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  1. Article: A bit of give and take: the relationship between the extracellular matrix and the developing chondrocyte.

    Behonick, Danielle J / Werb, Zena

    Mechanisms of development

    2003  Volume 120, Issue 11, Page(s) 1327–1336

    Abstract: The extracellular matrix (ECM), once thought to be a static structural component of tissues, is now known to play a complex and dynamic role in a variety of cellular functions in a number of diverse tissues. A significant body of literature attests to ... ...

    Abstract The extracellular matrix (ECM), once thought to be a static structural component of tissues, is now known to play a complex and dynamic role in a variety of cellular functions in a number of diverse tissues. A significant body of literature attests to the ability of the ECM to communicate both spatial and temporal information to adherent cells, thereby directing cell behavior via interactions between the ECM and cell-surface receptors. Moreover, volumes of experimental data show that a great deal of communication travels in the opposite direction, from the cell to the ECM, allowing for regulation of the cues transmitted by the ECM. As such, the ECM, with respect to its components and their organization, is not a fixed reflection of the state the local microenvironment in which a cell finds itself at a particular time, but rather is able to respond to and effect changes in its local microenvironment. As an example of the developmental consequences of ECM interactions, this review gives an overview of the 'give and take' relationship between the ECM and the cells of the developing skeletal elements, in particular, the chondrocyte.
    MeSH term(s) Animals ; Bone and Bones/pathology ; Cell Adhesion ; Cell Communication ; Cell Membrane/metabolism ; Chondrocytes/metabolism ; Extracellular Matrix/metabolism ; Gene Expression Regulation, Developmental ; Mesoderm/cytology ; Models, Biological ; Osteoblasts/metabolism ; Time Factors
    Language English
    Publishing date 2003-11
    Publishing country Ireland
    Document type Journal Article ; Research Support, U.S. Gov't, P.H.S. ; Review
    ZDB-ID 1055986-3
    ISSN 1872-6356 ; 0925-4773
    ISSN (online) 1872-6356
    ISSN 0925-4773
    DOI 10.1016/j.mod.2003.05.002
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  2. Article: Matrix remodeling during endochondral ossification.

    Ortega, Nathalie / Behonick, Danielle J / Werb, Zena

    Trends in cell biology

    2004  Volume 14, Issue 2, Page(s) 86–93

    Abstract: Endochondral ossification, the process by which most of the skeleton is formed, is a powerful system for studying various aspects of the biological response to degraded extracellular matrix (ECM). In addition, the dependence of endochondral ossification ... ...

    Abstract Endochondral ossification, the process by which most of the skeleton is formed, is a powerful system for studying various aspects of the biological response to degraded extracellular matrix (ECM). In addition, the dependence of endochondral ossification upon neovascularization and continuous ECM remodeling provides a good model for studying the role of the matrix metalloproteases (MMPs) not only as simple effectors of ECM degradation but also as regulators of active signal-inducers for the initiation of endochondral ossification. The daunting task of elucidating their specific role during endochondral ossification has been facilitated by the development of mice deficient for various members of this family. Here, we discuss the ECM and its remodeling as one level of molecular regulation for the process of endochondral ossification, with special attention to the MMPs.
    MeSH term(s) Animals ; Bone and Bones/blood supply ; Bone and Bones/cytology ; Bone and Bones/metabolism ; Cartilage/cytology ; Cartilage/growth & development ; Cartilage/metabolism ; Cell Differentiation/physiology ; Chondrocytes/cytology ; Chondrocytes/metabolism ; Extracellular Matrix/metabolism ; Humans ; Matrix Metalloproteinases/metabolism ; Neovascularization, Physiologic/physiology ; Osteogenesis/physiology
    Chemical Substances Matrix Metalloproteinases (EC 3.4.24.-)
    Language English
    Publishing date 2004-02
    Publishing country England
    Document type Journal Article ; Research Support, U.S. Gov't, P.H.S. ; Review
    ZDB-ID 30122-x
    ISSN 1879-3088 ; 0962-8924
    ISSN (online) 1879-3088
    ISSN 0962-8924
    DOI 10.1016/j.tcb.2003.12.003
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  3. Article: Galectin-3 is a downstream regulator of matrix metalloproteinase-9 function during endochondral bone formation.

    Ortega, Nathalie / Behonick, Danielle J / Colnot, Céline / Cooper, Douglas N W / Werb, Zena

    Molecular biology of the cell

    2005  Volume 16, Issue 6, Page(s) 3028–3039

    Abstract: Endochondral bone formation is characterized by the progressive replacement of a cartilage anlagen by bone at the growth plate with a tight balance between the rates of chondrocyte proliferation, differentiation, and cell death. Deficiency of matrix ... ...

    Abstract Endochondral bone formation is characterized by the progressive replacement of a cartilage anlagen by bone at the growth plate with a tight balance between the rates of chondrocyte proliferation, differentiation, and cell death. Deficiency of matrix metalloproteinase-9 (MMP-9) leads to an accumulation of late hypertrophic chondrocytes. We found that galectin-3, an in vitro substrate of MMP-9, accumulates in the late hypertrophic chondrocytes and their surrounding extracellular matrix in the expanded hypertrophic cartilage zone. Treatment of wild-type embryonic metatarsals in culture with full-length galectin-3, but not galectin-3 cleaved by MMP-9, mimicked the embryonic phenotype of Mmp-9 null mice, with an increased hypertrophic zone and decreased osteoclast recruitment. These results indicate that extracellular galectin-3 could be an endogenous substrate of MMP-9 that acts downstream to regulate hypertrophic chondrocyte death and osteoclast recruitment during endochondral bone formation. Thus, the disruption of growth plate homeostasis in Mmp-9 null mice links galectin-3 and MMP-9 in the regulation of the clearance of late chondrocytes through regulation of their terminal differentiation.
    MeSH term(s) Animals ; Blotting, Western ; Bone Development ; Bone and Bones/cytology ; Bone and Bones/enzymology ; Bone and Bones/metabolism ; Cell Differentiation ; Cells, Cultured ; Chondrocytes/metabolism ; Extracellular Matrix/metabolism ; Galectin 3/metabolism ; Growth Plate/cytology ; Growth Plate/embryology ; Growth Plate/growth & development ; Growth Plate/metabolism ; Humerus/cytology ; Humerus/embryology ; Immunohistochemistry ; In Situ Hybridization ; Matrix Metalloproteinase 9/metabolism ; Metatarsal Bones/cytology ; Metatarsal Bones/embryology ; Mice ; Mice, Mutant Strains ; Platelet Endothelial Cell Adhesion Molecule-1/metabolism
    Chemical Substances Galectin 3 ; Platelet Endothelial Cell Adhesion Molecule-1 ; Matrix Metalloproteinase 9 (EC 3.4.24.35)
    Language English
    Publishing date 2005-06
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
    ZDB-ID 1098979-1
    ISSN 1939-4586 ; 1059-1524
    ISSN (online) 1939-4586
    ISSN 1059-1524
    DOI 10.1091/mbc.E04-12-1119
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  4. Article ; Online: Role of matrix metalloproteinase 13 in both endochondral and intramembranous ossification during skeletal regeneration.

    Behonick, Danielle J / Xing, Zhiqing / Lieu, Shirley / Buckley, Jenni M / Lotz, Jeffrey C / Marcucio, Ralph S / Werb, Zena / Miclau, Theodore / Colnot, Céline

    PloS one

    2007  Volume 2, Issue 11, Page(s) e1150

    Abstract: Extracellular matrix (ECM) remodeling is important during bone development and repair. Because matrix metalloproteinase 13 (MMP13, collagenase-3) plays a role in long bone development, we have examined its role during adult skeletal repair. In this study ...

    Abstract Extracellular matrix (ECM) remodeling is important during bone development and repair. Because matrix metalloproteinase 13 (MMP13, collagenase-3) plays a role in long bone development, we have examined its role during adult skeletal repair. In this study we find that MMP13 is expressed by hypertrophic chondrocytes and osteoblasts in the fracture callus. We demonstrate that MMP13 is required for proper resorption of hypertrophic cartilage and for normal bone remodeling during non-stabilized fracture healing, which occurs via endochondral ossification. However, no difference in callus strength was detected in the absence of MMP13. Transplant of wild-type bone marrow, which reconstitutes cells only of the hematopoietic lineage, did not rescue the endochondral repair defect, indicating that impaired healing in Mmp13-/- mice is intrinsic to cartilage and bone. Mmp13-/- mice also exhibited altered bone remodeling during healing of stabilized fractures and cortical defects via intramembranous ossification. This indicates that the bone phenotype occurs independently from the cartilage phenotype. Taken together, our findings demonstrate that MMP13 is involved in normal remodeling of bone and cartilage during adult skeletal repair, and that MMP13 may act directly in the initial stages of ECM degradation in these tissues prior to invasion of blood vessels and osteoclasts.
    MeSH term(s) Animals ; Bone Regeneration ; Fracture Healing ; Matrix Metalloproteinase 13/genetics ; Matrix Metalloproteinase 13/metabolism ; Mice ; Mice, Knockout ; Osteogenesis
    Chemical Substances Matrix Metalloproteinase 13 (EC 3.4.24.-) ; Mmp13 protein, mouse (EC 3.4.24.-)
    Language English
    Publishing date 2007-11-07
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ISSN 1932-6203
    ISSN (online) 1932-6203
    DOI 10.1371/journal.pone.0001150
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  5. Article: Type I collagen is a genetic modifier of matrix metalloproteinase 2 in murine skeletal development.

    Egeblad, Mikala / Shen, H-C Jennifer / Behonick, Danielle J / Wilmes, Lisa / Eichten, Alexandra / Korets, Lidiya V / Kheradmand, Farrah / Werb, Zena / Coussens, Lisa M

    Developmental dynamics : an official publication of the American Association of Anatomists

    2007  Volume 236, Issue 6, Page(s) 1683–1693

    Abstract: Recessive inactivating mutations in human matrix metalloproteinase 2 (MMP2, gelatinase A) are associated with syndromes that include abnormal facial appearance, short stature, and severe bone loss. Mmp2(-/-) mice have only mild aspects of these ... ...

    Abstract Recessive inactivating mutations in human matrix metalloproteinase 2 (MMP2, gelatinase A) are associated with syndromes that include abnormal facial appearance, short stature, and severe bone loss. Mmp2(-/-) mice have only mild aspects of these abnormalities, suggesting that MMP2 function is redundant during skeletal development in the mouse. Here, we report that Mmp2(-/-) mice with additional mutations that render type I collagen resistant to collagenase-mediated cleavage to TC(A) and TC(B) fragments (Col1a1(r/r) mice) have severe developmental defects resembling those observed in MMP2-null humans. Composite Mmp2(-/-);Col1a1(r/r) mice were born in expected Mendelian ratios but were half the size of wild-type, Mmp2(-/-), and Col1a1(r/r) mice and failed to thrive. Furthermore, composite Mmp2(-/-);Col1a1(r/r) animals had very abnormal craniofacial features with shorter snouts, bulging skulls, incompletely developed calvarial bones and unclosed cranial sutures. In addition, trabecular bone mass was reduced concomitant with increased numbers of bone-resorbing osteoclasts and osteopenia. In vitro, MMP2 had a unique ability among the collagenolytic MMPs to degrade mutant collagen, offering a possible explanation for the genetic interaction between Mmp2 and Col1a1(r). Thus, because mutations in the type I collagen gene alter the phenotype of mice with null mutations in Mmp2, we conclude that type I collagen is an important modifier gene for Mmp2. Developmental Dynamics 236:1683-1693, 2007. (c) 2007 Wiley-Liss, Inc.
    MeSH term(s) Animals ; Bone Density ; Bone Diseases, Metabolic/genetics ; Bone Diseases, Metabolic/metabolism ; Bone Diseases, Metabolic/pathology ; Bone and Bones/metabolism ; Collagen Type I/metabolism ; Craniofacial Abnormalities ; Edema/genetics ; Edema/metabolism ; Edema/pathology ; Gene Expression Regulation, Developmental ; Humans ; Joints/abnormalities ; Joints/metabolism ; Matrix Metalloproteinase 2/deficiency ; Matrix Metalloproteinase 2/genetics ; Matrix Metalloproteinase 2/metabolism ; Mice ; Mice, Transgenic
    Chemical Substances Collagen Type I ; Matrix Metalloproteinase 2 (EC 3.4.24.24)
    Language English
    Publishing date 2007-06
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 1102541-4
    ISSN 1097-0177 ; 1058-8388
    ISSN (online) 1097-0177
    ISSN 1058-8388
    DOI 10.1002/dvdy.21159
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  6. Article ; Online: Role of matrix metalloproteinase 13 in both endochondral and intramembranous ossification during skeletal regeneration.

    Danielle J Behonick / Zhiqing Xing / Shirley Lieu / Jenni M Buckley / Jeffrey C Lotz / Ralph S Marcucio / Zena Werb / Theodore Miclau / Céline Colnot

    PLoS ONE, Vol 2, Iss 11, p e

    2007  Volume 1150

    Abstract: Extracellular matrix (ECM) remodeling is important during bone development and repair. Because matrix metalloproteinase 13 (MMP13, collagenase-3) plays a role in long bone development, we have examined its role during adult skeletal repair. In this study ...

    Abstract Extracellular matrix (ECM) remodeling is important during bone development and repair. Because matrix metalloproteinase 13 (MMP13, collagenase-3) plays a role in long bone development, we have examined its role during adult skeletal repair. In this study we find that MMP13 is expressed by hypertrophic chondrocytes and osteoblasts in the fracture callus. We demonstrate that MMP13 is required for proper resorption of hypertrophic cartilage and for normal bone remodeling during non-stabilized fracture healing, which occurs via endochondral ossification. However, no difference in callus strength was detected in the absence of MMP13. Transplant of wild-type bone marrow, which reconstitutes cells only of the hematopoietic lineage, did not rescue the endochondral repair defect, indicating that impaired healing in Mmp13-/- mice is intrinsic to cartilage and bone. Mmp13-/- mice also exhibited altered bone remodeling during healing of stabilized fractures and cortical defects via intramembranous ossification. This indicates that the bone phenotype occurs independently from the cartilage phenotype. Taken together, our findings demonstrate that MMP13 is involved in normal remodeling of bone and cartilage during adult skeletal repair, and that MMP13 may act directly in the initial stages of ECM degradation in these tissues prior to invasion of blood vessels and osteoclasts.
    Keywords Medicine ; R ; Science ; Q
    Subject code 616
    Language English
    Publishing date 2007-11-01T00:00:00Z
    Publisher Public Library of Science (PLoS)
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  7. Article: Altered endochondral bone development in matrix metalloproteinase 13-deficient mice.

    Stickens, Dominique / Behonick, Danielle J / Ortega, Nathalie / Heyer, Babette / Hartenstein, Bettina / Yu, Ying / Fosang, Amanda J / Schorpp-Kistner, Marina / Angel, Peter / Werb, Zena

    Development (Cambridge, England)

    2004  Volume 131, Issue 23, Page(s) 5883–5895

    Abstract: The assembly and degradation of extracellular matrix (ECM) molecules are crucial processes during bone development. In this study, we show that ECM remodeling is a critical rate-limiting step in endochondral bone formation. Matrix metalloproteinase (MMP) ...

    Abstract The assembly and degradation of extracellular matrix (ECM) molecules are crucial processes during bone development. In this study, we show that ECM remodeling is a critical rate-limiting step in endochondral bone formation. Matrix metalloproteinase (MMP) 13 (collagenase 3) is poised to play a crucial role in bone formation and remodeling because of its expression both in terminal hypertrophic chondrocytes in the growth plate and in osteoblasts. Moreover, a mutation in the human MMP13 gene causes the Missouri variant of spondyloepimetaphyseal dysplasia. Inactivation of Mmp13 in mice through homologous recombination led to abnormal skeletal growth plate development. Chondrocytes differentiated normally but their exit from the growth plate was delayed. The severity of the Mmp13- null growth plate phenotype increased until about 5 weeks and completely resolved by 12 weeks of age. Mmp13-null mice had increased trabecular bone, which persisted for months. Conditional inactivation of Mmp13 in chondrocytes and osteoblasts showed that increases in trabecular bone occur independently of the improper cartilage ECM degradation caused by Mmp13 deficiency in late hypertrophic chondrocytes. Our studies identified the two major components of the cartilage ECM, collagen type II and aggrecan, as in vivo substrates for MMP13. We found that degradation of cartilage collagen and aggrecan is a coordinated process in which MMP13 works synergistically with MMP9. Mice lacking both MMP13 and MMP9 had severely impaired endochondral bone, characterized by diminished ECM remodeling, prolonged chondrocyte survival, delayed vascular recruitment and defective trabecular bone formation (resulting in drastically shortened bones). These data support the hypothesis that proper ECM remodeling is the dominant rate-limiting process for programmed cell death, angiogenesis and osteoblast recruitment during normal skeletal morphogenesis.
    MeSH term(s) Animals ; Bone Development ; Bone and Bones/abnormalities ; Bone and Bones/enzymology ; Bone and Bones/metabolism ; Bromodeoxyuridine/pharmacology ; Cartilage/metabolism ; Cell Differentiation ; Cells, Cultured ; Chondrocytes/metabolism ; Collagenases/genetics ; Collagenases/metabolism ; Collagenases/physiology ; Extracellular Matrix/metabolism ; Humans ; Immunohistochemistry ; In Situ Hybridization ; Matrix Metalloproteinase 13 ; Matrix Metalloproteinase 9/metabolism ; Mice ; Models, Genetic ; Mutation ; Neovascularization, Pathologic ; Phenotype ; Recombination, Genetic ; Time Factors ; Tomography, X-Ray Computed ; Transgenes
    Chemical Substances Collagenases (EC 3.4.24.-) ; MMP13 protein, human (EC 3.4.24.-) ; Matrix Metalloproteinase 13 (EC 3.4.24.-) ; Mmp13 protein, mouse (EC 3.4.24.-) ; Matrix Metalloproteinase 9 (EC 3.4.24.35) ; Bromodeoxyuridine (G34N38R2N1)
    Language English
    Publishing date 2004-04-30
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
    ZDB-ID 90607-4
    ISSN 1477-9129 ; 0950-1991
    ISSN (online) 1477-9129
    ISSN 0950-1991
    DOI 10.1242/dev.01461
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  8. Article: Gene therapy of prostate cancer with the soluble vascular endothelial growth factor receptor Flk1.

    Becker, Christian M / Farnebo, Filip A / Iordanescu, Irina / Behonick, Danielle J / Shih, Mei-Chiung / Dunning, Patricia / Christofferson, Rolf / Mulligan, Richard C / Taylor, George A / Kuo, Calvin J / Zetter, Bruce R

    Cancer biology & therapy

    2002  Volume 1, Issue 5, Page(s) 548–553

    Abstract: A variety of novel therapeutic approaches have emerged recently for the treatment of human cancers. We have coupled two of these therapeutic approaches, gene therapy and antiangiogenic therapy and tested them in two murine prostate cancer models ... ...

    Abstract A variety of novel therapeutic approaches have emerged recently for the treatment of human cancers. We have coupled two of these therapeutic approaches, gene therapy and antiangiogenic therapy and tested them in two murine prostate cancer models Recombinant adenovirus encoding the ligand-binding ectodomain of the VEGF receptor 2 (Flk1) fused to an Fc domain was administered to SCID mice carrying orthotopic human LNCaP tumors as well as to transgenic (TRAMP) mice with spontaneous prostate tumors. Ad Flk1-Fc injection reduced tumor growth by 66% for orthotopic LNCaP tumors and by 42% for spontaneous tumors in TRAMP mice. Microvessel density in the primary tumors was reduced by 68% and 40% in the two models respectively. A decrease in microvessel density was also observed in lymphatic metastases in Ad Flk1-Fc-treated TRAMP mice and was correlated with a decrease in the frequency of regional metastases in the treated animals. Survival time was also extended in the Ad Flk1-Fc-treated TRAMP mice relative to the control-treated animals. Our results suggest that adenoviral delivery of soluble Flk1 receptor can reduce vascular density and prostate tumor growth and prolong survival time in orthotopically implanted tumors as well as in spontaneous prostate tumors in transgenic animals.
    MeSH term(s) Adenoviridae/genetics ; Animals ; Cell Line ; Cell Transplantation ; Gene Transfer Techniques ; Genetic Therapy/methods ; Humans ; Kinetics ; Lymphatic Metastasis ; Male ; Mice ; Mice, SCID ; Mice, Transgenic ; Neovascularization, Pathologic/drug therapy ; Neovascularization, Pathologic/genetics ; Neovascularization, Pathologic/metabolism ; Prostate-Specific Antigen/blood ; Prostatic Neoplasms/genetics ; Prostatic Neoplasms/metabolism ; Prostatic Neoplasms/therapy ; Receptors, Fc/genetics ; Recombinant Fusion Proteins/metabolism ; Transplantation, Heterologous ; Vascular Endothelial Growth Factor Receptor-2/genetics
    Chemical Substances Receptors, Fc ; Recombinant Fusion Proteins ; Vascular Endothelial Growth Factor Receptor-2 (EC 2.7.10.1) ; Prostate-Specific Antigen (EC 3.4.21.77)
    Language English
    Publishing date 2002-12-20
    Publishing country United States
    Document type Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
    ZDB-ID 2146305-0
    ISSN 1538-4047
    ISSN 1538-4047
    DOI 10.4161/cbt.1.5.176
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