The Experts below are selected from a list of 90 Experts worldwide ranked by ideXlab platform

Yukio Kato - One of the best experts on this subject based on the ideXlab platform.

  • enhancement of cell adhesion and spreading by a cartilage specific Noncollagenous Protein cartilage matrix Protein cmp matrilin 1 via integrin α1β1
    Journal of Biological Chemistry, 1999
    Co-Authors: Seicho Makihira, Shigeru Ohno, Takeshi Kawamoto, Katsumi Fujimoto, Akinobu Okimura, Eri Yoshida, Mitsuhide Noshiro, Taizo Hamada, Yukio Kato
    Abstract:

    Abstract Cartilage matrix Protein (CMP; also known as matrilin-1), one of the major Noncollagenous Proteins in most cartilages, binds to aggrecan and type II collagen. We examined the effect of CMP on the adhesion of chondrocytes and fibroblasts using CMP-coated dishes. The CMP coating at 10–20 μg/ml enhanced the adhesion and spreading of rabbit growth plate, resting and articular chondrocytes, and fibroblasts and human epiphyseal chondrocytes and MRC5 fibroblasts. The effect of CMP on the spreading of chondrocytes was synergistically increased by native, but not heated, type II collagen (gelatin). The monoclonal antibody to integrin α1 or β1 abolished CMP-induced cell adhesion and spreading, whereas the antibody to integrin α2, α3, α5, β2, α5β1, or αVβ5had little effect on cell adhesion or spreading. The antibody to integrin α1, but not to other subunits, coprecipitated125I-CMP that was added to MRC5 cell lysates, indicating the association of CMP with the integrin α1 subunit. Unlabeled CMP competed for the binding to integrin α1with 125I-CMP. These findings suggest that CMP is a potent adhesion factor for chondrocytes, particularly in the presence of type II collagen, and that integrin α1β1 is involved in CMP-mediated cell adhesion and spreading. Since CMP is expressed almost exclusively in cartilage, this adhesion factor, unlike fibronectin or laminin, may play a special role in the development and remodeling of cartilage.

  • Enhancement of Cell Adhesion and Spreading by a Cartilage-specific Noncollagenous Protein, Cartilage Matrix Protein (CMP/Matrilin-1), via Integrin α1β1
    Journal of Biological Chemistry, 1999
    Co-Authors: Seicho Makihira, Shigeru Ohno, Takeshi Kawamoto, Katsumi Fujimoto, Akinobu Okimura, Eri Yoshida, Mitsuhide Noshiro, Taizo Hamada, Yukio Kato
    Abstract:

    Abstract Cartilage matrix Protein (CMP; also known as matrilin-1), one of the major Noncollagenous Proteins in most cartilages, binds to aggrecan and type II collagen. We examined the effect of CMP on the adhesion of chondrocytes and fibroblasts using CMP-coated dishes. The CMP coating at 10–20 μg/ml enhanced the adhesion and spreading of rabbit growth plate, resting and articular chondrocytes, and fibroblasts and human epiphyseal chondrocytes and MRC5 fibroblasts. The effect of CMP on the spreading of chondrocytes was synergistically increased by native, but not heated, type II collagen (gelatin). The monoclonal antibody to integrin α1 or β1 abolished CMP-induced cell adhesion and spreading, whereas the antibody to integrin α2, α3, α5, β2, α5β1, or αVβ5had little effect on cell adhesion or spreading. The antibody to integrin α1, but not to other subunits, coprecipitated125I-CMP that was added to MRC5 cell lysates, indicating the association of CMP with the integrin α1 subunit. Unlabeled CMP competed for the binding to integrin α1with 125I-CMP. These findings suggest that CMP is a potent adhesion factor for chondrocytes, particularly in the presence of type II collagen, and that integrin α1β1 is involved in CMP-mediated cell adhesion and spreading. Since CMP is expressed almost exclusively in cartilage, this adhesion factor, unlike fibronectin or laminin, may play a special role in the development and remodeling of cartilage.

Anne George - One of the best experts on this subject based on the ideXlab platform.

  • Transcriptional regulation of dentin matrix Protein 1 (DMP1) in odontoblasts and osteoblasts.
    Connective tissue research, 2020
    Co-Authors: Alexander Jacob, Youbin Zhang, Anne George
    Abstract:

    Dentin matrix Protein 1 (DMP1) is a Noncollagenous Protein important for the mineralization of bones and teeth. Examination of the transcription factor binding sites within the 6.24 kb upstream sequence of rat DMP1 promoter by Matinspector software revealed that TCF11 had the highest number (six) of binding sites with 100% matrix similarity. Four of these sites are conserved in the mouse DMP1 promoter. TCF11 is a member of the Cap-n-Collar (cnc) family of basic leucine zipper transcription factors. Results from this study showed that TCF11 can bind specifically to the DMP1 promoter and activate its transcription in odontoblasts and osteoblasts. This could be attributed to both direct and indirect effects of TCF11. Electrophoretic mobility shift (EMSA) assay showed differential interaction between TCF11 and its binding sites on the DMP1 promoter. 21 bp oligos spanning the TCF11 matrix were used as probes in EMSA, and the results showed that the binding was specific to the sequence of the TCF11 matrix as well as the flanking sequences and this is typical of a heterodimer binding site. Results also showed changes in the binding pattern when cells were differentiated in osteogenic medium for 2 d. Thus, TCF11 may play an important role in the transcriptional regulation of DMP1 gene.

  • DMP1 Binds Specifically to Type I Collagen and Regulates Mineral Nucleation and Growth
    Biomineralization, 2018
    Co-Authors: Anne George, Elizabeth Guirado, Yinghua Chen
    Abstract:

    Extracellular matrix of bone and dentin is highly complex and involves a dynamic process of deposition and removal. Cells are the main architect that build this designer matrix that is highly specialized to calcified tissues. Osteoblasts or odontoblasts secrete both collagen and Noncollagenous Proteins in a temporal and spatial manner. Type I collagen self-assembles and forms a fabric-like template onto which Noncollagenous Proteins and mineral bind in a well-regulated manner. Dentin matrix Protein 1 (DMP1) is one such Noncollagenous Protein that contains several acidic groups that can bind calcium ions which in turn binds phosphate and initiates the calcification process. In this study, we demonstrate that DMP1 is localized at specific sites on the self-assembled collagen matrix of dentin. In vitro nucleation studies on demineralized and deProteinized dentin slice adsorbed with DMP1 show bundles of well-ordered needle-shaped nanohydroxyapatite deposited on the dentin matrix. The nucleated mineral structures had uniform length and width and their long axis was oriented parallel to the collagen fibril axis. Overall, the physiologically self-assembled collagen and DMP1 mediated ordered deposition of nanocrystalline HAP.

  • transcriptional regulation of dentin matrix Protein 1 dmp1 in odontoblasts and osteoblasts
    Connective Tissue Research, 2014
    Co-Authors: Alexander Jacob, Youbin Zhang, Anne George
    Abstract:

    AbstractDentin matrix Protein 1 (DMP1) is a Noncollagenous Protein important for the mineralization of bones and teeth. Examination of the transcription factor binding sites within the 6.24 kb upstream sequence of rat DMP1 promoter by Matinspector software revealed that TCF11 had the highest number (six) of binding sites with 100% matrix similarity. Four of these sites are conserved in the mouse DMP1 promoter. TCF11 is a member of the Cap-n-Collar (cnc) family of basic leucine zipper transcription factors. Results from this study showed that TCF11 can bind specifically to the DMP1 promoter and activate its transcription in odontoblasts and osteoblasts. This could be attributed to both direct and indirect effects of TCF11. Electrophoretic mobility shift (EMSA) assay showed differential interaction between TCF11 and its binding sites on the DMP1 promoter. 21 bp oligos spanning the TCF11 matrix were used as probes in EMSA, and the results showed that the binding was specific to the sequence of the TCF11 matr...

  • abstract 500 dmp1 activates osteolytic cycle in a tumor environment
    Cancer Research, 2012
    Co-Authors: Asha S. Eapen, Anne George
    Abstract:

    Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL Bone metastasis is one of the skeletal malignancies that could be caused by breast cancer. Dentin matrix Protein 1 (DMP1) is an acidic Noncollagenous Protein localized specifically in the mineralized matrix of bone and dentin. It is a multifunctional Protein, involved in gene regulation (within the cell) and HAP nucleation (in the ECM). DMP1 is endocytosed by preosteoblasts, triggering the calcium dependent and calcium independent signaling pathways resulting in a series of downstream events leading to osteoblast differentiation. These signaling events facilitate the activation of a calcium dependent stress-induced p38 MAP kinase and a calcium independent integrin mediated ERK1/2 MAP kinase pathway resulting in the expression of downstream target genes such as Runx2 and osteocalcin. Results from this study have shown that the osteoblast cells upon differentiation secrete receptor activator of nuclear factor kappa B ligand (RANKL) that stimulates the differentiation of precursor monocytes to osteoclasts. The study also focuses on identifying the role of DMP1 in breast cancer cells that could enhance osteoclast formation thereby accelerating bone resportion. Thus, the study reveals a new mechanism by which DMP1 can activate the vicious cycle leading to the aggressive growth and behavior of the cancer cells. To address the mechanism by which DMP1 might contribute to the osteolytic process, DMP1 was overexpressed in the metastatic cancer cell line MDA MB231. Upregulation of markers like Runx2, MMP2, MMP9, RANKL, OPN, BSP, VEGF and the activation of Smad2/3 and MAP kinase pathways (p38 and ERK1/2 pathways) were observed in overexpressed cells. Results from this study have shown that DMP1 secreted by the breast cancer cells into the extracellular environment could stimulate the differentiation of osteoblasts, leading to the secretion of factors that signal monocytes to differentiate to osteoclast thus resulting in bone metastasis. Overall, the results obtained from this study identify a new role for DMP1 in the differentiation of breast cancer tumor cells that may be directly related to their metastatic potential. Supported by NIH DE 115657 and the Brodie Endowment Fund Citation Format: {Authors}. {Abstract title} [abstract]. In: Proceedings of the 103rd Annual Meeting of the American Association for Cancer Research; 2012 Mar 31-Apr 4; Chicago, IL. Philadelphia (PA): AACR; Cancer Res 2012;72(8 Suppl):Abstract nr 500. doi:1538-7445.AM2012-500

  • Dentin Matrix Protein 1 Immobilized on Type I Collagen Fibrils Facilitates Apatite Deposition in Vitro
    Journal of Biological Chemistry, 2003
    Co-Authors: He, Anne George
    Abstract:

    Abstract During bone and dentin mineralization, the crystal nucleation and growth processes are considered to be matrix regulated. Osteoblasts and odontoblasts synthesize a polymeric collagenous matrix, which forms a template for apatite initiation and elongation. Coordinated and controlled reaction between type I collagen and bone/dentin-specific Noncollagenous Proteins are necessary for well defined biogenic crystal formation. However, the process by which collagen surfaces become mineralized is not understood. Dentin matrix Protein 1 (DMP1) is an acidic Noncollagenous Protein expressed during the initial stages of mineralized matrix formation in bone and dentin. Here we show that DMP1 bound specifically to type I collagen, with the binding region located at the N-telopeptide region of type I collagen. Peptide mapping identified two acidic clusters in DMP1 responsible for interacting with type I collagen. The collagen binding property of these domains was further confirmed by site-directed mutagenesis. Transmission electron microscopy analyses have localized DMP1 in the gap region of the collagen fibrils. Fibrillogenesis assays further demonstrated that DMP1 accelerated the assembly of the collagen fibrils in vitro and also increased the diameter of the reconstituted collagen fibrils. In vitro mineralization studies in the presence of calcium and phosphate ions demonstrated apatite deposition only at the collagen-bound DMP1 sites. Thus specific binding of DMP1 and possibly other Noncollagenous Proteins on the collagen fibril might be a key step in collagen matrix organization and mineralization.

Seicho Makihira - One of the best experts on this subject based on the ideXlab platform.

  • enhancement of cell adhesion and spreading by a cartilage specific Noncollagenous Protein cartilage matrix Protein cmp matrilin 1 via integrin α1β1
    Journal of Biological Chemistry, 1999
    Co-Authors: Seicho Makihira, Shigeru Ohno, Takeshi Kawamoto, Katsumi Fujimoto, Akinobu Okimura, Eri Yoshida, Mitsuhide Noshiro, Taizo Hamada, Yukio Kato
    Abstract:

    Abstract Cartilage matrix Protein (CMP; also known as matrilin-1), one of the major Noncollagenous Proteins in most cartilages, binds to aggrecan and type II collagen. We examined the effect of CMP on the adhesion of chondrocytes and fibroblasts using CMP-coated dishes. The CMP coating at 10–20 μg/ml enhanced the adhesion and spreading of rabbit growth plate, resting and articular chondrocytes, and fibroblasts and human epiphyseal chondrocytes and MRC5 fibroblasts. The effect of CMP on the spreading of chondrocytes was synergistically increased by native, but not heated, type II collagen (gelatin). The monoclonal antibody to integrin α1 or β1 abolished CMP-induced cell adhesion and spreading, whereas the antibody to integrin α2, α3, α5, β2, α5β1, or αVβ5had little effect on cell adhesion or spreading. The antibody to integrin α1, but not to other subunits, coprecipitated125I-CMP that was added to MRC5 cell lysates, indicating the association of CMP with the integrin α1 subunit. Unlabeled CMP competed for the binding to integrin α1with 125I-CMP. These findings suggest that CMP is a potent adhesion factor for chondrocytes, particularly in the presence of type II collagen, and that integrin α1β1 is involved in CMP-mediated cell adhesion and spreading. Since CMP is expressed almost exclusively in cartilage, this adhesion factor, unlike fibronectin or laminin, may play a special role in the development and remodeling of cartilage.

  • Enhancement of Cell Adhesion and Spreading by a Cartilage-specific Noncollagenous Protein, Cartilage Matrix Protein (CMP/Matrilin-1), via Integrin α1β1
    Journal of Biological Chemistry, 1999
    Co-Authors: Seicho Makihira, Shigeru Ohno, Takeshi Kawamoto, Katsumi Fujimoto, Akinobu Okimura, Eri Yoshida, Mitsuhide Noshiro, Taizo Hamada, Yukio Kato
    Abstract:

    Abstract Cartilage matrix Protein (CMP; also known as matrilin-1), one of the major Noncollagenous Proteins in most cartilages, binds to aggrecan and type II collagen. We examined the effect of CMP on the adhesion of chondrocytes and fibroblasts using CMP-coated dishes. The CMP coating at 10–20 μg/ml enhanced the adhesion and spreading of rabbit growth plate, resting and articular chondrocytes, and fibroblasts and human epiphyseal chondrocytes and MRC5 fibroblasts. The effect of CMP on the spreading of chondrocytes was synergistically increased by native, but not heated, type II collagen (gelatin). The monoclonal antibody to integrin α1 or β1 abolished CMP-induced cell adhesion and spreading, whereas the antibody to integrin α2, α3, α5, β2, α5β1, or αVβ5had little effect on cell adhesion or spreading. The antibody to integrin α1, but not to other subunits, coprecipitated125I-CMP that was added to MRC5 cell lysates, indicating the association of CMP with the integrin α1 subunit. Unlabeled CMP competed for the binding to integrin α1with 125I-CMP. These findings suggest that CMP is a potent adhesion factor for chondrocytes, particularly in the presence of type II collagen, and that integrin α1β1 is involved in CMP-mediated cell adhesion and spreading. Since CMP is expressed almost exclusively in cartilage, this adhesion factor, unlike fibronectin or laminin, may play a special role in the development and remodeling of cartilage.

Taizo Hamada - One of the best experts on this subject based on the ideXlab platform.

  • enhancement of cell adhesion and spreading by a cartilage specific Noncollagenous Protein cartilage matrix Protein cmp matrilin 1 via integrin α1β1
    Journal of Biological Chemistry, 1999
    Co-Authors: Seicho Makihira, Shigeru Ohno, Takeshi Kawamoto, Katsumi Fujimoto, Akinobu Okimura, Eri Yoshida, Mitsuhide Noshiro, Taizo Hamada, Yukio Kato
    Abstract:

    Abstract Cartilage matrix Protein (CMP; also known as matrilin-1), one of the major Noncollagenous Proteins in most cartilages, binds to aggrecan and type II collagen. We examined the effect of CMP on the adhesion of chondrocytes and fibroblasts using CMP-coated dishes. The CMP coating at 10–20 μg/ml enhanced the adhesion and spreading of rabbit growth plate, resting and articular chondrocytes, and fibroblasts and human epiphyseal chondrocytes and MRC5 fibroblasts. The effect of CMP on the spreading of chondrocytes was synergistically increased by native, but not heated, type II collagen (gelatin). The monoclonal antibody to integrin α1 or β1 abolished CMP-induced cell adhesion and spreading, whereas the antibody to integrin α2, α3, α5, β2, α5β1, or αVβ5had little effect on cell adhesion or spreading. The antibody to integrin α1, but not to other subunits, coprecipitated125I-CMP that was added to MRC5 cell lysates, indicating the association of CMP with the integrin α1 subunit. Unlabeled CMP competed for the binding to integrin α1with 125I-CMP. These findings suggest that CMP is a potent adhesion factor for chondrocytes, particularly in the presence of type II collagen, and that integrin α1β1 is involved in CMP-mediated cell adhesion and spreading. Since CMP is expressed almost exclusively in cartilage, this adhesion factor, unlike fibronectin or laminin, may play a special role in the development and remodeling of cartilage.

  • Enhancement of Cell Adhesion and Spreading by a Cartilage-specific Noncollagenous Protein, Cartilage Matrix Protein (CMP/Matrilin-1), via Integrin α1β1
    Journal of Biological Chemistry, 1999
    Co-Authors: Seicho Makihira, Shigeru Ohno, Takeshi Kawamoto, Katsumi Fujimoto, Akinobu Okimura, Eri Yoshida, Mitsuhide Noshiro, Taizo Hamada, Yukio Kato
    Abstract:

    Abstract Cartilage matrix Protein (CMP; also known as matrilin-1), one of the major Noncollagenous Proteins in most cartilages, binds to aggrecan and type II collagen. We examined the effect of CMP on the adhesion of chondrocytes and fibroblasts using CMP-coated dishes. The CMP coating at 10–20 μg/ml enhanced the adhesion and spreading of rabbit growth plate, resting and articular chondrocytes, and fibroblasts and human epiphyseal chondrocytes and MRC5 fibroblasts. The effect of CMP on the spreading of chondrocytes was synergistically increased by native, but not heated, type II collagen (gelatin). The monoclonal antibody to integrin α1 or β1 abolished CMP-induced cell adhesion and spreading, whereas the antibody to integrin α2, α3, α5, β2, α5β1, or αVβ5had little effect on cell adhesion or spreading. The antibody to integrin α1, but not to other subunits, coprecipitated125I-CMP that was added to MRC5 cell lysates, indicating the association of CMP with the integrin α1 subunit. Unlabeled CMP competed for the binding to integrin α1with 125I-CMP. These findings suggest that CMP is a potent adhesion factor for chondrocytes, particularly in the presence of type II collagen, and that integrin α1β1 is involved in CMP-mediated cell adhesion and spreading. Since CMP is expressed almost exclusively in cartilage, this adhesion factor, unlike fibronectin or laminin, may play a special role in the development and remodeling of cartilage.

Mitsuhide Noshiro - One of the best experts on this subject based on the ideXlab platform.

  • enhancement of cell adhesion and spreading by a cartilage specific Noncollagenous Protein cartilage matrix Protein cmp matrilin 1 via integrin α1β1
    Journal of Biological Chemistry, 1999
    Co-Authors: Seicho Makihira, Shigeru Ohno, Takeshi Kawamoto, Katsumi Fujimoto, Akinobu Okimura, Eri Yoshida, Mitsuhide Noshiro, Taizo Hamada, Yukio Kato
    Abstract:

    Abstract Cartilage matrix Protein (CMP; also known as matrilin-1), one of the major Noncollagenous Proteins in most cartilages, binds to aggrecan and type II collagen. We examined the effect of CMP on the adhesion of chondrocytes and fibroblasts using CMP-coated dishes. The CMP coating at 10–20 μg/ml enhanced the adhesion and spreading of rabbit growth plate, resting and articular chondrocytes, and fibroblasts and human epiphyseal chondrocytes and MRC5 fibroblasts. The effect of CMP on the spreading of chondrocytes was synergistically increased by native, but not heated, type II collagen (gelatin). The monoclonal antibody to integrin α1 or β1 abolished CMP-induced cell adhesion and spreading, whereas the antibody to integrin α2, α3, α5, β2, α5β1, or αVβ5had little effect on cell adhesion or spreading. The antibody to integrin α1, but not to other subunits, coprecipitated125I-CMP that was added to MRC5 cell lysates, indicating the association of CMP with the integrin α1 subunit. Unlabeled CMP competed for the binding to integrin α1with 125I-CMP. These findings suggest that CMP is a potent adhesion factor for chondrocytes, particularly in the presence of type II collagen, and that integrin α1β1 is involved in CMP-mediated cell adhesion and spreading. Since CMP is expressed almost exclusively in cartilage, this adhesion factor, unlike fibronectin or laminin, may play a special role in the development and remodeling of cartilage.

  • Enhancement of Cell Adhesion and Spreading by a Cartilage-specific Noncollagenous Protein, Cartilage Matrix Protein (CMP/Matrilin-1), via Integrin α1β1
    Journal of Biological Chemistry, 1999
    Co-Authors: Seicho Makihira, Shigeru Ohno, Takeshi Kawamoto, Katsumi Fujimoto, Akinobu Okimura, Eri Yoshida, Mitsuhide Noshiro, Taizo Hamada, Yukio Kato
    Abstract:

    Abstract Cartilage matrix Protein (CMP; also known as matrilin-1), one of the major Noncollagenous Proteins in most cartilages, binds to aggrecan and type II collagen. We examined the effect of CMP on the adhesion of chondrocytes and fibroblasts using CMP-coated dishes. The CMP coating at 10–20 μg/ml enhanced the adhesion and spreading of rabbit growth plate, resting and articular chondrocytes, and fibroblasts and human epiphyseal chondrocytes and MRC5 fibroblasts. The effect of CMP on the spreading of chondrocytes was synergistically increased by native, but not heated, type II collagen (gelatin). The monoclonal antibody to integrin α1 or β1 abolished CMP-induced cell adhesion and spreading, whereas the antibody to integrin α2, α3, α5, β2, α5β1, or αVβ5had little effect on cell adhesion or spreading. The antibody to integrin α1, but not to other subunits, coprecipitated125I-CMP that was added to MRC5 cell lysates, indicating the association of CMP with the integrin α1 subunit. Unlabeled CMP competed for the binding to integrin α1with 125I-CMP. These findings suggest that CMP is a potent adhesion factor for chondrocytes, particularly in the presence of type II collagen, and that integrin α1β1 is involved in CMP-mediated cell adhesion and spreading. Since CMP is expressed almost exclusively in cartilage, this adhesion factor, unlike fibronectin or laminin, may play a special role in the development and remodeling of cartilage.