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Weefselcollagenase en zijn substraten Tissue collagenase and its substrates /Bos, Teunis van den, January 1979 (has links)
Thesis (doctoral)--Utrecht, 1979.
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Production of Collagenase Inhibitor by Mouse Calvaria in Tissue CultureSAKAMOTO, SEIZABURO, NAGAYAMA, MASARU 11 1900 (has links)
No description available.
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Tissue inhibitor of metalloproteinase-1 expression by human hepatic lipocytes and its role in liver diseaseIredale, John Peter January 1994 (has links)
No description available.
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Collagenolytic activities of intercranial tumours : In-vitro biochemical and immunolocalization studiesHalaka, A. N. A. M. January 1986 (has links)
No description available.
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Identification and Targeting of Collagen in the Capsule of Rat Knees with Immobilization-Induced Flexion ContracturesWong, Kayleigh January 2015 (has links)
Immobility causes joint contractures, loss in range of motion (ROM), notably in elderly and bed-ridden patients. In a rat knee immobilization flexion contracture (FC) model, the posterior capsule contributes to irreversible limitation of ROM. Through microarray, extracellular matrix and collagen pathways were identified as differentially expressed in the posterior capsule of knees with FC. We hypothesized that intra-articular injection of collagenases in rats with knee FC will interfere with collagen in the capsule and allow increased ROM. After four weeks of hind-limb immobilization, rats develop knee FC; two weeks of remobilization with collagenase treatment showed increased ROM compared to buffer injected knees of 8.043° (p-value=0.046). Histological analysis of knee sections revealed changes in collagen content of the extracellular matrix in posterior capsule. In vitro incubation of rat capsules with collagenases confirmed changes in collagen. Along with current rehabilitation methods, treatment with collagenase may augment ROM recovery from knee joint contractures.
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Isolation and Characterization of Mouse Bone Collagenase InhibitorSAKAMOTO, SEIZABURO, NAGAYAMA, MASARU 11 1900 (has links)
No description available.
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Novel roles for matix metalloproteinases in cell-matrix interactionsMessent, Anthea Jane January 1997 (has links)
No description available.
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Bioactive Chitosan Nanoparticles and Photodynamic Therapy Inhibit Collagen Degradation in vitroPersadmehr, Anousheh 09 December 2013 (has links)
This study evaluated the ability of photodynamic therapy (PDT), chitosan nanoparticles
(CSnp), or their combination, to inhibit bacterial collagenase-mediated degradation of
collagen. Rat type 1 fibrillar collagen matrices were untreated or treated with 2.5%
glutaraldehyde (GD), 2.5% GD followed by 1% CSnp, 1% CSnp, PDT, or 1% CSnp
followed by PDT. Samples, except untreated controls, were exposed to Clostridium
histolyticum collagenase. The soluble digestion products were
assessed by hydroxyproline assay and the remaining adherent collagen was quantified by
picrosirius red (PSR) staining. Collagen treated with CSnp, PDT, or a combination of
CSnp and PDT, exhibited less degradation than controls. The abundance of posttreatment
residual collagen correlated with the extent of degradation. Fourier transform
infrared (FTIR) spectroscopy analysis showed that PDT treatment enhanced collagen
cross-linking. Immunoblotting of sedimented CSnp indicated that CSnp and collagenase
bound with low affinity. However, CSnp-bound collagenase showed a significant
reduction in collagenolytic activity compared with controls.
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Bioactive Chitosan Nanoparticles and Photodynamic Therapy Inhibit Collagen Degradation in vitroPersadmehr, Anousheh 09 December 2013 (has links)
This study evaluated the ability of photodynamic therapy (PDT), chitosan nanoparticles
(CSnp), or their combination, to inhibit bacterial collagenase-mediated degradation of
collagen. Rat type 1 fibrillar collagen matrices were untreated or treated with 2.5%
glutaraldehyde (GD), 2.5% GD followed by 1% CSnp, 1% CSnp, PDT, or 1% CSnp
followed by PDT. Samples, except untreated controls, were exposed to Clostridium
histolyticum collagenase. The soluble digestion products were
assessed by hydroxyproline assay and the remaining adherent collagen was quantified by
picrosirius red (PSR) staining. Collagen treated with CSnp, PDT, or a combination of
CSnp and PDT, exhibited less degradation than controls. The abundance of posttreatment
residual collagen correlated with the extent of degradation. Fourier transform
infrared (FTIR) spectroscopy analysis showed that PDT treatment enhanced collagen
cross-linking. Immunoblotting of sedimented CSnp indicated that CSnp and collagenase
bound with low affinity. However, CSnp-bound collagenase showed a significant
reduction in collagenolytic activity compared with controls.
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Studium vybraných modifikovaných kolagenových biomateriálů / Study of some modified colagen biomaterialsZouharová, Lucie January 2009 (has links)
The aim of the presented work is the study and biochemical characterization of some modified collagen materials (prepared on Institute of Material Science, Faculty of Chemistry, BUT), optimalization of collagen isolation from various types of animal tissues and testing of isolated collagen stability. First, isolation of collagen from five different animal tissues was performed with satisfactory yields. The concentration of total proteins was measured by Biuret and Hartree – Lowry method, the concentration of free amino groups was measured by TNBSA method. Protein analysis in colllagen preparatives was peformed by vertical electrophoresis PAGE-SDS and by microfluidic electrophoretic system Experion for comparison. Further purification and separation of collagen isolates by gel permeation chromatography was tested too. To detailed characterization thermal stability of collagen specimens was performed by high performance ultrasonic spectroscopy. Biological stability of collagen was tested in model physiological conditions.
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