydrocarbon/metabolism ; Tetrachlorodibenzodioxin/*pharmacology ; Up-Regulation/*drug effects ; Vault Ribonucleoprotein Particles/genetics/metabolism

Purpose: Identification of type I protein arginine methyltransferase (PRMT) substrates and their functional significance during tumorigenesis is becoming more important. The present study aimed to identify target substrates for type I PRMT using 2-dimensional (2D) gel electrophoresis (GE) and 2D Western blotting (WB). Methods: Using immunoblot analysis, we compared the expression of type I PRMTs and endogenous levels of arginine methylation between the primary colorectal cancer (CRC) and adjacent noncancerous tissues paired from the same patient. To identify arginine-methylated proteins in HCT116 cells, we carried out 2D-GE and 2D-WB with a type I PRMT product-specific antibody (anti-dimethyl-arginine antibody, asymmetric [ASYM24]). Arginine-methylated protein spots were identified by mass spectrometry, and messenger RNA (mRNA) levels corresponding to the identified proteins were analyzed using National Center for Biotechnology Information (NCBI) microarray datasets between the primary CRC and noncancerous tissues. Results: Type I PRMTs and methylarginine-containing proteins were highly maintained in CRC tissues compared to noncancerous tissues. We matched 142 spots using spot analysis software between a Coomassie blue (CBB)-stained 2D gel and 2D-WB, and we successfully identified 7 proteins that reacted with the ASYM24 antibody: CACYBP, GLOD4, MAPRE1, CCT7, TKT, CK8, and HSPA8. Among these proteins, the levels of 4 mRNAs including MAPRE1, CCT7, TKT, and HSPA8 in CRC tissues showed a statistically significant increase compared to noncancerous tissues from patients using the NCBI microarray datasets. Conclusion Our results indicate that the method shown here is useful in identifying arginine-methylated proteins, and significance of arginine modification in the proteins identified here should be further identified during CRC development.