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.
Notbohm
H
H
Institut für Medizinische Molekularbiologie, Medizinische Universität zu Lübeck, Federal Republic of Germany.
Bigi
A
A
Roveri
N
N
Hoch
J
J
Açil
Y
Y
Koch
M H
MH
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