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Bone in dermatosparaxis. II. Chemical analysis

B Nusgens, C M Lapière

    Calcified Tissue Research
    |August 3, 1976
    PubMed
    Summary
    This summary is machine-generated.

    Dermatosparactic (D-) bone exhibits altered collagen and increased hydroxyapatite, leading to hypercalcification. Procollagen fiber defects may cause excess glycoproteins, driving abnormal calcium salt deposition in D-bone.

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    Area of Science:

    • Biochemistry
    • Biomineralization
    • Connective Tissue Biology

    Background:

    • Dermatosparaxis (D-) is a genetic disorder affecting collagen processing.
    • Altered collagen mechanical properties are implicated in bone calcification disorders.
    • Understanding D-bone matrix composition is crucial for elucidating hypercalcification mechanisms.

    Purpose of the Study:

    • To analyze the organic matrix of D-bone.
    • To evaluate the role of altered procollagen fiber mechanical properties in D-bone calcification.
    • To compare D-bone and normal (N-) bone composition and calcification.

    Main Methods:

    • Physical and chemical analysis of bone organic matrix.
    • Density gradient fractionation via centrifugation.

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  • Quantification of collagen, hydroxyapatite, and glycoproteins.

    • Main Results:

    • D-bone had less collagen and more hydroxyapatite than N-bone.
    • D-bone contained >80% highly calcified fraction vs. 37% in N-bone.
    • D-bone showed increased glycoproteins in newly formed matrix and higher collagen reduction during calcification.

    Conclusions:

    • Altered procollagen fibers in D-bone may lead to excess glycoproteins.
    • These matrix alterations likely contribute to D-bone hypercalcification.
    • Mechanisms include increased calcium salt deposition and fibrous framework distension.