Isolation and structural identification of a labile intermolecular crosslink in collagen

Bailey, Allen J.; Peach, Catherine M.

doi:10.1016/0006-291x(68)90233-7

Cited by 148 publications

(49 citation statements)

References 15 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Analysis of collagen stabilized by borohydride reduction has resulted in the identification of a number of new amino acids, the structures of which support our belief that in their non-reduced form they act as intermolecular cross-links or as the precursors to more complex cross-links (Bailey & Peach, 1968;Bailey, Peach & Fowler, 1970b).…”

Section: Discussionmentioning

confidence: 81%

“…The two standards, hydroxylysinonorleucine and lysinonorleucine, were synthesized by a coupling reaction of 5-8-bromobutylhydrantoin with hydroxylysine (Bailey & Peach, 1968) and lysine (Franzblau, Faris & Papioannou, 1969) respectively. On the basis of chromatographic evidence peaks I and II were provisionally identified as hydroxylysinonorleucine and lysinonorleucine respectively.…”

Section: Reduction and Analysis Of The Collagenfibresmentioning

confidence: 99%

See 1 more Smart Citation

The chemistry of the collagen cross-links. The absence of reduction of dehydrolysinonorleucine and dehydrohydroxylysinonorleucine in vivo

Bailey

Peach

1971

Biochemical Journal

Self Cite

View full text Add to dashboard Cite

Two aldimine bonds have been shown to be present as stabilizing cross-links in intact collagen fibres from soft tissues: dehydrohydroxylysinonorleucine as a major component and dehydrolysinonorleucine being present in trace quantities. In the highly insoluble collagens less dehydrohydroxylysinonorleucine is present but the proportion of dehydrolysinonorleucine increases. In elastin the latter aldimine is reduced in vivo to give a more stable cross-link but no comparable reduction could be detected with either of the aldimines present in collagen.

show abstract

Section: Discussionmentioning

confidence: 81%

Section: Reduction and Analysis Of The Collagenfibresmentioning

confidence: 99%

The chemistry of the collagen cross-links. The absence of reduction of dehydrolysinonorleucine and dehydrohydroxylysinonorleucine in vivo

Bailey

Peach

1971

Biochemical Journal

Self Cite

View full text Add to dashboard Cite

show abstract

“…Evidence to date indicates that collagen cross-linking involves oxidative deamination of certain lysyl residues to form allysine (a-aminoadipic-8-semialdehyde) that then reacts via Schiff base formation with an e-amino group of a lysyl or hydroxylysyl residue located on an adjacent molecule to form the reducible intermolecular cross-links, A67 dehydrolysinonorleucine or A6'7 dehydrohydroxylysinonorleucine (12)(13)(14)(15)(16). In a separate pathway, two residues of the aldehyde, allysine, may condense in an aldol condensation to form the "intra"-molecular cross-link (17)(18)(19)(20)(21).…”

Section: Introductionmentioning

confidence: 99%

A Collagen Defect in Homocystinuria

1973

View full text Add to dashboard Cite

The biochemical mechanism accounting for the connective tissue abnormalities in homocystinuria was explored by examining the effects of various amino acids known to accumulate in the plasma of patients with this disease on cross-link formation in collagen. Neutral salt solutions of purified, rat skin collagen, rich in cross-link precursor aldehydes, were polymerized to native type fibrils by incubating at 370C in the presence of homocysteine, homocystine, or methionine. After the polymerization was completed, each sample was examined for the formation of covalent intermolecular cross-links, assessed indirectly by solubility tests and directly by measuring the cross-link compounds after reduction with tritiated sodium borohydride and hydrolysis.Collagen solutions containing homocysteine (0.01 M-0.1 M) failed to form insoluble fibrils. Furthermore, much less of the reducible cross-links, A"'7 dehydrohydroxylysinonorleucine, A67 dehydrohydroxylysinohydroxynorleucine, and histidino-dehydrohydroxymerodesmosine were formed in the preparations containing homocysteine as compared with the control and the samples containing methionine or homocystine. The content of the precursor aldehydes, a-aminoadipic-8-semialdehyde (allysine) and the aldol condensation product, was also markedly diminished in tropocollagen incubated with homocysteine. It is concluded that homocysteine interferes with the formation of intermolecular

show abstract

“…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.

View full text Add to dashboard Cite

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.

show abstract

Isolation and structural identification of a labile intermolecular crosslink in collagen

Cited by 148 publications

References 15 publications

The chemistry of the collagen cross-links. The absence of reduction of dehydrolysinonorleucine and dehydrohydroxylysinonorleucine in vivo

The chemistry of the collagen cross-links. The absence of reduction of dehydrolysinonorleucine and dehydrohydroxylysinonorleucine in vivo

A Collagen Defect in Homocystinuria

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

Contact Info

Product

Resources

About