OBJECTIVETo analyze the differential protein expression of left-sided colon cancer and right-sided colon cancer.

METHODSTissue samples of left-sided colon cancer (n=7) and right-sided colon cancer (n=7) were collected. Tissue protein was abstracted and two-dimensional gel electrophoresis (2-DE) was used to examine the gel images. Peptide mass fingerprintings (PMF) was acquired by matrix assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS) and the proteins were identified by data searching with bioinformatics. Immunohistochemical SP method was used for the detection of glucose regulated protein 78 kD (GRP78) and heat shock protein 20 (HSP20) in left-sided colon cancer (n=50) and right-sided colon cancer (n=50) tissues.

RESULTSSixteen differentiating protein spots were identified. Compared with right-sided colon cancer, 10 proteins including GRP78 up-regulated and 6 proteins including HSP20 down-regulated in left-sided colon cancer. Immunohistochemical detection showed that in left and right sided colon cancer, the positive expression rate of GRP78 was 78% (39/50) and 56% (28/50) and the positive expression rate of HSP20 was 34% (17/50) and 72% (36/50), respectively, and the differences were statistically significant (both P<0.05). The positive rate of GRP78 was associated with tumor differentiation, infiltration layer, TNM staging, lymph node metastasis, and liver metastasis, while the positive rate of HSP20 was associated with tumor gross morphology, TNM staging, and lymph node metastasis (P<0.05).

CONCLUSIONSThere are differentially expressed proteins between left-sided colon cancer and right-sided colon cancer, especially for GRP78 and HSP20, which may be the cause leading to the biological differences between left-sided and right-sided colon cancer.

Adult ; Aged ; Colonic Neoplasms ; metabolism ; Female ; Gene Expression Regulation, Neoplastic ; HSP20 Heat-Shock Proteins ; metabolism ; Heat-Shock Proteins ; metabolism ; Humans ; Male ; Middle Aged

Preeclampsia (PE) is a pregnancy-specific, multi-system disorder and the leading cause of maternal and perinatal morbidity and mortality in obstetrics worldwide. Excessive vasoconstriction and dysregulated coagulation function are closely associated with PE. Heat shock protein 20 (HSP20) is ubiquitously expressed under normal physiological conditions and has important roles in vascular dilatation and suppression of platelet aggregation. However, the role of HSP20 in the pathogenesis of PE remains unclear. In this study, we collected chorionic plate resistance arteries (CPAs) and serum from 118 healthy pregnant women and 80 women with PE and detected the levels of HSP20 and its phosphorylated form. Both HSP20 and phosphorylated HSP20 were downregulated in CPAs from women with PE. Comparison of the vasodilative ability of CPAs from the two groups showed impaired relaxation responses to acetyl choline in preeclamptic vessels. In addition to the reduced HSP20 in serum from women with PE, the platelet distribution width and mean platelet volume were also decreased, and the activated partial thromboplastin time and thromboplastin time were elevated.With regard to the vital roles of HSP20 in mediating vasorelaxation and coagulation function, the decreased HSP20 might contribute to the pathogenesis of PE.
Adult ; Case-Control Studies ; Chorion ; blood supply ; Female ; HSP20 Heat-Shock Proteins ; metabolism ; Humans ; Phosphorylation ; Placenta ; blood supply ; Platelet Function Tests ; Pre-Eclampsia ; metabolism ; Pregnancy ; Vasoconstriction ; Vasodilation

The influence of spinal cord injury (SCI) on protein expression in the rat urinary bladder was assessed by proteomic analysis at different time intervals post-injury. After contusion SCI between T9 and T10, bladder tissues were processed by 2-DE and MALDI-TOF/MS at 6 hr to 28 days after SCI to identify proteins involved in the healing process of SCI-induced neurogenic bladder. Approximately 1,000 spots from the bladder of SCI and sham groups were visualized and identified. At one day after SCI, the expression levels of three protein were increased, and seven spots were down-regulated, including heat shock protein 27 (Hsp27) and heat shock protein 20 (Hsp20). Fifteen spots such as S100-A11 were differentially expressed seven days post-injury, and seven proteins including transgelin had altered expression patterns 28 days after injury. Of the proteins with altered expression levels, transgelin, S100-A11, Hsp27 and Hsp20 were continuously and variably expressed throughout the entire post-SCI recovery of the bladder. The identified proteins at each time point belong to eight functional categories. The altered expression patterns identified by 2-DE of transgelin and S100-A11 were verified by Western blot. Transgelin and protein S100-A11 may be candidates for protein biomarkers in the bladder healing process after SCI.
Animals ; Biological Markers/metabolism ; Electrophoresis, Gel, Two-Dimensional ; Female ; HSP20 Heat-Shock Proteins/metabolism ; HSP27 Heat-Shock Proteins/metabolism ; Microfilament Proteins/metabolism ; Muscle Proteins/metabolism ; Proteome/*biosynthesis ; Proteomics ; Rats ; Rats, Sprague-Dawley ; S100 Proteins/metabolism ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization ; Spinal Cord Injuries/*metabolism/pathology ; Urinary Bladder/*metabolism ; *Wound Healing