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  • 1
    ISSN: 1433-8580
    Keywords: Fractures ; Calcitonine ; Ribonucleic acids ; Amino acids ; Kallikrein ; Growth hormone ; Adenosine monophosphate ; Frakturen ; Calcitonin ; Ribonucleinsäuren ; Aminosäuren ; Kallikrein ; Wachstumshormon ; Adenosinmonophosphat
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Zusammenfassung In Tierversuchen wurde der Einfluß von Calcitonin, Ribonucleinsäuren, Aminosäuren, Kallikrein, Wachstumshormon und cyclischem Adenosin 3′5′ monophosphat auf die Heilung von Tibiafrakturen der Kaninchen geprüft. Um objektive Meßergebnisse der Callusstabilität zu erhalten, wurden die Knochen maschinell bis zur Refraktur gebogen. Die angewandte Kraft und der Grad der Durchbiegung wurden fortlaufend gemessen und in Kurven aufgetragen. Der Anstiegswinkel der erzielten Kurven galt als Parameter der Callusstabilität. Versuche mit Calcitonin zeigten keinen Effekt auf die Knochenbruchheilung. Injektionen von Ribonucleinsäuren, Aminosäuren, Kallikrein und Wachstumshormon ließen einen begrenzten Einfluß auf die Callusfestigung erkennen. Eine Verbesserung der Frakturheilung wurde durch cyclisches Adenosin 3′5′ monophosphat erreicht. Durch die Kombination von cyclischem Adenosin 3′5′ monophosphat mit Aminosäuren, Ribonucleinsäuren und Kallikrein wurde ein optimales Resultat erzielt.
    Notes: Summary The influence of calcitonine, amino acids, ribonucleid acids, kallikrein, growth hormone, and cyclic adenosine 3′5′ monophosphate on fracture repair was tested in rabbits. To obtain an objective measurement of callus stability the bones were bent mechanically. The force applied and the degree of bending were recorded continuously. The slope of the curve was taken as a parameter of callus stability. In the series with calcitonine no influence on fracture healing was found. Injections of ribonucleic acids, amino acids, kallikrein, and growth hormone demonstrated a limited effect on bone repair. Callus formation was stimulated by adenosine 3′5′ monophosphate. Optimal results were achieved by a combination of adenosine 3′5′ monophosphate, amino acids, ribonucleic acids, and kallikrein.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Hoboken, NJ [u.a.] : Wiley-Blackwell
    Journal of Orthopaedic Research 7 (1989), S. 228-234 
    ISSN: 0736-0266
    Keywords: Tendon ; Metalloprotease ; Collagenase ; Gelatinase ; Chicken ; Stromelysin ; Life and Medical Sciences
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Tendon repair following trauma, rupture, or surgery involves both synthesis and degradation of collagen in order to reweave new collagen bundles in with the old. Using an in situ assay on polyacrylamide gels containing gelatin, we have identified protease activity from tendon tissue and from tendon cells in culture. A population of synovial cells from the epitenon surrounding the tendon as well as the tendon fibroblasts themselves were examined. The cells and the conditioned medium from both cell populations exhibited a major band of gelatin-degrading activity at 70 kdaltons and a minor band of activity at 60 kdaltons. When preparations were reacted with p-aminophenylmercuric acetate (APMA) before electrophoresis, a third band appeared at 63 kdaltons. The main band at 70 kdaltons comigrated with a [35S]methionine-radiolabeled protein band. Inhibitor and pH studies identified the enzymes as neutral metalloproteases requiring disulfide bonds for activity. No proteolytic activity was detected on casein-containing gels, ruling out the presence of stromelysin. Since electrophoresis in the presence of SDS would separate the metalloprotease from the smaller molecular weight inhibitor (TIMP), these in situ assays provide a sensitive screening system for gelatindegrading enzymes present in tendon without prior removal of TIMP.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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