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Research at OU

Biology

73  Esumi, S.; Kakazu, N.; Taguchi, Y.; Hirayama, T.; Sasaki, A.; Hirabayashi, T.; Koide, T.; Kitsukawa, T.; Hamada, S.; Yagi, T.
(Graduate School of Frontier Biosciences)
Monoallelic Yet Combinatorial Expression of Variable Exons of the Protocadherin-α Gene Cluster in Single Neurons
Nature Genetics, 37, 171-176 (2004)


74 Hanayama, R.*1; Tanaka, M.*1; Miyasaka, K.*1,2; Aozasa, K.*1; Koike, M.*1; Uchiyama, Y.*1; Nagata, S.*1,2
*1 (Graduate School of Medicine) *2 (Graduate School of Frontier Biosciences)
Autoimmune Disease and Impaired Uptake of Apoptotic Cells in MFG-E8-Deficient Mice
Science, 304, 1147-1150 (2004)


75 Hayase, A.*1,2; Takagi, M.*1,2; Miyazaki, T.*1,2; Oshiumi, H.*1; Shinohara, M.*1; Shinohara, A.*1,2
*1 (Institute for Protein Research) *2 (Graduate School of Science)
A Protein Complex Containing Mei5 and Sae3 Promotes the Assembly of the Meiosis-Specific RecA Homolog Dmc1
Cell, 119, 927-940 (2004)


76 Hirasaki, E.; Ogihara, N.; Hamada, Y.; Kumakura, H.; Nakatsukasa, M.
(Graduate School of Human Sciences)
Do Highly Trained Monkeys Walk Like Humans? A Kinematic Study of Bipedal Locomotion in Bipedally Trained Japanese Macaques
Journal of Human Evolution, 46, 739-750 (2004)

Experiments that compared the bipedal walking of highly trained and ordinary monkeys provides two insights into the early stage of the evolution of human bipedalism. The finding that training considerably improved bipedal walking suggests that behavioral changes preceded morphological changes in the evolution of bipedalism. The finding that macaques, which are phylogenetically distant from humans, developed human-like gait characteristics with training, provides strong support for the commonly held but unproven idea that the human gait characteristics are advantageous to bipedalism.


77 Hishida, T.; Han, Y.-W.; Shibata, T.; Kubota, Y.; Ishino, Y.; Iwasaki, H.; Shinagawa, H.
(Research Institute for Microbial Diseases)
Role of the Escherichia coli RecQ DNA Helicase in SOS Signaling and Genome Stabilization at Stalled Replication Forks
Genes & Development, 18, 1886-1897 (2004)

The RecQ protein family is a highly conserved group of DNA helicases that plays role in maintaining genomic stability. In this study, we found that RecQ generates a single-stranded DNA gap on the lagging strand that can recruit RecA for SOS induction and recombination at stalled replication fork. These findings have uncovered a conserved role of the prokaryotic and eukaryotic RecQ family of helicases in the integration of the DNA replication with DNA recombination and checkpoint response.


78 Horiki, M.; Imamura, T.; Okamoto, M.; Hayashi, M.; Murai, J.; Myoui, A.; Ochi, T.; Miyazono, K.; Yoshikawa, H.; Tsumaki, N.
(Graduate School of Medicine)
Smad6/Smurf1 Overexpression in Cartilage Delays Chondrocyte Hypertrophy and Causes Dwarfism with Osteopenia
The Journal of Cell Biology, 165, 433-445 (2004)

Chondrocyte differentiation is strictly regulated for normal development and growth of bone. We generated transgenic mice overexpressing Smad6 and Smad ubiquitin regulatory factor 1 (Smurf1) in chondrocytes, to investigate their roles in skeletal development. Smad6 overexpression down-regulated Smad1/5/8 phosphorylation and inhibited chondrocyte hypertrophy induced by bone morphogenetic protein 2. The reduced population of hypertrophic chondrocytes was associated with bone loss. Cartilage phenotype of Smad6/Smurf1 double transgenic mice provided evidence that Smurf1 supports Smad6 function in vivo.


79 Ikeda, F.; Nishimura, R.; Matsubara, T.; Tanaka, S.; Inoue, J.; Reddy, S.V.; Hata, K.; Yamashita, K.; Hiraga, T.; Watanabe, T.; Kukita, T.; Yoshioka, K.; Rao, A.; Yoneda, T.
(Graduate School of Dentistry)
Critical Roles of c-Jun Signaling in Regulation of NFAT Family and RANKL-regulated Osteoclast Differentiation
The Journal of Clinical Investigation, 114, 475-484 (2004)


80 Inamori, K.; Endo, T.; Gu, J.; Matsuo, I.; Ito, Y.; Fujii, S.; Iwasaki, H.;Narimatsu, H.; Miyoshi, E.; Honke, K.; Taniguchi, N.
(Graduate School of Medicine)
N-Acetylglucosaminyltransferase IX Acts on the GlcNAcβ1,2-Manα1-Ser/Thr Moiety, Forming a 2,6-Branched Structure in Brain O-Mannosyl Glycan
Journal of Biological Chemistry, 279, 2337-2340 (2004)

O-Mannosyl glycan is one of major O-glycans in mammalian brain, which contains GlcNAcβ1,2-Man and GlcNAcβ1,2-(GlcNAcβ1,6-)Man structures. It has been shown that the deficiencies of the biosynthetic pathway of O-mannosyl glycan cause congenital muscular dystrophies with associated defects in brain development. We demonstrated that a brain specific β1,6-N-acetylglucosaminyltransferase GnT-IX acts on the O-mannosyl glycan, forming the GlcNAcβ1,2-(GlcNAcβ1,6-)Man structure. Although the biological function of the β1,6-branching structure is unknown so far, it may be involved in normal brain development.


81 Inoue, N.*1; Ikawa, M.*1; Isotani, A.*1,2; Okabe, M.*1,2
*1 (Research Institute for Microbial Diseases) *2 (Graduate School of Pharmaceutical Sciences)
The Immunoglobulin Superfamily Protein Izumo is Required for Sperm to Fuse with Eggs
Nature, 434, 234-238 (2005)


82 Kubo, Y.*1; Sekiya, S.*1,2; Ohigashi, M.*1,2; Takenaka, C.; Tamura, K.; Nada, S.*3; Nishi, T.*1; Yamamoto, A.; Yamaguchi, A.*1,2
*1 (Institute of Scientific and Industrial Research) *2 (Graduate School of Pharmaceutical Sciences) *3 (Research Institute for Microbial Diseases)
ABCA5 Resides in Lysosomes and ABCA5 Knockout Mice Develop Lysosomal Disease-Like Symptoms.
Molecular and Cellular Biology, 25, 4138-4149 (2005)

ABCA5 is a member of the ABC transporter A-subfamily. Mouse ABCA5 is expressed in brain, lung, heart and thyroid gland and its subcellular localization were lysosomes and late-endosomes. Abca5-/- mice exhibited dilated cardiomyopathy-like heart that is observed in several lysosomal diseases, although no prominent abnormalities were found in the brain or lung. KO mice also exhibited exophthalmos and collapse of the thyroid gland. Therefore, ABCA5 is a lysosomal associated protein and plays important roles in cardiomyocytes and follicular cells.


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