Biomedical subjects

D Noda

Publications and source records attributed to D Noda.

3 recordsLinked to original sources

PubMed2006

ELAC2, a putative prostate cancer susceptibility gene product, potentiates TGF-beta/Smad-induced growth arrest of prostate cells.

Transforming growth factor-beta (TGF-beta) elicits a potent growth inhibitory effect on many normal cells by binding to specific serine/threonine kinase receptors and activating specific Smad proteins, which regulate the expression of cell cycle genes, including the p21 cyclin-dependent kinase (CDK) inhibitor gene. Interestingly, cancer cells are often insensitive to the anti-mitogenic effects of TGF-beta for which the molecular mechanisms are not well understood. In this study, we found that the candidate prostate cancer susceptibility gene ELAC2 potentiates TGF-beta/Smad-induced transcriptional responses. ELAC2 associates with activated Smad2; the C-terminal MH2 domain of Smad2 interacts with the N-terminal region of ELAC2. Small interfering siRNA-mediated knock-down of ELAC2 in prostate cells suppressed TGF-beta-induced growth arrest. Moreover, ELAC2 was shown to specifically associate with the nuclear Smad2 partner, FAST-1 and to potentiate the interaction of activated Smad2 with transcription factor Sp1. Furthermore, activation of the p21 CDK inhibitor promoter by TGF-beta is potentiated by ELAC2. Taken together our data indicate an important transcriptional scaffold function for ELAC2 in TGF-beta/Smad signaling mediated growth arrest.

Animals↗

PubMed2000

[MRSA septicemia caused by an infected pacemaker lead: a case report with a review of Japanese literatures].

A 50-year-old woman was admitted to our hospital because of MRSA septicemia caused by a contaminated permanent pacemaker lead. A pacemaker system was successfully removed under cardiopulmonary bypass support. Postoperative antibiotics was administered for 7 weeks. Total removal of a pacemaker system under cardiopulmonary bypass support is the treatment of choice in a case with pacemaker infection associated with MRSA septicemia.

Aminoglycosides↗

PubMed1981

Adipose cell size-function relationships: insulin binding and degradation.

125I-insulin binding and degradation have been studied in isolated rat adipose cells of increasing size. Binding at 24 degrees C reaches a steady state by 40-60 min in the absence of significant degradation. At 37 degrees C, binding reaches only a transient maximum by 10-15 min because insulin is rapidly degraded. Cellular enlargement is associated with increasing steady-state binding per cell at 24 degrees C, and increasing maximum binding and degradation per cell at 37 degrees C, in spite of increasing plasma insulin concentrations in the rats from which cells were prepared. Detailed steady-state studies at 24 degrees C, however, fail to delineate the mechanism of these alterations. Although dissociation experiments are consistent with the presence of a small degree of negatively cooperative binding site interaction, its magnitude is unchanged with increasing cell size. Furthermore, binding levels per unit cellular surface at 24 degrees C, at least at those insulin concentrations eliciting a biological response, remain relatively constant. None of the alterations in insulin binding observed here can explain the enlarged adipose cell's markedly decreased metabolic response to insulin.

Adipose Tissue↗