The Experts below are selected from a list of 483309 Experts worldwide ranked by ideXlab platform
Markku Jalkanen - One of the best experts on this subject based on the ideXlab platform.
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A novel laminin-binding form of syndecan-1 (cell surface proteoglycan) produced by syndecan-1 cDNA-transfected NIH-3T3 cells.
Experimental Cell Research, 1994Co-Authors: Markku Salmivirta, Markku Mali, Jyrki Heino, Jorma Hermonen, Markku JalkanenAbstract:Syndecan-1, a cell surface proteoglycan, binds many extracellular matrix components via its heparan sulfate side chains. In previous studies syndecan-1 has failed to bind laminin, although both syndecan-1 and laminin are expressed at sites of early matrix accumulation, like in basement membranes of epithelial-mesenchyma boundaries and in condensing mesenchymes during embryonic development. In order to study whether syndecan-1 regulates the adhesion of Mesenchymal cells to laminin, syndecan-1 was expressed in NIH-3T3 cells by transfection. Syndecan-1-transfected cells showed increased binding to laminin in comparison to control transfected cells. We then compared the properties of syndecan-1 isolated from transfected NIH-3T3 cells and from NMuMG mammary epithelial cells. In solid-phase binding assays, syndecan-1 from NIH-3T3 cells, but not NMuMG cells, bound to laminin. NIH-3T3-derived syndecan contained more chondroitin sulfate than NMuMG-derived syndecan-1, and our results revealed that both heparan sulfate and chondroitin sulfate mediate syndecan-1 binding to laminin. E3 domain revealed highest binding for syndecan-1 among the elastase-derived fragments of laminin. These results suggest that induction of syndecan-1 in Mesenchymal cells may be involved in cellular recognition of laminin during developmental processes.
Markku Salmivirta - One of the best experts on this subject based on the ideXlab platform.
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A novel laminin-binding form of syndecan-1 (cell surface proteoglycan) produced by syndecan-1 cDNA-transfected NIH-3T3 cells.
Experimental Cell Research, 1994Co-Authors: Markku Salmivirta, Markku Mali, Jyrki Heino, Jorma Hermonen, Markku JalkanenAbstract:Syndecan-1, a cell surface proteoglycan, binds many extracellular matrix components via its heparan sulfate side chains. In previous studies syndecan-1 has failed to bind laminin, although both syndecan-1 and laminin are expressed at sites of early matrix accumulation, like in basement membranes of epithelial-mesenchyma boundaries and in condensing mesenchymes during embryonic development. In order to study whether syndecan-1 regulates the adhesion of Mesenchymal cells to laminin, syndecan-1 was expressed in NIH-3T3 cells by transfection. Syndecan-1-transfected cells showed increased binding to laminin in comparison to control transfected cells. We then compared the properties of syndecan-1 isolated from transfected NIH-3T3 cells and from NMuMG mammary epithelial cells. In solid-phase binding assays, syndecan-1 from NIH-3T3 cells, but not NMuMG cells, bound to laminin. NIH-3T3-derived syndecan contained more chondroitin sulfate than NMuMG-derived syndecan-1, and our results revealed that both heparan sulfate and chondroitin sulfate mediate syndecan-1 binding to laminin. E3 domain revealed highest binding for syndecan-1 among the elastase-derived fragments of laminin. These results suggest that induction of syndecan-1 in Mesenchymal cells may be involved in cellular recognition of laminin during developmental processes.
Hee Su Lee - One of the best experts on this subject based on the ideXlab platform.
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Bone formation of embryonic stem cell-derived Mesenchymal stem cells
Tissue Engineering and Regenerative Medicine, 2015Co-Authors: Yeon Tae Jung, Ki-yeon Yoo, Hee Su LeeAbstract:Human embryonic stem cells are multipotent cells. In this study, We observed osteogenesis of human embryonic stem cell derived Mesenchymal stem cells. mbryonic body formation method was used to derive Mesenchymal stem cells from human embryonic stem cells. Embryonic stem cell derived Mesenchymal stem cells were immunostained for CD 73 to make characterization of mesencymal stem cells. Osteogenesis of CD 73 positive mesencymal stem cells with media included ascorbic acid, dexamethasone and glycerophosphate was induced. After 10 days culture with osteogenesis media, the cells were immunostained with type I collagen, osteocalcin and Runx-2. After 21 days culture with osteogenesis media, the cells were stained with alizarin red to observe bone nodule formation. Mesenchymal stem cells were derived from human embryonic stem cells by embryonic body method. After these cells were cultured with osteogenesis media, the cells were differentiated into osteoblast and showed bone nodule formation.
Jorma Hermonen - One of the best experts on this subject based on the ideXlab platform.
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A novel laminin-binding form of syndecan-1 (cell surface proteoglycan) produced by syndecan-1 cDNA-transfected NIH-3T3 cells.
Experimental Cell Research, 1994Co-Authors: Markku Salmivirta, Markku Mali, Jyrki Heino, Jorma Hermonen, Markku JalkanenAbstract:Syndecan-1, a cell surface proteoglycan, binds many extracellular matrix components via its heparan sulfate side chains. In previous studies syndecan-1 has failed to bind laminin, although both syndecan-1 and laminin are expressed at sites of early matrix accumulation, like in basement membranes of epithelial-mesenchyma boundaries and in condensing mesenchymes during embryonic development. In order to study whether syndecan-1 regulates the adhesion of Mesenchymal cells to laminin, syndecan-1 was expressed in NIH-3T3 cells by transfection. Syndecan-1-transfected cells showed increased binding to laminin in comparison to control transfected cells. We then compared the properties of syndecan-1 isolated from transfected NIH-3T3 cells and from NMuMG mammary epithelial cells. In solid-phase binding assays, syndecan-1 from NIH-3T3 cells, but not NMuMG cells, bound to laminin. NIH-3T3-derived syndecan contained more chondroitin sulfate than NMuMG-derived syndecan-1, and our results revealed that both heparan sulfate and chondroitin sulfate mediate syndecan-1 binding to laminin. E3 domain revealed highest binding for syndecan-1 among the elastase-derived fragments of laminin. These results suggest that induction of syndecan-1 in Mesenchymal cells may be involved in cellular recognition of laminin during developmental processes.
Jyrki Heino - One of the best experts on this subject based on the ideXlab platform.
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A novel laminin-binding form of syndecan-1 (cell surface proteoglycan) produced by syndecan-1 cDNA-transfected NIH-3T3 cells.
Experimental Cell Research, 1994Co-Authors: Markku Salmivirta, Markku Mali, Jyrki Heino, Jorma Hermonen, Markku JalkanenAbstract:Syndecan-1, a cell surface proteoglycan, binds many extracellular matrix components via its heparan sulfate side chains. In previous studies syndecan-1 has failed to bind laminin, although both syndecan-1 and laminin are expressed at sites of early matrix accumulation, like in basement membranes of epithelial-mesenchyma boundaries and in condensing mesenchymes during embryonic development. In order to study whether syndecan-1 regulates the adhesion of Mesenchymal cells to laminin, syndecan-1 was expressed in NIH-3T3 cells by transfection. Syndecan-1-transfected cells showed increased binding to laminin in comparison to control transfected cells. We then compared the properties of syndecan-1 isolated from transfected NIH-3T3 cells and from NMuMG mammary epithelial cells. In solid-phase binding assays, syndecan-1 from NIH-3T3 cells, but not NMuMG cells, bound to laminin. NIH-3T3-derived syndecan contained more chondroitin sulfate than NMuMG-derived syndecan-1, and our results revealed that both heparan sulfate and chondroitin sulfate mediate syndecan-1 binding to laminin. E3 domain revealed highest binding for syndecan-1 among the elastase-derived fragments of laminin. These results suggest that induction of syndecan-1 in Mesenchymal cells may be involved in cellular recognition of laminin during developmental processes.
