In this study, a new automatic sleep stage judgment system was proposed using a non-invasive type air mattress sensor enabling the detection of three useful bio-signals: heartbeat rate, respiratory rate and other body movement. We found that fairly good correlations exist between these signals and the sleep stage. Based on this knowledge, we developed a novel sleep estimation method free from any stress.

The classical mitogen-activated protein(MAP) kinase cascade is one of the central intracellular signaling pathways that play a crucial role in cell proliferation, cell differentiation, cell transformation, and many other cellular responses. Two novel MAP kinase cascades, the SAPK/JNK cascade and the p38/MPK2 cascade, were identified, and were shown to function in various stress responses and apoptotic processes. Intracellular distribution of classical MAP kinase kinase (MAPKK/MEK) is regulated by its nuclear export signal (NES) which may function to suppress malignant cell transformation. CRM1 protein has been identified as a receptor for leucine-rich NES. CRM1 binds to CAN/NUP214, one of nucleopore proteins, which has been suggested to be involved in myeloid leukemia. Thus, the nuclear export system may be by somehow related to cancer development.

Tungsten carbide powder with 3. 5 μ m average particle diameter was shocked by the indirect method to produce a quasi-isentropic plane compression wave normal to the cylinder axis. [1]Recovered specimens showed the evidence of melt and possible evaporation . For the lower temperature specimen, compacted structure possibly sintered through melt was observed and for the high temperature shock specimen newly formed triangular plates were observed.

Autophosphorylation of the recombinant mitogen-activated protein kinase (MAPK) from Xenopus laevis has been studied to detect the conformational changes in the region of regulatory phosphorylation upon enzyme activation. Slow autophosphorylation of Xenopus MAPK occurred predominantly on tyrosine, the major phosphoregulatory site of MAPKs, through an intramolecular mechanism and was accompanied by a low magnitude stimulation of the catalytic activity towards an exogenous substrate, myelin basic protein. Autophosphorylated but not unphosphorylated enzyme was shown to interact with the protein substrate. In contrast to the previously reported reversibility of many tyrosine kinase reactions, the tyrosine phosphorylation of Xenopus MAPK was found to be irreversible in the presence of high ADP concentrations, although ADP could competitively inhibit both autophosphorylation and myelin basic protein phosphorylation. We concluded, therefore, that the phosphoregulatory tyrosine is no more accessible to an intramolecular phosphotransferase reaction and is out of the reach of the enzyme catalytic center after phosphorylation. The conformational changes in the region of regulatory phosphorylation resulted in a reduced immunoprecipitation of autophosphorylated and MAPK-kinase-phosphorylated forms of the enzyme by a polyclonal antibody raised against a synthetic peptide corresponding to residues 173-197 of Xenopus MAPK which includes the sites of regulatory phosphorylation. The reduced recognition was not due to the phosphorylation itself, since the antibody efficiently immunoprecipitated SDS-denatured forms of the phosphorylated enzyme. The antibody was not a neutralizing antibody, allowing unphosphorylated MAPK to undergo autophosphorylation while in the immune complex. However, autophosphorylation caused a release of phosphorylated enzyme from the immune complex, suggesting that dramatic conformational changes, which could even overcome the antibody constraints, took place in the phosphoregulatory region of MAPK upon enzyme activation.

We have cloned a Saccharomyces cerevisiae gene (COF1) encoding a low-M(r) actin-binding protein of 143 amino acid (aa) residues (yeast cofilin; Cof); its aa sequence is 35% identical to porcine Cof. The yeast recombinant Cof produced in Escherichia coli exhibited in vitro activities on actin filaments similar to those of mammalian and avian Cof. Gene disruption and tetrad analysis showed that gene COF1 is essential for yeast cell growth. Expression of the cDNA of porcine Cof or destrin (Des), the latter a Cof-related protein, complemented the cof1 null allele in yeast cells.

Journal Article Nucleotide sequence of cofilin cDNA Get access Kenji Moriyama, Kenji Moriyama Search for other works by this author on: Oxford Academic PubMed Google Scholar Seiji Matsumoto, Seiji Matsumoto 1Department of Cell Biology, the Tokyo Metropolitan Institute of Medical ScienceHonkomagome, Tokyo 113, Japan Search for other works by this author on: Oxford Academic PubMed Google Scholar Eisuke Nishida, Eisuke Nishida Search for other works by this author on: Oxford Academic PubMed Google Scholar Hiloichi Sakai, Hiloichi Sakai Search for other works by this author on: Oxford Academic PubMed Google Scholar Ichiro Yahara Ichiro Yahara 1Department of Cell Biology, the Tokyo Metropolitan Institute of Medical ScienceHonkomagome, Tokyo 113, Japan Search for other works by this author on: Oxford Academic PubMed Google Scholar Nucleic Acids Research, Volume 18, Issue 10, 25 May 1990, Page 3053, https://doi.org/10.1093/nar/18.10.3053 Published: 25 May 1990 Article history Received: 12 April 1990 Published: 25 May 1990

is a pioneer in researches on primitive motile systems and has been playing a leading part in cell motility studies for more than forty years.On the occasion of

A new protein factor that modulates microtubule assembly in a Ca2+ or Mg2+ concentration-dependent manner was extracted from porcine brain and purified by ammonium sulfate fractionation, acetone fractionation, chromatography on an affinity column fixed with microtubule proteins, and high speed liquid chromatography. The isolated protein was nearly homogeneous on SDS-polyacrylamide gel, appearing as a 94,000-dalton polypeptide. The protein gave a single symmetric peak with a relatively large Stokes radius on Sepharose 4B gel filtration. Moreover, it sedimented as a single homogeneous component with a sedimentation constant of nearly 5 S on sucrose density gradient centrifugation. These analyses indicated the homogeneity of the isolated protein and the asymmetry of its conformation. The purified protein factor slightly inhibited microtubule assembly under standard assembly condition. Increase in the concentration of either free Ca2+ or free Mg2+ markedly enhanced its inhibitory effect. Neither Ni2+ nor Mn2+ potentiated the inhibitory effect of the protein. The inhibition was reversible in a fashion dependent on the concentration of Ca2+ or Mg2+ and appeared to be stoichiometric rather than catalytic. The inhibitory activity was totally destroyed by trypsin digestion, but was very heat stable and was not lost on treatment with N-ethylmaleimide. This new protein factor may play an important role in regulation of microtubule assembly and/or function.

Journal Article Effects of Solution Variables on the Calcium Sensitivity of the Microtubule Assembly System Get access Eisuke NISHIDA Eisuke NISHIDA Department of Biophysics and Biochemistry, Faculty of Science, The University of TokyoHongo, Bunkyo-ku, Tokyo 113 Search for other works by this author on: Oxford Academic PubMed Google Scholar The Journal of Biochemistry, Volume 84, Issue 3, September 1978, Pages 507–512, https://doi.org/10.1093/oxfordjournals.jbchem.a132154 Published: 01 September 1978 Article history Received: 07 March 1978 Published: 01 September 1978