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  • 1990-1994  (5)
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  • 1
    Publication Date: 1993-09-01
    Print ISSN: 0018-2222
    Electronic ISSN: 1432-119X
    Topics: Biology , Medicine
    Published by Springer
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Histochemistry and cell biology 100 (1993), S. 231-239 
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Type XI collagen was localized with polyclonal antibodies specific for α1(XI) and α2(XI) chains in the resting zone of epiphyseal cartilage from calf fetuses. The immunofluorescence technique was used on sections of cartilage, and the immunogold labelling technique for electron microscopy on fibrils isolated from cartilage and, for the fist time, in situ on blocks of cartilage fractured in liquid nitrogen. Immunofluorescence showed that without pepsin treatment the staining of type XI collagen was restricted to the pericellular zones; after pepsin treatment, the staining was co-distributed with that of type II collagen. Immunoelectron microscopy performed on isolated fibrils and on cartilage blocks showed that after disruption of fibrils with pepsin, type XI collagen was labelled on small filaments on the fibrils. When the fibrils were not disrupted, labelling was observed in situ only at the ends of the fibrils or on cross-sections of some fibrils. These results indicate that type XI collagen is located inside type II collagen fibrils in fetal bovine epiphyseal cartilage, as already postulated for embryonic chicken sterna.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Hoboken, NJ : Wiley-Blackwell
    Journal of Biomedical Materials Research 28 (1994), S. 159-165 
    ISSN: 0021-9304
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine , Technology
    Notes: Cross-linking of collagen-based biomaterials increases their strength and persistence in vivo. Recently, we described an efficient cross-linking process via the formation of acyl azide groups on methylated carboxyl groups of collagen using hydrazine and nitrous acid (referred to here as the hydrazine method). In this report, we propose a simpler, faster way to prepare acyl azide groups and to cross-link collagen-based biomaterials, using diphenylphosphorylazide (DPPA) as a reagent. After determining the optimal conditions of cross-linking with DPPA, we compared the efficiency of this protocol with that using hydrazine and with the classical glutaraldehyde treatment. In order to validate and quantitate the extent of reaction, the degree of crosslinking was determined by the measure of the free primary amino group content of the samples.Treatment of native bovine pericardium with 0.5% DPPA for 24 h led to efficient cross-linking, corresponding to a 50% decrease in the free primary amino group content of the sample and raising its thermal stability from 62.8 up to 81.3°C. In comparison, the thermal stabilities of glutaraldehydeor hydrazine-treated pericardium were 85 ± 0.4°C and 83.4 ± 0.1°C. Similar decreases in free primary amino group content and increases in thermal stability were obtained for collagen films treated with DPPA, glutaraldehyde, or hydrazine. These results were corroborated by resistance to bacterial collagenase digestion: DPPA-treated pericardium had a resistance to collagenase digestion similar to that of glutaraldehyde- or hydrazine-treated pericardium. Residual DPPA content: the concentration of phosphorus in tissue treated with 0.5% DPPA was not significantly different from that of untreated tissue. Treatment by DPPA thus appears to be an efficient, rapid method for cross-linking collagenbased biomaterials. © 1994 John Wiley & Sons, Inc.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Hoboken, NJ : Wiley-Blackwell
    Journal of Biomedical Materials Research 24 (1990), S. 689-703 
    ISSN: 0021-9304
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine , Technology
    Notes: The biocompatibility of a subcutaneously implanted bovine collagen sponge (Haemostagen) was studied in rats by analyzing tissue reactions up to 3 months by histological and ultrastructural methods; in addition, the level of serum antibodies to bovine type I collagen (the major implant collagen) was measured by solid-phase radio-immunoassay. By 8 h after implantation, the implant was completely filled with polymorphonuclear cells (PMNs). After 8 days, fibroblasts had developed a granulation tissue within the sponge and the PMNs had almost disappeared. The small residue that remained after 1 month consisted of some densely packed collagen fibrils containing giant cells, which had disappeared by 3 months. No antibodies to bovine type I collagen were found in the sera of implanted rats.
    Additional Material: 8 Ill.
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  • 5
    Electronic Resource
    Electronic Resource
    Hoboken, NJ : Wiley-Blackwell
    Journal of Biomedical Materials Research 24 (1990), S. 179-187 
    ISSN: 0021-9304
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine , Technology
    Notes: Collagen biomaterials should be cross-linked in order to prevent biodegradation when they are used as implants. We have compared the cross-linking efficiencies of glutaraldehyde and acyl azide in pericardium. Glutaraldehyde is used currently, but it elicits a cytotoxic effect which reduces the biocompatibility of cross-linked tissue. We have attempted to overcome this problem by developing a cross-linking method that obviates incorporation of foreign agents. Our process involves transformation of free carboxyl groups on collagen into acyl azide groups, which react with free amino groups on adjacent side chains. We have shown that the greatest increase in the thermal stability of collagen, as measured by differential scanning calorimetry, is achieved when tissue swelling is inhibited by the addition of sodium chloride (1 M) during acyl azide formation. Under these conditions, the denaturation temperature (Td) of pericardial collagen treated with acyl azide is raised to 83.4°C and that of tissue treated with glutaraldehyde to 85.1°C. Moreover, acyl-azide-treated tissues have the same resistance as glutaraldehydetreated tissues to chemical solubilization by cyanogen bromide and to enzymatic digestion by collagenase.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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