Ultrastructural and biochemical modifications of collagen from tissue of Morbus Dupuytren patients.
Small angle X-ray diffraction and biochemical analyses were carried out on normal palmar aponeurosis and on tissue from patients suffering from Dupuytren contractures (MD). Pathological tissue exhibits a higher overall content of collagen III. Type I collagen extracted from pathological tissue has a melting point of 0.8 degrees C higher than that of normal collagen. The only chemical differences compared to normal collagen I are 50% overhydroxylation of lysyl residues and a reduced amount of diglycosylated hydroxylysine residues. Analysis of the electron density distribution inside the collagen repeating period of MD-samples reveals disordered molecular packing in MD samples compared to in normal collagen. The disorder, which is higher in the gap region, is considerably reduced upon stretching.
Institut für Medizinische Molekularbiologie, Medizinische Universität zu Lübeck, Federal Republic of Germany.
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Notbohm
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Hoch
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D002240:Carbohydrate Sequence; D002942:Circular Dichroism; D003094:Collagen / Q000737:chemistry / Q000378:metabolism* / Q000648:ultrastructure*; D004387:Dupuytren Contracture / Q000378:metabolism*; D006358:Hot Temperature; D006801:Humans; D008969:Molecular Sequence Data; D014961:X-Ray Diffraction
D003094:Collagen