Cross-linking and stereospecific structure of collagen in mineralized and nonmineralized skeletal tissues.

Abstract:

:Molecular distributions of the intermolecular cross-links in fetal bovine bone type I collagen fibrils were quantitatively determined and compared with those of periodontal ligament. Results indicated that Hyl and Lys residues in the COOH-terminal nonhelical peptide portions (residues 16C) of both alpha 1 chains were quantitatively converted to aldehydes. These in turn stoichiometrically formed cross-links with residues Hyl-87 on both alpha 1 and alpha 2 chains of neighboring molecules. The ratio of cross-linked alpha 1 to alpha 2 chains was 3.5 to 1 indicating a stereospecific packing of collagen molecules in the fibrils similar manner to periodontal ligament collagen. It was found that there were few aldehyde derived cross-links in the NH2-terminal nonhelical portions of the bone type I collagen. The relative paucity of the cross-links in NH2-terminal region of bone collagens may favor mineralization.

journal_name

Connect Tissue Res

authors

Yamauchi M,Katz EP,Otsubo K,Teraoka K,Mechanic GL

doi

10.3109/03008208909050006

subject

Has Abstract

pub_date

1989-01-01 00:00:00

pages

159-67; discussion 168-9

issue

1-4

eissn

0300-8207

issn

1607-8438

journal_volume

21

pub_type

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