Intermolecular cross-links in collagen of human placenta

Kao, Kung-Ying Tang; Leslie, James G.

doi:10.1016/0005-2795(79)90148-x

Cited by 3 publications

(1 citation statement)

References 17 publications

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“…(a), (b) and (c) depict the elution profile of reduced cross-links of calvaria collagen from controls, dichloromethanediphosphonate-treated and 1-hydroxyethane-l,1-diphosphonate-treated rats respectively. The individual cross-links [(i) dihydroxylysinonorleucine, (ii) hydroxylysinonorleucine, (iii) lysinonorleucine and (iv) histidinohydroxymerodesmosinel were identified as described by Kao & Leslie (1979).…”

Section: Controlmentioning

confidence: 99%

The influence of 1-hydroxyethane-1,1-diphosphonate and dichloromethanediphosphonate on lysine hydroxylation and cross-link formation in rat bone, cartilage and skin collagen

Guenther¹,

Guenther²,

Fleisch³

1981

Biochemical Journal

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The effects in vivo of dichloromethanediphosphonate and 1-hydroxyethane 1,1-diphosphonate on collagen solubility, hydroxylation of lysine and proline and on the formation of collagen intermolecular cross-links were studied by using rat bone, cartilage and skin tissues. Dichloromethanediphosphonate decreased bone collagen solubility both in acetic acid and after pepsin treatment. Although none of the diphosphonates had any effect on the hydroxylation of proline, dichloromethane-diphosphonate, but not 1-hydroxyethane-1,1-diphosphonate, increased the number of hydroxylysine residues in the alpha-chains of bone, skin and cartilage collagen. The stimulatory effect was dose-dependent. The dichloromethanediphosphonate-mediated increase in hydroxylysine residues in bone and cartilage was manifested in an increase of dihydroxylysinonorleucine, the cross-link that is formed by the condensation of two hydroxylysine residues. The cross-link hydroxylysinonorleucine, a condensation product of hydroxylysine and lysine, on the other hand, was decreased. The total number of intermolecular cross-links was not changed by the diphosphonate.

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Section: Controlmentioning

confidence: 99%

The influence of 1-hydroxyethane-1,1-diphosphonate and dichloromethanediphosphonate on lysine hydroxylation and cross-link formation in rat bone, cartilage and skin collagen

Guenther¹,

Guenther²,

Fleisch³

1981

Biochemical Journal

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Analysis of the Crosslinking Components in Collagen and Elastin

Robins¹

1982

Methods of Biochemical Analysis

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Chemical characterization of glomerular and tubular basement membranes of men of different ages

Langeveld¹,

Veerkamp²,

duyf³

et al. 1981

Kidney International

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Pairs of glomerular and tubular basement membrane preparations were obtained from kidneys of individuals of premature age up to 80 years. The purity of the preparations was established with light and electron microscopy and by estimating the total phosphorus content. The amino acid and carbohydrate composition was determined and statistically evaluated for 33 to 38 preparations divided over five age groups. Comparison of glomerular and tubular basement membranes from the same kidneys showed that regardless of age glomerular basement membranes contain more 3-hydroxyproline and more of the heteropolysaccharide constituents neuraminic acids and mannose. These differences cannot be ascribed solely to the presence of a minor amount of interstitial collagen. The chemical composition of the two types of basement membranes changes with age. For the first few years after birth the contents of glycine and total imino acids increase and those of collagen-nonspecific amino acids decrease, whereas constituents of the heteropolysaccharide units do not change markedly. These results suggest that proportions of collagenous and noncollagenous peptide moieties gradually change with age in both glomerular and tubular basement membranes. In addition, the extent of hydroxylation of proline and lysine increases significantly with age, reaching an adult level for glomerular basement membranes after 4 to 7 months of age and for tubular basement membranes during late childhood. The contents of glucose and galactose rise with age to an extent comparable with that of hydroxylysine. The age-related changes in basement membrane composition may influence functional properties of these extracellular renal structures.

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Intermolecular cross-links in collagen of human placenta

Cited by 3 publications

References 17 publications

The influence of 1-hydroxyethane-1,1-diphosphonate and dichloromethanediphosphonate on lysine hydroxylation and cross-link formation in rat bone, cartilage and skin collagen

The influence of 1-hydroxyethane-1,1-diphosphonate and dichloromethanediphosphonate on lysine hydroxylation and cross-link formation in rat bone, cartilage and skin collagen

Analysis of the Crosslinking Components in Collagen and Elastin

Chemical characterization of glomerular and tubular basement membranes of men of different ages

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