Isolation and structure of a cross linked tripeptide from calf bone collagen

Fujii, Katsuyuki; Corcoran, Doris; Tanzer, Marvin L.

doi:10.1021/bi00691a011

Cited by 17 publications

(4 citation statements)

References 21 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Cross-links between residue 9N and helical residue 930 and between 16°and helical residue 87 of the 1 chain have been found in a variety of tissues such as rat tail tendon (Kang, 1972), bovine bone (Eyre & Glimcher, 1973), rabbit skin, bone, and tendon (Henkel et al, 1976), bovine skin (Becker et al, 1975Yamauchi et al, 1982), and bovine dentin (Kuboki et al, 1981b;Scott, 1980). Involvement of the a2 chain in cross-linking has been suggested in earlier studies (Fujii et al, 1975;Scott et al, 1976;Scott, 1980;Light & Bailey, 1985).…”

Section: Discussionmentioning

confidence: 83%

“…In this regard, we took special precautions to avoid contamination of the PL samples with type I collagen containing bone or tooth tissues. In contrast to all other collagen-containing tissues, PL collagen has relatively abundant reducible cross-links (Bailey, 1969;Fujii & Tanzer, 1974;Cannon & Davidson, 1977;Nielsen et al, 1983; Light & Bailey, 1979) and only small amounts of mature, nonreducible cross-links (Housley et al, 1975;Fujimoto et al, 1978;Eyre et al, 1981Eyre et al, , 1984; Walters & Eyre, 1983). This un-doubtedly reflects the exceptionally high rate of collagen turnover in this tissue (Sodek, 1977), Rapid turnover would not permit collagen fibrils to "age" and thus form mature cross-links.…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Intermolecular crosslinking and stereospecific molecular packing in type I collagen fibrils of the periodontal ligament

Yamauchi¹,

Katz²,

Mechanic³

1986

Biochemistry

133

119

View full text Add to dashboard Cite

A trypsin digest of denatured NaB3H4-reduced native bovine periodontal ligament was prepared and fractionated by gel filtration and cellulose ion-exchange column chromatography. Prior to trypsin digestion, a complete acid hydrolysate was subjected to analyses for nonreducible stable and reducible intermolecular cross-links. Minute amounts of the former and significant amounts of the reduced cross-links dihydroxylysinonorleucine (1.1 mol/mol of collagen), hydroxylysinonorleucine (0.9 mol/mol of collagen), and histidinohydroxymerodesmosine (0.6 mol/mol of collagen) were found. The covalent intermolecular cross-linked two-chained peptides that were isolated were subjected to amino acid and sequence analyses. The structures for the different two-chained linked peptides were alpha 1CB4-5(76-90)[Hyl-87] X alpha 1CB6-(993-22c)[Lysald-16c], alpha 1CB4-5(76-90)[Hyl-87] X alpha 1CB6(993-22c)[Hylald-16c], alpha 2CB4(76-90)[Hyl-87] X alpha 1CB6(993-22c)[Lysald-16c], and alpha 2CB4(76-90)[Hyl-87] X alpha 1CB6(993-22c)[Hylald-16c]. The cross-link in each peptide was glycosylated. This is the first characterization by sequence analysis of a cross-link involving Hyl-87 in an alpha 2 chain in collagen. A stoichiometric conversion of residue 16c aldehyde to an intermolecular cross-link in each of the COOH-terminal nonhelical peptide regions of both alpha 1 chains in a molecule of type I collagen was found. The ratio of alpha 1 to alpha 2 intermolecularly cross-linked chains involved was 3.3:1, indicating a stereospecific three-dimensional molecular packing of type I collagen molecules in bovine periodontal ligament.

show abstract

Section: Discussionmentioning

confidence: 83%

Section: Discussionmentioning

confidence: 99%

Intermolecular crosslinking and stereospecific molecular packing in type I collagen fibrils of the periodontal ligament

Yamauchi¹,

Katz²,

Mechanic³

1986

Biochemistry

133

119

View full text Add to dashboard Cite

show abstract

“…That is, the a2CB4 aldehyde donor peptide must form a helical region-helical region intermolecular cross-linkage. Fujii et al (1975) isolated a cross-link fragment peptide from calf bone collagen. This peptide was too small to be located definitively within the collagen sequence but the suggestion was made that it might join two helical regions involving al and a2 chains.…”

Section: Discussionmentioning

confidence: 99%

The identity of a cyanogen bromide fragment of bovine dentin collagen containing the site of an intermolecular cross-link

Scott¹,

Veis

Mechanic³

1976

Biochemistry

View full text Add to dashboard Cite

A peptide fraction isolated from a cyanogen bromide digest of bovine dentin collagen had a molecular weight of 46000. Its size and amino acid composition indicated that it could not consist of peptides derived from the cleavage of a single alpha chain. On reduction with tritiated sodium borohydride, radioactivity was incorporated primarily into 5, 5'-dihydroxylysinonorleucine without degradation at the peptide backbone. Periodate cleavage of the reduced or nonreduced peptide fraction generated one fragment of molecular weight 28000 and one of 18000 completely accounting for the size of the parent peptide. On amino acid analysis the constituent single-chain peptides were determined to be alpha2CB4 and alpha1CB6. Both peptides isolated after periodate oxidation of the tritiated borohydride reduced cross-link peptide were found to contain (3H)hydroxynorvaline. These data show that some hydroxylysine of alpha2CB4, a helical region peptide, was present in aldehyde form and could act as the aldehyde donor icross-link, Schiff's base formation. The only cross-linkage of this alpha2CB4 acting as an aldehyde donor peptide to alpha1CB6 would be a helical region to helical region bond, perhaps accounting for the unusual stability and low solubility of dentin collagen.

show abstract

“…Recently, a cross-linked tripeptide, prolylhydroxylysinohydroxynorleucylvaline, was isolated from calf bone collagen (Fujii et at., 1975) and its structure was consistent with a cross-link uniting two helical regions. This peptide, although small, could be attributed to very specific locations in the known primary structure of collagen a chains.…”

Section: Hydroxyaldol-histidinementioning

confidence: 99%

Cross-Linking

Tanzer

1976

Biochemistry of Collagen

View full text Add to dashboard Cite

Isolation and structure of a cross linked tripeptide from calf bone collagen

Cited by 17 publications

References 21 publications

Intermolecular crosslinking and stereospecific molecular packing in type I collagen fibrils of the periodontal ligament

Intermolecular crosslinking and stereospecific molecular packing in type I collagen fibrils of the periodontal ligament

The identity of a cyanogen bromide fragment of bovine dentin collagen containing the site of an intermolecular cross-link

Cross-Linking

Contact Info

Product

Resources

About