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Articles by A Kobayashi
Total Records ( 3 ) for A Kobayashi
  A. E Pepe , Q Xiao , A Zampetaki , Z Zhang , A Kobayashi , Y Hu and Q. Xu
 

Rationale: Nuclear factor erythroid 2-related factor (Nrf)3, a member of the cap ‘N’ collar family of transcription factors that bind to the DNA-antioxidant responsive elements, is involved in reactive oxygen species balancing and in muscle precursor migration during early embryo development.

Objective: To investigate the functional role of Nrf3 in smooth muscle cell (SMC) differentiation in vitro and in vivo.

Methods and Results: Nrf3 was upregulated significantly following 1 to 8 days of SMC differentiation. Knockdown of Nrf3 resulted in downregulation of smooth muscle specific markers expression, whereas enforced expression of Nrf3 enhanced SMC differentiation in a dose-dependent manner. SMC-specific transcription factor myocardin, but not serum response factor, was significantly upregulated by Nrf3 overexpression. Strikingly, the binding of SRF and myocardin to the promoter of smooth muscle differentiation genes was dramatically increased by Nrf3 overexpression, and Nrf3 can directly bind to the promoters of SMC differentiation genes as demonstrated by chromatin immunoprecipitation assay. Moreover, NADPH-derived reactive oxygen species production during SMC differentiation was further enhanced by Nrf3 overexpression through upregulation of NADPH oxidase and inhibition of antioxidant signaling pathway. In addition, Nrf3 was involved in the endoplasmic reticulum stressor induced SMC differentiation.

Conclusion: Our findings demonstrate for the first time that Nrf3 has a crucial role in SMC differentiation from stem cells indicating that Nrf3 could be a potential target for manipulation of stem cell differentiation toward vascular lineage.

  A Kobayashi , Y Matsuda , M Mitani , Y Makino and H. Ohta
 

Objective: The aim of this study was to analyze the antithrombin-III (AT-III) activity in the serum in relation to other laboratory findings, including the serum albumin, total protein (TP), and uric acid (UA), and to assess the recovery of the AT-III activity in the serum after its administration in obstetrically ill patients. Patients and Methods: The medical records of 27 patients who were diagnosed to have disseminated intravascular coagulation (DIC) based on the obstetric DIC scores were reviewed and the relationships between the activity of AT-III in the serum and other laboratory findings were evaluated. The effect of administration of AT-III on the recovery of AT-III activity in the serum was also evaluated. Results: All the patients survived without any sequelae. The mean obstetric DIC score was 11.1 ± 3.1 (range 8-19) and the mean blood loss during the first 24 hours was 3798 ± 3,435 mL (range 480-16 208 mL). There was a significant correlation between the serum AT-III activity before the treatment and the serum albumin (r = .67, P = .001) and TP (r = .59, P = .021), but not serum UA. Seven patients required over 3000 IU of AT-III concentrate to obtain an increase in the serum AT-III activity to over 70%. The UA level in this group was significantly higher than that in the remaining patients. Conclusion: The serum AT-III activity was correlated with the serum albumin level before the start of treatment. Therefore, measurement of the serum albumin level before and during treatment is helpful.

  H Kajiura , H Koiwa , Y Nakazawa , A Okazawa , A Kobayashi , T Seki and K. Fujiyama
 

N-Glycosylation is an important post-translational modification that occurs in many secreted and membrane proteins in eukaryotic cells. Golgi -mannosidase I hydrolases (MANI) are key enzymes that play a role in the early N-glycan modification pathway in the Golgi apparatus. In Arabidopsis thaliana, two putative MANI genes, AtMANIa (At3g21160) and AtMANIb (At1g51590), were identified. Biochemical analysis using bacterially produced recombinant AtMANI isoforms revealed that both AtMANI isoforms encode 1-deoxymannojirimycin-sensitive -mannosidase I and act on Man8GlcNAc2 and Man9GlcNAc2 structures to yield Man5GlcNAc2. Structures of hydrolytic intermediates accumulated in the AtMANI reactions indicate that AtMANIs employ hydrolytic pathways distinct from those of mammalian MANIs. In planta, AtMANI-GFP/DsRed fusion proteins were detected in the Golgi stacks. Arabidopsis mutant lines manIa-1, manIa-2, manIb-1, and manIb-2 showed N-glycan profiles similar to that of wild type. On the other hand, the manIa manIb double mutant lines produced Man8GlcNAc2 as the predominant N-glycan and lacked plant-specific complex and hybrid N-glycans. These data indicate that either AtMANIa or AtMANIb can function as the Golgi -mannosidase I that produces the Man5GlcNAc2 N-glycan structure necessary for complex N-glycan synthesis.

 
 
 
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