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Yu Yamaguchi

Researcher at National Foundation for Cancer Research

Publications -  10
Citations -  4164

Yu Yamaguchi is an academic researcher from National Foundation for Cancer Research. The author has contributed to research in topics: Decorin & Proteoglycan. The author has an hindex of 6, co-authored 10 publications receiving 4092 citations.

Papers
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Negative regulation of transforming growth factor-β by the proteoglycan decorin

TL;DR: The ability of decorin to bind transforming growth factor-β, an autocrine factor that stimulates the growth of Chinese hamster ovary cells, is reported, suggesting that decorin may be a component of a feedback system regulating cell growth.
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Proteoglycans as modulators of growth factor activities

TL;DR: Proteoglycans bind to extracellular proteins such as fibronectin and are found to be binders of many growth factors.
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Natural inhibitor of transforming growth factor-|[beta]| protects against scarring in experimental kidney disease

TL;DR: It is reported here that administration of decorin inhibits the increased production of extracellular matrix and attenuates manifestations of disease, confirming the hypothesis that decorin may eventually prove to be clinically useful in diseases associated with overproduction of TGF-β.
Journal ArticleDOI

Expression of human proteoglycan in Chinese hamster ovary cells inhibits cell proliferation.

TL;DR: Chinese hamster ovary cell lines expressing human decorin from a stably transfected complementary DNA construct form a more orderly monolayer and grow to a lower saturation density than control cells lacking decorin, revealing a novel growth inhibitory mechanism which may be related to contact inhibition of cell proliferation.
Patent

Inhibitors of cell regulatory factors

TL;DR: In this paper, a method of inhibiting an activity of a cell regulatory factor comprising contacting the cell regulatory factors with a purified polypeptide, wherein the polyPEptide comprises the cell-regulatory factor binding domain of a protein and wherein the protein is characterized by a leucine-rich repeat of about 24 amino acids.