Zobrazeno 1 - 10
of 22
pro vyhledávání: '"Kumiko Kogishi"'
Autor:
Yoichi Chiba, Atsuyoshi Shimada, Mamoru Satoh, Masaki Ueno, Kumiko Kogishi, Hiromi Fujisawa, Takatoshi Matsushita, Kazunori Hirayoshi, Ichiro Akiguchi, Yoshinori Yamashita, Masanori Hosokawa
Publikováno v:
International Congress Series. 1260:255-258
We studied changes in the quantity of reactive oxygen species (ROS) and the changes in mitochondrial morphology in cultured murine dermal fibroblast-like (MDF) cells from SAMP11 and SAMR1 mice. The quantity of ROS in the SAMP11 cells was greater than
Autor:
Kaori Kitagawa, Jing Wang, Masanori Hosokawa, Zhanjun Guo, Keiichi Higuchi, Xiaoying Fu, Kumiko Kogishi, Takatoshi Mastushita, Masayuki Mori
Publikováno v:
Amyloid. 10:207-214
In mice, apolipoprotein A-II (apoA-II) associates to form amyloid fibrils in an age-associated manner. We determined the complete nucleotide sequences of the apoA-II gene (Apoa2) cDNA in 41 inbred strains of mice including Mus musculus domesticus (la
Autor:
Hisatoshi Kondo, Akihiro Nakamura, Kumiko Kogishi, Akira Ohta, Takuya Chiba, Takatoshi Matsushita, Masanori Hosokawa, Keiichi Higuchi, Jing Wang, Masayuki Mori, Chen Xia
Publikováno v:
The Journals of Gerontology Series A: Biological Sciences and Medical Sciences. 55:B432-B439
Biochemical and genetic data suggest that the Apoa2 c allele of the apolipoprotein A-II gene causes severe senile amyloidosis (AApoAII) in SAMP1, a mouse model for accelerated senescence. We analyzed the effects of replacement of Apoa2 c in SAMP1 mic
Autor:
Masanori Hosokawa, Jing Wang, Keiichi Higuchi, Jun-ichi Miyazaki, Izumu Saito, Cher Xia, Takatoshi Matsushita, Kumiko Kogishi, Takuya Chiba
Publikováno v:
The American Journal of Pathology. 155:1319-1326
Apolipoprotein A-II (apoA-II), the second most abundant apolipoprotein of serum high density lipoprotein, deposits as an amyloid fibril (AApoAII) in old mice. Mouse strains with a high incidence of senile amyloidosis have the type C apoA-II gene (Apo
Autor:
Naoyuki Seriu, Shizue Yoshimura, Toshio Takeda, Akira Ohta, Masanori Hosokawa, Hiromasa Tojo, Makiko Umezawa, Kumiko Kogishi
Publikováno v:
The Journal of Nutrition. 129:431-437
Semipurified diets incorporating either perilla oil [high in alpha-linolenate, 18:3(n-3)] or safflower oil [high in linoleate, 18:2(n-6)] were fed to senescence-resistant SAMR1 mouse dams and their pups. Male offspring at 15 mo were examined using be
Autor:
Masanori Hosokawa, Takatoshi Matsushita, Keiichi Higuchi, Chen Xia, Kumiko Kogishi, Takuya Chiba, Jing Wang
Publikováno v:
Biochemical Journal. 325:653-659
Apolipoprotein A-II (apoA-II), the major apoprotein of serum high-density lipoprotein, is deposited as amyloid fibrils (AApoAII) in murine senile amyloidosis. We have identified and purified a more basic amyloid protein from old-mouse liver. N-termin
Autor:
Yoshiko Kishimoto, Kumiko Kogishi, Yoshiaki Omori, Masanori Hosokawa, Eishi Deguchi, Toshio Abe, Keiichi Higuchi, Toshio Takeda, Kuraichi Yasuoka, Takatoshi Matsushita, Kozo Shimakawa
Publikováno v:
Experimental Gerontology. 32:111-116
The Senescence-Accelerated Mouse (SAM) was established by inbreeding and pedigree selection based on the life span, degree of senescence, as well as the incidence and degree of several age-associated disorders. At first, SAM strains were developed un
Publikováno v:
Journal of Lipid Research, Vol 33, Iss 12, Pp 1753-1764 (1992)
Apolipoprotein B (apoB) mRNA is modified by a post-transcriptional editing reaction (C to U) changing a glutamine (CAA) to a translational stop codon (UAA) and producing apoB-48 mRNA in mammalian liver and intestine. Developmental and age-related cha
Autor:
Tatsumi Korenaga, Takatoshi Matsushita, Akihiro Nakamura, Masayuki Mori, Zhanjun Guo, Kumiko Kogishi, Junjie Yao, Masanori Hosokawa, Xiaoying Fu, Fuyuki Kametani, Yanming Xing, Keiichi Higuchi
Publikováno v:
The Journal of biological chemistry. 277(36)
Aggregated amyloid fibrils can induce further polymerization of precursor proteins in vitro, thus providing a possible basis for propagation or transmission in the pathogenesis of amyloidoses. Previously, we postulated that the transmission of amyloi