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7. Paradoxical increase in retinoblastoma protein in colorectal carcinomas may protect cells from apoptosis

Author

Yamamoto H, Jw, Soh, Monden T, Mg, Klein, Lm, Zhang, Shirin H, Nadir Arber, Tomita N, Schieren I, Ca, Stein, and Ib, Weinstein

Subjects
Cell Cycle, Apoptosis, Cell Cycle Proteins, Oligonucleotides, Antisense, Immunohistochemistry, Retinoblastoma Protein, E2F Transcription Factors, DNA-Binding Proteins, Tumor Cells, Cultured, Humans, Carrier Proteins, Colorectal Neoplasms, Transcription Factor DP1, Cell Division, Cells, Cultured, Cell Size, Retinoblastoma-Binding Protein 1, Transcription Factors
Abstract

The retinoblastoma (Rb) gene is inactivated in a variety of human cancers, but in colorectal carcinomas there is frequently increased expression of this gene. This is paradoxical in view of the known role of Rb as a tumor suppressor gene. In the present study, we compared the levels of expression of the Rb protein (pRb) in normal human colorectal mucosa, adenomatous polyps, and carcinomas by immunohistochemistry. In vitro studies were also done to examine the phenotypic effects of an antisense oligodeoxynucleotide (AS-Rb) targeted to Rb mRNA in the HCT116 colon carcinoma cell line that expresses a relatively high level of pRb. The incidence of pRb-positive cells was increased during multistage colorectal carcinogenesis. In vitro treatment of HCT116 cells with AS-Rb decreased the level of pRb by about 70% and also decreased the levels of the cyclin D1 protein and cyclin D1-associated kinase activity. AS-Rb inhibited growth of HCT116 cells and induced apoptosis. Reporter assays indicated about a 17-fold increase in E2F activity. These findings suggest that the increased expression of pRb in colorectal carcinoma cells may provide a homeostatic mechanism that protects them from growth inhibition and apoptosis, perhaps by counterbalancing potentially toxic effects of excessive E2F activity.

Published
1999

26. Lineage- and differentiation stage-specific expression of LSM-1 (LPAP), a possible substrate for CD45, in human hematopoietic cells

Author

Shimizu, Y., primary, Sugiyama, H., additional, Fujii, Y., additional, Sasaki, K., additional, Inoue, K., additional, Ogawa, H., additional, Tamaki, H., additional, Miyake, S., additional, Oji, Y., additional, Soma, T., additional, Yamagami, T., additional, Hirata, M., additional, Ikeda, K., additional, Monden, T., additional, and Kishimoto, T., additional

Published
1997
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38. Omission of [(15)O]CO scan for PET CMRO(2) examination using (15)O-labelled compounds.

Author

Sasakawa Y, Kudomi N, Yamamoto Y, Monden T, Kawai N, Nishiyama Y, Sasakawa, Yasuhiro, Kudomi, Nobuyuki, Yamamoto, Yuka, Monden, Toshihide, Kawai, Nobuyuki, and Nishiyama, Yoshihiro

Abstract

Objective: CBF, OEF and CMRO(2) provide us important clinical indices and are used for assessing ischemic degree in cerebrovascular disorders. These quantitative images can be measured by PET using (15)O-labelled tracers such as C(15)O, C(15)O(2) and (15)O(2). To reduce the time of scan, one possibility is to omit the use of CBV data. The present study investigated the influence of fixing the CBV to OEF and CMRO(2) values on subjects with and without cerebrovascular disorders. Methods: The study consisted of three groups, namely, GROUP-0 (n = 10), GROUP-1 (n = 9), and GROUP-2 (n = 10), corresponding to--without significant disorder, with elevated CBV, and with reduced CBF and elevated OEF, respectively. All subjects received PET examination and using the PET data OEF and CMRO(2) images were computed by fixing CBV and with CBV data. The computed OEF and CMRO(2) values were compared between the methods. Results: The OEF and CMRO(2) values obtained by fixing the CBV were around 10% underestimation against that with CBV data. The regression analysis showed that these values were comparable (r = 0.93-0.98, P < 0.001). The simulation showed that fixing of the CBV would not derive significant error in either OEF or CMRO(2) values, when changed from 0 to 0.08 ml/g. Conclusion: This study shows the feasibility of fixing the CBV value for computing OEF and CMRO(2) values in the PET examination, suggesting the CO scan could be eliminated. [ABSTRACT FROM AUTHOR]

Published
2011
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45. Excision of a Urachal Sinus with Use of a Voice-Controlled Laparoscope.

Author

Yano, H., Iwazawa, T., and Monden, T.

Subjects
SURGICAL excision, PERITONEUM, LAPAROSCOPIC surgery
Abstract

A 34-year-old man with an umbilical urachal sinus underwent a voice-controlled robot-assisted laparoscopic excision. In the operational procedure, three trocars were inserted into the peritoneal cavity. Exploration with a laparoscope revealed a cystic lesion at the middle part of the lower abdomen that extended about 4 cm in the major axis just from the umbilicus. The caudal stump of the urachus was ligated with an absorbable clip and divided. The cephalic side of the lesion was ligated just at the umbilicus with an Endo-Loop and divided. The lesion was then peeled from the peritoneum and taken from the peritoneal cavity. The robot allowed a safer and more secure movement of the scope. The postoperative course was uneventful, the surgical wound scars were very small, and the cosmetic results were satisfactory. There was no recurrence and no transformation of the navel. Our experience was encouraging enough to suggest that voice-controlled robot-assisted laparoscopic excision in patients with urachal disease is a beneficial therapeutic option that is easy, safe, and minimally invasive, with excellent cosmetic results. [ABSTRACT FROM AUTHOR]

Published
2003
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50. Isolation and characterization of a novel ligand-dependent thyroid hormone receptor-coactivating protein.

Author

Monden, T, Wondisford, F E, and Hollenberg, A N

Abstract

The thyroid hormone receptor (TR) regulates the expression of target genes upon binding to triiodothyronine (T3) response elements. In the presence of T3, the TR recruits coactivating proteins that both modulate and integrate the ligand response. We report here the cloning of a novel protein using the TR ligand-binding domain as bait in the yeast two-hybrid system. Analysis of a putative full-length clone demonstrates a cDNA sequence that encodes a protein of 920 amino acids with a size of 120 kDa (p120). Alignment with known sequences shows homology to a previously identified protein of unknown function, termed skeletal muscle abundant protein. Interaction studies demonstrate that p120 interacts with the TR AF-2 domain in the presence of ligand through a 111-amino acid region. Northern analysis demonstrates widespread expression in human tissues. Cotransfection assays in CV-1 cells demonstrate that p120 enhances TR-mediated transactivation on multiple T3 response elements in the presence of T3. In addition, CREB-binding protein synergizes with p120 to enhance this effect. When linked to the GAL4 DNA-binding domain, p120 is an activator of transcription alone. Thus, p120 satisfies a number of important criteria as a nuclear receptor coactivator.

Published
1997

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