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Ikuo Yana

Researcher at University of Tokyo

Publications -  25
Citations -  3045

Ikuo Yana is an academic researcher from University of Tokyo. The author has contributed to research in topics: Matrix metalloproteinase & Extracellular matrix. The author has an hindex of 17, co-authored 24 publications receiving 2929 citations. Previous affiliations of Ikuo Yana include University of Michigan.

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Journal ArticleDOI

Regulation of Cell Invasion and Morphogenesis in a Three-Dimensional Type I Collagen Matrix by Membrane-Type Matrix Metalloproteinases 1, 2, and 3

TL;DR: It is demonstrated that MT-MMP–expressing cells can penetrate and remodel type I collagen-rich tissues by using membrane-anchored metalloproteinases as pericellular collagenases.
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Regulation of membrane type-1 matrix metalloproteinase activation by proprotein convertases.

TL;DR: The existence of a proprotein convertase-MT1-MMP axis that can regulate extracellular matrix remodeling is demonstrated and two sets of basic motifs in the propeptide region of MT1- MMP are identified that potentially can be recognized by the proprotein converts of subtilisin-like proteases.
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CD44 directs membrane‐type 1 matrix metalloproteinase to lamellipodia by associating with its hemopexin‐like domain

TL;DR: It is demonstrated that MT1‐MMP forms a complex with CD44H via the hemopexin‐like (PEX) domain, andCD44H appears to act as a linker that connects MT1 •MMP to the actin cytoskeleton and to play a role in directing MT1•MMPto the migration front.
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Cytoplasmic tail-dependent internalization of membrane-type 1 matrix metalloproteinase is important for its invasion-promoting activity.

TL;DR: It is reported that MT1-MMP is internalized from the surface and that this event depends on the sequence of its cytoplasmic tail, and dynamic turnover at the migration edge by internalization is important for proper enzyme function during cell migration and invasion.
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Negative Regulation of Osteoclastogenesis by Ectodomain Shedding of Receptor Activator of NF-κB Ligand

TL;DR: Soluble RANKL produced by osteoblasts from MMP14-deficient mice was markedly reduced, and their osteoclastogenic activity was promoted, consistent with the findings of increased osteoclineogenesis in vivo.