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  • 11
    Online-Ressource
    Online-Ressource
    Promoting Neuronal Outgrowth Using Ridged Scaffolds Coated with Extracellular Matrix Proteins
    MDPI AG ; 2021
    In:  Biomedicines Vol. 9, No. 5 ( 2021-04-27), p. 479-
    Details
    In: Biomedicines, MDPI AG, Vol. 9, No. 5 ( 2021-04-27), p. 479-
    Kurzfassung: Spinal cord injury (SCI) results in cell death, demyelination, and axonal loss. The spinal cord has a limited ability to regenerate, and current clinical therapies for SCI are not effective in helping promote neurologic recovery. We have developed a novel scaffold biomaterial that is fabricated from the biodegradable hydrogel oligo(poly(ethylene glycol)fumarate) (OPF). We have previously shown that positively charged OPF scaffolds (OPF+) in an open spaced, multichannel design can be loaded with Schwann cells to support axonal generation and functional recovery following SCI. We have now developed a hybrid OPF+ biomaterial that increases the surface area available for cell attachment and that contains an aligned microarchitecture and extracellular matrix (ECM) proteins to better support axonal regeneration. OPF+ was fabricated as 0.08 mm thick sheets containing 100 μm high polymer ridges that self-assemble into a spiral shape when hydrated. Laminin, fibronectin, or collagen I coating promoted neuron attachment and axonal outgrowth on the scaffold surface. In addition, the ridges aligned axons in a longitudinal bipolar orientation. Decreasing the space between the ridges increased the number of cells and neurites aligned in the direction of the ridge. Schwann cells seeded on laminin coated OPF+ sheets aligned along the ridges over a 6-day period and could myelinate dorsal root ganglion neurons over 4 weeks. This novel scaffold design, with closer spaced ridges and Schwann cells, is a novel biomaterial construct to promote regeneration after SCI.
    Materialart: Online-Ressource
    ISSN: 2227-9059
    URL: Article
    DOI: 10.3390/biomedicines9050479
    Sprache: Englisch
    Verlag: MDPI AG
    Publikationsdatum: 2021
    ZDB Id: 2720867-9
    Standort Signatur Einschränkungen Verfügbarkeit
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    Online-Ressource
  • 12
    Online-Ressource
    Online-Ressource
    Nucleation of fibronectin fibril assembly requires binding between heparin and the 13th type III module of fibronectin
    Elsevier BV ; 2023
    In:  Journal of Biological Chemistry Vol. 299, No. 5 ( 2023-05), p. 104622-
    Details
    In: Journal of Biological Chemistry, Elsevier BV, Vol. 299, No. 5 ( 2023-05), p. 104622-
    Materialart: Online-Ressource
    ISSN: 0021-9258
    URL: Article
    DOI: 10.1016/j.jbc.2023.104622
    Sprache: Englisch
    Verlag: Elsevier BV
    Publikationsdatum: 2023
    ZDB Id: 2141744-1
    ZDB Id: 1474604-9
    SSG: 12
    Standort Signatur Einschränkungen Verfügbarkeit
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    Online-Ressource
  • 13
    Online-Ressource
    Online-Ressource
    Tetraspanin Proteins Regulate Membrane Type-1 Matrix Metalloproteinase-dependent Pericellular Proteolysis
    American Society for Cell Biology (ASCB) ; 2009
    In:  Molecular Biology of the Cell Vol. 20, No. 7 ( 2009-04), p. 2030-2040
    Details
    In: Molecular Biology of the Cell, American Society for Cell Biology (ASCB), Vol. 20, No. 7 ( 2009-04), p. 2030-2040
    Kurzfassung: Membrane type-1 matrix metalloproteinase (MT1-MMP) supports tumor cell invasion through extracellular matrix barriers containing fibrin, collagen, fibronectin, and other proteins. Here, we show that simultaneous knockdown of two or three members of the tetraspanin family (CD9, CD81, and TSPAN12) markedly decreases MT1-MMP proteolytic functions in cancer cells. Affected functions include fibronectin proteolysis, invasion and growth in three-dimensional fibrin and collagen gels, and MMP-2 activation. Tetraspanin proteins (CD9, CD81, and TSPAN2) selectively coimmunoprecipitate and colocalize with MT1-MMP. Although tetraspanins do not affect the initial biosynthesis of MT1-MMP, they do protect the newly synthesized protein from lysosomal degradation and support its delivery to the cell surface. Interfering with MT1-MMP-tetraspanin collaboration may be a useful therapeutic approach to limit cancer cell invasion and metastasis.
    Materialart: Online-Ressource
    ISSN: 1059-1524 , 1939-4586
    URL: Article
    DOI: 10.1091/mbc.e08-11-1149
    Sprache: Englisch
    Verlag: American Society for Cell Biology (ASCB)
    Publikationsdatum: 2009
    ZDB Id: 1474922-1
    SSG: 12
    Standort Signatur Einschränkungen Verfügbarkeit
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    Online-Ressource
  • 14
    Online-Ressource
    Online-Ressource
    Integrin-mediated Protein Kinase A Activation at the Leading Edge of Migrating Cells
    American Society for Cell Biology (ASCB) ; 2008
    In:  Molecular Biology of the Cell Vol. 19, No. 11 ( 2008-11), p. 4930-4941
    Details
    In: Molecular Biology of the Cell, American Society for Cell Biology (ASCB), Vol. 19, No. 11 ( 2008-11), p. 4930-4941
    Kurzfassung: cAMP-dependent protein kinase A (PKA) is important in processes requiring localized cell protrusion, such as cell migration and axonal path finding. Here, we used a membrane-targeted PKA biosensor to reveal activation of PKA at the leading edge of migrating cells. Previous studies show that PKA activity promotes protrusion and efficient cell migration. In live migrating cells, membrane-associated PKA activity was highest at the leading edge and required ligation of integrins such as α4β1 or α5β1 and an intact actin cytoskeleton. α4 integrins are type I PKA-specific A-kinase anchoring proteins, and we now find that type I PKA is important for localization of α4β1 integrin-mediated PKA activation at the leading edge. Accumulation of 3′ phosphorylated phosphoinositides [PtdIns(3,4,5)P 3 ] products of phosphatidylinositol 3-kinase (PI3-kinase) is an early event in establishing the directionality of migration; however, polarized PKA activation did not require PI3-kinase activity. Conversely, inhibition of PKA blocked accumulation of a PtdIns(3,4,5)P 3 -binding protein, the AKT-pleckstrin homology (PH) domain, at the leading edge; hence, PKA is involved in maintaining cell polarity during migration. In sum, we have visualized compartment-specific PKA activation in migrating cells and used it to reveal that adhesion-mediated localized activation of PKA is an early step in directional cell migration.
    Materialart: Online-Ressource
    ISSN: 1059-1524 , 1939-4586
    URL: Article
    DOI: 10.1091/mbc.e08-06-0564
    Sprache: Englisch
    Verlag: American Society for Cell Biology (ASCB)
    Publikationsdatum: 2008
    ZDB Id: 1474922-1
    SSG: 12
    Standort Signatur Einschränkungen Verfügbarkeit
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    Online-Ressource
  • 15
    Online-Ressource
    Online-Ressource
    Elevated glucose alters global gene expression and tenascin-C alternative splicing in mesangial cells
    Elsevier BV ; 2020
    In:  Matrix Biology Plus Vol. 8 ( 2020-11), p. 100048-
    Details
    In: Matrix Biology Plus, Elsevier BV, Vol. 8 ( 2020-11), p. 100048-
    Materialart: Online-Ressource
    ISSN: 2590-0285
    URL: Article
    DOI: 10.1016/j.mbplus.2020.100048
    Sprache: Englisch
    Verlag: Elsevier BV
    Publikationsdatum: 2020
    ZDB Id: 2976377-0
    Standort Signatur Einschränkungen Verfügbarkeit
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    Online-Ressource
  • 16
    Online-Ressource
    Online-Ressource
    Modulation of Cell–Fibronectin Matrix Interactions during Tissue Repair
    Elsevier BV ; 2006
    In:  Journal of Investigative Dermatology Symposium Proceedings Vol. 11, No. 1 ( 2006-09), p. 73-78
    Details
    In: Journal of Investigative Dermatology Symposium Proceedings, Elsevier BV, Vol. 11, No. 1 ( 2006-09), p. 73-78
    Materialart: Online-Ressource
    ISSN: 1087-0024
    URL: Article
    DOI: 10.1038/sj.jidsymp.5650005
    Sprache: Englisch
    Verlag: Elsevier BV
    Publikationsdatum: 2006
    ZDB Id: 2041664-7
    Standort Signatur Einschränkungen Verfügbarkeit
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    Online-Ressource
  • 17
    Online-Ressource
    Online-Ressource
    Differential targeting of recombinant fibronectins in AtT-20 cells based on their efficiency of aggregation
    The Company of Biologists ; 1995
    In:  Journal of Cell Science Vol. 108, No. 12 ( 1995-12-01), p. 3827-3837
    Details
    In: Journal of Cell Science, The Company of Biologists, Vol. 108, No. 12 ( 1995-12-01), p. 3827-3837
    Kurzfassung: In pituitary-derived AtT-20 cells, recombinant fibronectin containing the N-terminal matrix assembly domain and the C-terminal half of fibronectin does not follow the regulated secretory pathway but instead concentrates in distinct organelles prior to secretion. These organelles are larger than the dense-core granules and localize to the cell body at sites that differ from lysosomes, endosomes and endo-plasmic reticulum. Unlike the dense-core granules, their discharge is not stimulated by 8-bromo-cyclic-AMP or phorbol esters. The kinetics of intracellular transport and secretion of the recombinant fibronectin suggest that it is present in a post-Golgi pool that turns over more slowly than constitutive vesicles. Indeed, the fibronectin-contain-ing organelles disappear with a half-time of 3 hours after inhibiting protein synthesis. Presence of the organelles correlates with intracellular aggregation of dimeric fibronectin polypeptides. The organelles are absent in cells expressing monomeric recombinant fibronectin (lacking C-terminal dimerization sites) or the C-terminal half of fibronectin (which dimerizes but lacks the N-terminal matrix assembly domain), both of which aggregate less efficiently than dimeric fibronectin. Instead, the latter polypeptides enter the dense-core granules. Thus while the formation of the fibronectin-containing organelles may require efficient aggregation, it may not require a specific structural signal. Moreover, efficient aggregation is not necessarily a prerequisite for following the regulated pathway.
    Materialart: Online-Ressource
    ISSN: 0021-9533 , 1477-9137
    URL: Article
    DOI: 10.1242/jcs.108.12.3827
    Sprache: Englisch
    Verlag: The Company of Biologists
    Publikationsdatum: 1995
    ZDB Id: 219171-4
    ZDB Id: 1483099-1
    SSG: 12
    Standort Signatur Einschränkungen Verfügbarkeit
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    Online-Ressource
  • 18
    Online-Ressource
    Online-Ressource
    Mislocalized Scaffolding by the Na-H Exchanger NHE1 Dominantly Inhibits Fibronectin Production and TGF-β Activation
    American Society for Cell Biology (ASCB) ; 2009
    In:  Molecular Biology of the Cell Vol. 20, No. 8 ( 2009-04-15), p. 2327-2336
    Details
    In: Molecular Biology of the Cell, American Society for Cell Biology (ASCB), Vol. 20, No. 8 ( 2009-04-15), p. 2327-2336
    Kurzfassung: Secretion and assembly of the extracellular matrix protein fibronectin regulates a number of normal cell and tissue functions and is dysregulated in disease states such as fibrosis, diabetes, and cancer. We found that mislocalized scaffolding by the plasma membrane Na-H exchanger NHE1 suppresses fibronectin expression, secretion, and assembly. In fibroblasts, wild-type NHE1 localizes to the distal margin of membrane protrusions or lamellipodia but a mutant NHE1-KRA2 lacking binding sites for PI(4,5)P2 and the ERM proteins ezrin, radixin, and moesin is mislocalized and found uniformly along the plasma membrane. Although NHE1 regulates intracellular pH homeostasis, fibronectin production is not regulated by changes in intracellular pH, nor is it attenuated in NHE1-deficient cells, indicating fibronectin expression is independent of NHE1 activity. However, fibronectin production is nearly absent in cells expressing NHE1-KRA2 because scaffolding by NHE1 is mislocalized. Additionally, secretion of active but not latent TGF-β is reduced and exogenous TGF-β restores fibronectin secretion and assembly. Our data indicate that scaffolding by NHE1-KRA2 dominantly suppresses fibronectin synthesis and TGF-β activation, and they suggest that NHE1-KRA2 can be used for obtaining a mechanistic understanding of how fibronectin production is regulated and speculatively for therapeutic control of dysregulated production in pathological conditions.
    Materialart: Online-Ressource
    ISSN: 1059-1524 , 1939-4586
    URL: Article
    DOI: 10.1091/mbc.e08-08-0842
    Sprache: Englisch
    Verlag: American Society for Cell Biology (ASCB)
    Publikationsdatum: 2009
    ZDB Id: 1474922-1
    SSG: 12
    Standort Signatur Einschränkungen Verfügbarkeit
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    Online-Ressource
  • 19
    Online-Ressource
    Online-Ressource
    BPAG1e Maintains Keratinocyte Polarity through β4 Integrin–mediated Modulation of Rac 1 and Cofilin Activities
    American Society for Cell Biology (ASCB) ; 2009
    In:  Molecular Biology of the Cell Vol. 20, No. 12 ( 2009-06-15), p. 2954-2962
    Details
    In: Molecular Biology of the Cell, American Society for Cell Biology (ASCB), Vol. 20, No. 12 ( 2009-06-15), p. 2954-2962
    Kurzfassung: α6β4 integrin, a component of hemidesmosomes, also plays a role in keratinocyte migration via signaling through Rac1 to the actin-severing protein cofilin. Here, we tested the hypothesis that the β4 integrin-associated plakin protein, bullous pemphigoid antigen 1e (BPAG1e) functions as a scaffold for Rac1/cofilin signal transduction. We generated keratinocyte lines exhibiting a stable knockdown in BPAG1e expression. Knockdown of BPAG1e does not affect expression levels of other hemidesmosomal proteins, nor the amount of β4 integrin expressed at the cell surface. However, the amount of Rac1 associating with β4 integrin and the activity of both Rac1 and cofilin are significantly lower in BPAG1e-deficient cells compared with wild-type keratinocytes. In addition, keratinocytes deficient in BPAG1e exhibit loss of front-to-rear polarity and display aberrant motility. These defects are rescued by inducing expression of constitutively active Rac1 or active cofilin. These data indicate that the BPAG1e is required for efficient regulation of keratinocyte polarity and migration by determining the activation of Rac1.
    Materialart: Online-Ressource
    ISSN: 1059-1524 , 1939-4586
    URL: Article
    DOI: 10.1091/mbc.e09-01-0051
    Sprache: Englisch
    Verlag: American Society for Cell Biology (ASCB)
    Publikationsdatum: 2009
    ZDB Id: 1474922-1
    SSG: 12
    Standort Signatur Einschränkungen Verfügbarkeit
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    Online-Ressource
  • 20
    Online-Ressource
    Online-Ressource
    Fibrillin Assembly Requires Fibronectin
    American Society for Cell Biology (ASCB) ; 2009
    In:  Molecular Biology of the Cell Vol. 20, No. 3 ( 2009-02), p. 846-858
    Details
    In: Molecular Biology of the Cell, American Society for Cell Biology (ASCB), Vol. 20, No. 3 ( 2009-02), p. 846-858
    Kurzfassung: Fibrillins constitute the major backbone of multifunctional microfibrils in elastic and nonelastic extracellular matrices. Proper assembly mechanisms are central to the formation and function of these microfibrils, and their properties are often compromised in pathological circumstances such as in Marfan syndrome and in other fibrillinopathies. Here, we have used human dermal fibroblasts to analyze the assembly of fibrillin-1 in dependence of other matrix-forming proteins. siRNA knockdown experiments demonstrated that the assembly of fibrillin-1 is strictly dependent on the presence of extracellular fibronectin fibrils. Immunolabeling performed at the light and electron microscopic level showed colocalization of fibrillin-1 with fibronectin fibrils at the early stages of the assembly process. Protein-binding assays demonstrated interactions of fibronectin with a C-terminal region of fibrillin-1, -2, and -3 and with an N-terminal region of fibrillin-1. The C-terminal half of fibrillin-2 and -3 had propensities to multimerize, as has been previously shown for fibrillin-1. The C-terminal of all three fibrillins interacted strongly with fibronectin as multimers, but not as monomers. Mapping studies revealed that the major binding interaction between fibrillins and fibronectin involves the collagen/gelatin-binding region between domains FNI 6 and FNI 9 .
    Materialart: Online-Ressource
    ISSN: 1059-1524 , 1939-4586
    URL: Article
    DOI: 10.1091/mbc.e08-08-0830
    Sprache: Englisch
    Verlag: American Society for Cell Biology (ASCB)
    Publikationsdatum: 2009
    ZDB Id: 1474922-1
    SSG: 12
    Standort Signatur Einschränkungen Verfügbarkeit
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    Online-Ressource
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