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Articles by H. Endo
Total Records ( 2 ) for H. Endo
  H. Endo , M. Tabuchi , M.S. Ashenagar , K. Ooshima , H. Chen and H. Higashino
  To clarify the role of adrenal glands in hypertensive animals, levels of catecholamines and corticosteroids in plasma and the mRNA expression of the associated enzymes were measured in 6 and 9-week-old stroke-prone spontaneously hypertensive rats (SHRSP) and normotensive Wistar Kyoto rats (WKY) following cold stress. With and without cold stress immersing in cold water at 4°C for 15 sec, catecholamines, adrenocorticotropic hormone (ACTH) and corticosteroids in plasma and mRNA expression in adrenal glands were measured using high performance liquid chromatography (HPLC), enzyme immunoassay (EIA) and DNA microarray, respectively. L-dopa, dopamine and adrenaline in plasma increased more in SHRSP than WKY at 6 and 9 weeks of age after cold stress. Th, Ddc and Dbh mRNAs were upregulated in the adrenal glands of SHRSP after cold stress, more apparent at 6 weeks than at 9 weeks of age. Corticosterone and aldosterone in plasma increased in both SHRSP and WKY, but this effect was more apparent in SHRSP after elevation of ACTH evoked by cold stress. Expressions of cyp11a1 and cyp21a1 mRNAs were upregulated in both SHRSP and WKY at 6 weeks of age after cold stress. We conclude that l-dopa, dopamine, and adrenaline were synthesized following induction of Th, Ddc and Dbh mRNAs. Corticosterone and aldosterone in plasma increased following the induction of cyp11a1 and cyp21a1 mRNAs which are stimulated along with ACTH elevation following cold stress in young SHRSP more than WKY. This difference may be related to the initiation and/or development of hypertension in SHRSP in normal condition and/or during stress.
  M Sumitani , K Kasashima , E Ohta , D Kang and H. Endo

We have identified a novel mitochondrial protein, termed M19, by proteomic analysis of mitochondrial membrane proteins from HeLa cells. M19 is highly conserved among vertebrates, and possesses no homologous domains with other known proteins. By northern and western blotting, mouse M19 was shown to be expressed in various tissues, and to be especially abundant in the brain. Human M19 (hM19) is present in mitochondria, and protease-protection experiment showed it to be sublocalized in the matrix space. Carboxy-terminally tagged hM19 appeared as spotted signals within mitochondria and co-localized with signals arising from mitochondrial DNA (mtDNA), suggesting the inclusion of M19 in the mtDNA–protein complex (mitochondrial nucleoids). Fractionation of mitochondrial nucleoids from HeLa cells revealed that hM19 has a similar distribution pattern like that of known nucleoid components, such as mtSSB and PHBs, and surely exists in the nucleoid fraction. Furthermore, expression of M19 is closely related to the amount of mtDNA, because it was down-regulated in mtDNA-depleted 0 HeLa cells. These results indicate that M19 associates with the nucleoid and likely regulates the organization and metabolism of mtDNA.

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