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Institution

CJ CheilJedang

CompanySeoul, South Korea
About: CJ CheilJedang is a company organization based out in Seoul, South Korea. It is known for research contribution in the topics: Fermentation & Polynucleotide. The organization has 1342 authors who have published 859 publications receiving 7826 citations.


Papers
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Journal Article
TL;DR: The p38 kinase is revealed as a key signaling molecule differentially regulated by H-ras and N-ras, leading to H-ra-specific cell invasive and migrative phenotypes in human breast epithelial cells.
Abstract: Ras expression has been suggested as a marker for tumor aggressiveness of breast cancer,including the degrees of invasion and tumor recurrence.We showed previously that H-ras, but not N-ras, up-regulates matrix metalloproteinase 2 expression and induces invasive phenotype in MCF10A human breast epithelial cells (A. Moon, et al. Int. J. Cancer, 85: 176–181, 2000). In this study, we show that H-ras also promotes cell motility more effectively than N-ras in MCF10A cells. We have investigated H-ras-specific signaling pathway(s) critical for H-ras-mediated cell motility and invasive phenotype. Whereas neither H-ras nor N-ras activated c-Jun NH2-terminal kinase 1, both H-ras and N-ras effectively activated extracellular signal-regulated protein kinase (ERK) -1,2. Importantly, prominent activation of p38 mitogen-activated protein kinase was shown only in H-ras-activated cells but not in N-ras-activated MCF10A cells. Functional significance of H-ras-activated p38 in invasiveness and cell motility was evidenced by studies using SB203580, a chemical inhibitor of p38, and a dominant-negative construct of p38. Whereas inhibition of c-Jun NH2-terminal kinase 1 activity had no effect on H-ras-induced MCF10A cell invasion and motility, the inhibition of the ERK pathway using a chemical inhibitor PD98059 or dominant-negative mutant of mitogen-activated protein/ERK kinase 1, an activator of ERKs, significantly reduced H-ras-induced invasion and migration. We also provide evidence that p38 and, to a lesser degree, ERKs, are critical for H-ras-mediated up-regulation of matrix metalloproteinase 2. Taken together, the present study shows that H-ras activation of both p38 and ERKs induces cell invasion and motility, whereas N-ras activation of ERKs alone is not sufficient. This study reveals the p38 kinase as a key signaling molecule differentially regulated by H-ras and N-ras, leading to H-ras-specific cell invasive and migrative phenotypes in human breast epithelial cells.

193 citations

Journal ArticleDOI
TL;DR: B. amyloliquefaciens showed significant improvement in nutritional quality and bioactivity by removing the protein- and carbohydrate-based anti-nutritional factors, as well as allergens, from solid-state fermentation process.
Abstract: To evaluate the impact of fermentation with Bacillus amyloliquefaciens U304 on nutritional quality and bioactivity of soybean meal (SBM), we analyzed the solid-state fermentation process for Bacillus amyloliquefaciens, Lactobacillus spp., and Saccharomyces cerevisiae. B. amyloliquefaciens showed significant improvement in nutritional quality and bioactivity by removing the protein- and carbohydrate-based anti-nutritional factors (ANFs), as well as allergens. The total phenolic content, reducing power, free radical scavenging ability, and Ca2+ chelating ability of SBM, as indicators of the antioxidant activity, increased to 195.8, 201.7% (at 10 mg/mL), 136.6% (at 10 mg/mL), and 122.3%, respectively, after Bacillus fermentation. S. cerevisiae decomposed carbohydrate-based but not protein-based ANFs, and fermentation with this organism produced similar values of the antioxidant markers of unfermented soybean meal, except for the reducing power (160.0% at 10 mg/mL). Lactobacillus spp. was only effective for decreasing the activity of trypsin inhibitors, but not other ANFs, resulting in lower bioactivity of fermented soybean meal. B. amyloliquefaciens U304 can substantially improve both the nutritional quality and bioactivity of SBM.

159 citations

Patent
18 Sep 1998
TL;DR: In this paper, the gene encoding a 4-hydroxybutyryl-Co A transferase has been isolated from bacteria and integrated into the genome of bacteria also expressing a polyhydroxyalkanoate synthase, to yield an improved production process for 4HB-containing polyhydroxalkanoates using transgenic organisms, including both bacteria and plants.
Abstract: The gene encoding a 4-hydroxybutyryl-Co A transferase has been isolated from bacteria and integrated into the genome of bacteria also expressing a polyhydroxyalkanoate synthase, to yield an improved production process for 4HB-containing polyhydroxyalkanoates using transgenic organisms, including both bacteria and plants. The new pathways provide means for producing 4HB containing PHAs from cheap carbon sources such as sugars and fatty acids, in high yields, which are stable. Useful strains are obtaining by screening strains having integrated into their genomes a gene encoding a 4HB-CoA transferase and/or PHA synthase, for polymer production. Processes for polymer production use recombinant systems that can utilize cheap substrates. Systems are provided which can utilize amino acid degradation pathways, α-ketoglutarate, or succinate as substrate.

153 citations

Journal ArticleDOI
TL;DR: The results suggest that Fxn supplementation plays a beneficial role in not only regulating the plasma and hepatic lipids metabolism but also for blood glucose-lowering action in high-fat fed mice.

152 citations

Journal ArticleDOI
TL;DR: These newly identified lactobacilli hold promise for use as probiotic agents, feed additives and/or in food applications as well as against a panel of pathogenic bacteria.

151 citations


Authors

Showing all 1342 results

NameH-indexPapersCitations
Deok-Kun Oh482707516
Hye Jin Kim321994065
Jeong Hwan Kim291802582
Cheong-Weon Cho291602708
Hye-Jung Kim29842396
Jinhwan Lee28535247
Han-Joon Hwang27622269
Jae-Gu Pan25571971
Young-Ok Kim241762377
Jong-Hyun Kim221481645
Wei Niu22642601
Jee Eun Han21591391
Oliver P. Peoples21861911
Jun-Gu Choi20481302
Seung Won Park201811291
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Performance
Metrics
No. of papers from the Institution in previous years
YearPapers
20221
202127
202073
201973
201866
201755