The Macromolecular Structure of Collagen in Tendon Fibres of Dermatosparactic Animals

Mosler, E.; Folkhard, W.; Geercken, W.; Helle, O.; Knörzer, E.; Koch, Marta; Lapière, Ch. M.; Nemetschek-Gansler, H.; Nusgens, Betty; Nemetschek, Th.

doi:10.1515/znc-1986-0419

Cited by 6 publications

(1 citation statement)

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“…This may also underline that fulvic acid is not the sole factor causing Kashin-Beck disease. A molecular model of how an impaired conversion of pNcollagen I1 disturbs the fiber formation has been proposed [22]. Accordingly, one may assume that, in Kashin-Beck disease, the fiber formation is greatly disturbed by the presence of pN-collagen 11 as well as by the thermally labile and overhydroxylated collagen 11.…”

Section: Discussionmentioning

confidence: 99%

Fulvic acid disturbs processing of procollagen II in articular cartilage of embryonic chicken and may also cause Kashin‐Beck disease

Yang

Bodó

Notbohm

et al. 1991

European Journal of Biochemistry

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Kashin-Beck disease is a n endemic osteoarthropathy in China which may lead to skeletal deformation and dwarfism. We have analysed articular cartilage from two patients and found an accumulation of the precursor molecule, pro-pN-collagen I1 (pN, peptide atached at the amino-terminus) which was not present in extracts of control fetal cartilage. In addition, collagen I1 isolated from the same tissue by limited pepsin digestion had a decreased electrophoretic mobility, increased proline hydroxylation and decreased thermal stability. Previously, a genetic defect in pro-pN-collagen-I processing has been described in calf and sheep (dermatosparaxis) and man (Ehlers-Danlos, type VII) which caused an extreme fragility of the skin [Lenaers, A,, Ansay, M., Nusgens, B.

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Section: Discussionmentioning

confidence: 99%

Fulvic acid disturbs processing of procollagen II in articular cartilage of embryonic chicken and may also cause Kashin‐Beck disease

Yang

Bodó

Notbohm

et al. 1991

European Journal of Biochemistry

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Ehlers-Danlos Type VII-C, or Human Dermatosparaxis

Lapière¹

1993

Arch Dermatol

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The regulation of size and form in the assembly of collagen fibrils in vivo

Chapman

1989

Biopolymers

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A possible mechanism for regulating the lateral growth of collagen fibrils in vivo is considered. A growth inhibitor associated with a particular part of the long semiflexible collagen molecule restricts that part of the molecule to the surface of the growing assembly. Lateral accretion ceases when these inhibitors form a complete circumferential layer around the fibril surface. Cell-mediated removal of the inhibitors allows lateral growth to proceed to a second limiting layer, and so on to subsequent limiting layers. In this way, cycles of inhibitor removal and limited lateral accretion permit growth to be synchronized over large populations of fibrils. Observed diameter distributions in bundles of embryonic and neonatal fibrils are those expected from a mechanism of this kind. The mechanism depends on the existence of axial order (D-periodicity) in fibrils, but not on any specific lateral packing of molecules. Rather, contacts between newly assembled molecules are presumed to be partly fluid-like in lateral directions (except where covalent cross-links have formed). Some initial fluidity in lateral packing prior to cross-linking does not preclude the subsequent emergence of quasi-crystalline packing as cross-links form. The cylindrical shape of fibrils in vivo may also be attributable in part to fluidity of intermolecular contacts at the growing surface.

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The Macromolecular Structure of Collagen in Tendon Fibres of Dermatosparactic Animals

Abstract: Small-angle x-ray diffraction spectra of dermatosparactic tendon collagen show a decreased intensity of the first order reflection. We interprete this finding to be due to the N-terminal propeptide which fills the intermolecular gap region partially.

Cited by 6 publications

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Fulvic acid disturbs processing of procollagen II in articular cartilage of embryonic chicken and may also cause Kashin‐Beck disease

Fulvic acid disturbs processing of procollagen II in articular cartilage of embryonic chicken and may also cause Kashin‐Beck disease

Ehlers-Danlos Type VII-C, or Human Dermatosparaxis

The regulation of size and form in the assembly of collagen fibrils in vivo

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