Glykosaminoglykan- und Kollagenanalysen bei Osteogenesis imperfecta

Bleckmann, H.; Kresse, Hans; Wollensak, J.; Buddecke, Eckhart

doi:10.1007/bf00446347

Cited by 22 publications

(9 citation statements)

References 10 publications

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“…ferent types of collagen crosslinking between normal dermis and dermal scar of the guinea pig. and Bleckman et al 38 concluded that Osteogenesis Imperfecta is due t o a deficiency in the crosslinking reactions of collagen. It may well be that the development of the hypertrophic scar is due to, or occurs in concert with, similar defects in crosslinking of collagen.…”

Section: Discussionmentioning

confidence: 98%

Collagen and Mucopolysaccharides in the Hypertrophic Scar

Kischer

Shetlar

1974

Connective Tissue Research

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The hypertrophic scar occurs in healed skin from deep burns or equivalent injury in humans. It is erythematous, elevated, hard to the touch, and can produce severe contractures. This scar is characterized by marked increases in collagen and chondroitin-4-sulfate. Transmission electron microscopy, including localization of ruthenium red, scanning electron microscopy and appropriate biochemical assays have served to evaluate the relationship between collagen and interstitial mucopolysaccharide material in the hypertrophic scar. These results have been compared to those obtained for normal skin, mature scar, and granulation tissue, and are interpreted from the standpoint of explaining some of the clinical aspects of the scar. Two basic forms of interstitial material are observed, globular and filamentous. The globular forms predominate in normal skin, mature scar and granulation tissue. Hypertrophic scar demonstrates a marked dominance of the filamentous forms, which often appear to link collagen in chain-like fashion. Scanning electron microscopy complements this view by demonstrating a near homogeneous dermal matrix, as if the collagen filaments were "glued" together. In mature scar, this dermal mass appears to be resolving into individual collagen filaments. Globular forms of the interstitial material can be demonstrated in hypertrophic scar if the tissue is stretched and held in position from 1 to 3 hours prior to fixation. However, no change in chondroitin-4-sulfate is observed. In the stretch condition individual collagen filaments are observed. It is suggested that one of the factors generating the rigid character of the hypertrophic scar may be a firm intercollagen linkage mediated by chondroitin-4-sulfate. 205Connect Tissue Res Downloaded from informahealthcare.com by University of Newcastle Upon Tyne on 12/20/14For personal use only.

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Section: Discussionmentioning

confidence: 98%

Collagen and Mucopolysaccharides in the Hypertrophic Scar

Kischer

Shetlar

1974

Connective Tissue Research

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“…has been shown in an earlier study to reIease more free hydroxylysine on partial acid hydrolysis than did a normal control (albeit not aged-matched in that study). Bleckmann et al(1971) have also reported an increased hydroxylysine content in the collagen of OI. These studies also seem to suggest a common type of change in the primary sequence of collagen in both types of OI.…”

Section: Discussionmentioning

confidence: 89%

Osteogenesis imperfecta: Evidence for the existence of an abnormal amino acid sequence in the molecule of dermal collagen

Heathcote

Al-Alawi

1978

J of Inher Metab Disea

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A collagen-type pattern of peptide and amino acid spots was obtained when partial hydrolysates of normal human dermis were examined by a specially developed thin-layer chromatographic (TLC) 'finger-printing' technique. The pattern was consistent and independent of age and sex. Two clinically similar cases of osteogenesis imperfecta congenita gave identical patterns which differed in specific regions from those given by their age-matched, normal controls. A single case of osteogenesis imperfecta tarda showed the same overall pattern as the congenita cases. It is concluded that an abnormal amino acid sequence occurs in the collagen molecule of both types of osteogenesis imperfecta.

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“…Defects in cross-linkage formation, such as occur in lathyrism, result in a higher proportion of soluble collagen [7]. The reports of altered lysine [40] and hydroxylysine [8] contents of bone collagen in osteogenesis imperfecta may reflect abnormal cross-linkage formation in collagen, which would not necessarily be apparent in the ultrastructure.…”

Section: Discussionmentioning

confidence: 99%

“…Niemann [40] demonstrated an increase of aspartic and glutamic acids and a decrease of lysine in bone collagen. Bleckmann et al [8] found normal proline and hydroxyproline content in bone with an increase in hydroxylysine; these authors postulated a deficiency in cross-linking of collagen. Investigations of cellular oxidative metabolism have suggested that osteogenesis imperfecta is a generalized metabolic disorder with a disturbance of high energy phosphate metabolism which results in abnormal pyrophosphate metabolism [22,49].…”

Section: Introductionmentioning

confidence: 99%

“…Biochemical analysis of mucopolysaccharides in osteogenesis imperfecta has shown decreased levels in bone [48] and increased levels in cartilage [8]. Although amino acid abnormalities have been reported in osteogenesis imperfecta [10,53,54], Albright and Grunt [3] were unable to confirm such abnormalities and found normal calcium kinetics and balance studies of calcium, phosphorus, nitrogen, magnesium, and potassium.…”

Section: Introductionmentioning

confidence: 99%

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Osteogenesis Imperfecta: Morphologic and Biochemical Studies of Connective Tissue

1973

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ExtractIn iliac crest biopsies from 11 patients (ages from 4 to 22 years) with osteogenesis imperfecta, cortical thickness, osteoid width, and number of osteons were less than normal at all ages. Bone surface activity (formation and resorption), measured by quantitative microradiography, was lower than normal in younger patients; the normal pubertal decrease in surface activity was not evident in patients with osteogenesis imperfecta and, consequently, bone surface activity in the older patients was higher than in age-matched normal subjects. The ultrastructure of osteocytes, bone collagen, and scleral collagen did not differ from normal; corneal collagen fibers, however, were approximately half the diameter of normal. Total urinary hydroxyproline excretion, measured in 11 patients, was below normal in all except 2 infants (less than 12 months old). Serum parathyroid hormone levels, measured in nine patients, were normal. Long term treatment with sodium fluoride (two patients) and. treatment with magnesium oxide (three patients) did not alter bone morphology or bone surface activity. SpeculationThe supposition that in osteogenesis imperfecta the connective tissue is characterized by an immature form of collagen was not substantiated by this study. The abnormal fibrillar pattern and paucity of collagen in various connective tissues suggest a qualitative defect, related to collagen maturation, as well as a quantitative deficit in the amount of collagen produced.

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Glykosaminoglykan- und Kollagenanalysen bei Osteogenesis imperfecta

Cited by 22 publications

References 10 publications

Collagen and Mucopolysaccharides in the Hypertrophic Scar

Collagen and Mucopolysaccharides in the Hypertrophic Scar

Osteogenesis imperfecta: Evidence for the existence of an abnormal amino acid sequence in the molecule of dermal collagen

Osteogenesis Imperfecta: Morphologic and Biochemical Studies of Connective Tissue

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