In the elderly, preoperative pulmonary risk is frequently present, and careful perioperative management is needed while paying special attention to pulmonary and cardiovascular complications. However, when the indications for surgery can be strictly determined, an esophagectomy is considered a viable treatment alternative with satisfactory prognosis even in patients 80 years of age and older without any increased morbidity or mortality.

The cell synthesis of heat shock proteins is increased by a variety of environmental and pathophysiological stressful conditions. The 70-kD heat shock protein family (HSP70 family) which constitutively expresses hsc70 and heat-inducible hsp70 is thought to be involved in protein-protein interactions, including oncogene products. We investigated the HSP70 family expression and biological behavior of gastric cancer, and its relation to p53 overexpression. Expressions of HSP70 and p53 in 164 primary gastric tumors were determined immunohistochemically. Exploratory data were analyzed on a set of 164 primary gastric cancers, and we constructed in prognostic significance of the HSP70 expression level and the relation to p53 overexpression. Expression of HSP70 (hsc70 and hsp70) were detected in nuclei and/or cytoplasm of cancer cells. Western blotting analysis showed that hsc70 and hsp70 were both expressed in five gastric cancer cell lines. Immunohistochemically stained positive cells of HSP70 varied from 0 (very weak) to 100%, in each case. The median level of positive cell rate was 19.0%. A HSP70 expression of over 19.0% was related to the differentiated tissue type of gastric cancer, but not to other clinicopathological factors. There was no difference in survival rates in subjects with higher and lower groups of HSP70 expression. HSP70 expression was also not related to p53 overexpression in the nuclei and p53 overexpression-related poorer prognosis. Our findings show that the expression of HSP70 is not associated with tumor advance-related characteristics or with the prognosis of gastric cancer. Measurements of HSP70 expression do not appear to be a useful prognostic marker.

he Y-box protein family, which is widely distributed from bacteria to mammals, contains a cold-shock domain which is highly conserved from prokaryotic cold-shock proteins.1) The human Y-box binding protein, YB-1, which is located on chromosome 1p34, was initially identified as a transcription factor which associates with the Y-box sequence appearing in the major histocompatibility complex class II genes. 2-4)It has been hypothesized that YB-1 might play a role in promoting cell proliferation through the transcriptional regulation of various relevant genes, including proliferating cell nuclear antigen, epidermal growth factor receptor, DNA topoisomerase IIα, thymidine kinase, and DNA polymerase α.5, 6) In our laboratory, we have shown that YB-1 is involved in transcriptional activation of the human multidrug resistance 1 gene. [7][8][9] and also the DNA topoisomerase IIα gene 10) in response to various environmental stimuli. YB-1 appears to play a critical role in cell proliferation, DNA replication, and drug resistance. The biological roles of YB-1 include modification of chromatin, translational masking of mRNA, participation in the redox signaling pathway, RNA chaperoning, and stress response regulation.11) It has also been demonstrated that eukaryotic Y-box proteins regulate gene expression at the translational level by recognizing RNA.12, 13) The murine YB-1 protein (MSY1) is specifically expressed in testis rather than other tissues, and regulates the translation of germ cell RNA.14) The Y-box binding proteins thus appear to play critical roles in both mRNA turnover and translational control.YB-1 also appears to protect mammalian cells from the cytotoxic effects induced by DNA damage. We have previously reported that human cancer cell lines overexpressing YB-1 showed resistance to cisplatin, while the reduction of YB-1 itself leads to increased drug sensitivity to cisplatin, other DNAinteracting drugs, and UV irradiation.15) We also demonstrated that YB-1 protein is localized mainly in the cytoplasm, but translocates to the nucleus when cells are irradiated with UV or treated with anticancer drugs.16) YB-1 specifically binds to cisplatin-modified DNA, apurinic DNA and also 8-oxo-guaninecontaining RNA. [17][18][19] We have further demonstrated that YB-1 binds directly to repair-associated proteins such as proliferating cell nuclear antigen and p53 protein. 18,20) YB-1 may thus be involved in the process of DNA repair and/or DNA damage response. In clinical studies on YB-1, the cellular level of YB-1 was found to be closely associated with tumor growth and prognosis in ovarian cancers, lung cancers, and breast cancers. 21-23)To gain more insight into how YB-1 proteins exert their multiple functions, we carried out a targeted disruption of the mouse YB-1 gene (MSY1) in mouse embryonic stem (ES) cells. We have established ES cell lines with a heterozygously targeted disruption of the YB-1 gene (YB-1 +/− ), which we found to result in hypersensitivity to cytotoxic agents, such as cisplatin and mitomycin C. Mater...

This report describes the case of a patient who had undergone surgery to resect bilateral ovarian tumors and then presented with colon metastasis 20 years later. A 69-year-old woman was admitted to the hospital for a clinical survey. She had been operated on for bilateral ovarian cancer in 1987 and was treated by postoperative adjuvant chemotherapy. The patient's follow-up showed no abnormality until 2006. Colonoscopy revealed an elevated irregular lesion in the cecum. A biopsy of the lesion showed a group V, moderately differentiated adenocarcinoma. A right hemicolectomy with a partial resection of the ileum and a lymphadenectomy was performed. Immunohistochemical staining during the pathological diagnosis showed the lesion to be colon metastasis from a serous papillary adenocarcinoma of the ovary. Immunohistochemical staining was positive for cytokeratin 7, carbohydrate antigen (CA)-125, and estrogen receptors, and negative for cytokeratin 20, carcinoembryonic antigen, and CA19-9. The use of immunohistochemistry demonstrated the tumor to be of ovarian origin.

Elastography is a good tool for evaluating hepatic injury after FOLFOX treatment.