The nature of crosslinking in collagens from mineralized tissues

Mechanic, Gerald L.; Gallop, Paul M.; Tanzer, Marvin L.

doi:10.1016/0006-291x(71)90465-7

Cited by 150 publications

(64 citation statements)

References 15 publications

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“…Lysyl oxidase, an enzyme involved in the initiation of this process, has been demonstrated in the odontoblast/predentin layer (Numata and Hayakawa, 1986). Of the two borohydride-reducible bifunctional cross-links, dihydroxylysinonorleucine (DHLNL) and hydroxylysinonorleucine (HLNL), the former constitutes the major cross-link in dentin and bone (Mechanic et al, 1971). In addition, pyridinoline, which is trifunctional and nonreducible, is known to be a major cross-link (Eyre and Oguchi, 1980;Kuboki et al, 1981).…”

Section: A Collagensmentioning

confidence: 99%

Dentinogenesis

Linde

Goldberg

1993

Critical Reviews in Oral Biology & Medicine

428

333

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The formation of dentin, dentinogenesis, comprises a sophisticated interplay between several factors in the tissue, cellular as well as extracellular. Dentin may be regarded as a calcified connective tissue. In this respect, as well as in its mode of formation, it is closely related to bone. Using dentinogenesis as an experimental model to study biomineralization provides several practical advantages, and the results may be extrapolated to understand similar processes in other tissues, primarily bone. After describing dentin structure and composition, this review discusses items such as the morphology of dentinogenesis; the dentinogenically active odontoblast, transport, and concentrations of mineral ions; the constituents of the dentin organic matrix; and the presumed mechanisms involved in mineral formation.

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Section: A Collagensmentioning

confidence: 99%

Dentinogenesis

Linde

Goldberg

1993

Critical Reviews in Oral Biology & Medicine

428

333

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“…All three are based on the reactions of lysine-and hydroxylysine-derived aldehydes and, after reduction with borohydride, result in the formation of hydroxylysinonorleucine (I) [I] , dihydroxylysinonorleucine (II) [2,3] and histidinohydroxymerodesmosine (III) [4,5] . During our early studies into the nature of these bonds we showed that in their non-reduced form two of them, I and III, were extremely labile, being readily cleaved by dilute acids, a-amino-fl-thiols and thermal denaturation…”

Section: Introductionmentioning

confidence: 99%

Relative stabilities of the intermediate reducible crosslinks present in collagen fibres

Robins

Bailey

1973

FEBS Letters

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“…Hydroxylysine is a precursor in the biosynthesis of certain collagen crosslinks (3,4 don, bone, and cartilage collagens (3)(4)(5)(6)(7)(8)(9)(10)(11). Each tissue reveals a unique distribution of these reducible crosslinks that changes as the tissue matures and ages (8,10).…”

mentioning

confidence: 99%

Reducible Crosslinks in Hydroxylysine-Deficient Collagens of a Heritable Disorder of Connective Tissue

Eyre

Glimcher

1972

Proc. Natl. Acad. Sci. U.S.A.

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Reducible compounds that participate in crosslinking were analyzed in hydroxylysine-deficient collagens of patients with a heritable disorder of connective tissue. After treatment with [3H1sodium borohydride, new compounds, as well as a totally different pattern of tritiated compounds, were found in hydroxylysine-deficient collagen from skin as compared with age-matched controls. The amount of desmosines detected indicated that more elastin was present in abnormal skin than in control skin.Bone collagen, which was not as deficient in hydroxylysine as skin collagen, had the same compounds as normal bone collagen, but their relative proportions were altered, consistent with a deficiency of hydroxylysine, a precursor of the crosslinks. Although the content of hydroxylysine in collagen of cartilage is essentially normal in these patients, analysis after reduction revealed a different pattern of reduced compounds from that of normal cartilage. It is speculated that Type II collagen, the major collagen component in cartilage, contains a normal amount of hydroxylysine, while Type I collagen, which is the major source of the crosslinks, is hydroxylysine-deficient. This distribution would explain the findings of an abnormal profile of reducible compounds despite an almost normal total hydroxylysine content.The finding that the deficiency of hydroxylysine in the collagen of these patients is accompanied by changes in number, chemical nature, and, probably, distribution of crosslinkages, and the previously reported alterations in the solubility characteristics, suggest that at least some skeletal and connective tissue abnormalities are directly related to underlying molecular pathology.

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The nature of crosslinking in collagens from mineralized tissues

Cited by 150 publications

References 15 publications

Dentinogenesis

Dentinogenesis

Relative stabilities of the intermediate reducible crosslinks present in collagen fibres

Reducible Crosslinks in Hydroxylysine-Deficient Collagens of a Heritable Disorder of Connective Tissue

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