Thesis (doctoral)--Utrecht, 1979.

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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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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.

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.

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.