epsilon(gamma-Glutamyl)lysine crosslinks are concentrated in a non-collagenous microfibrillar fraction of cartilage

Biochem Cell Biol. 1997;75(1):89-91. doi: 10.1139/o96-060.


Fractions of rib cartilage were obtained by homogenization and extracted with 4 M guanidinium chloride, and the washed residue was digested with purified collagenase. Differential centrifugation of the insoluble residue from this digestion yielded a non-collagenous fraction that earlier work had shown to contain microfibrils. This material contains a much higher concentration of epsilon(gamma-glutamyl)lysine than the ribs or any of the other cartilage fractions. This transglutaminase-derived crosslink may be a common component of extracellular matrix microfibrils.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cartilage / chemistry*
  • Dipeptides / chemistry*
  • Dipeptides / metabolism
  • Fibrillins
  • Microfilament Proteins / chemistry
  • Rabbits
  • Solubility
  • Transglutaminases / metabolism


  • Dipeptides
  • Fibrillins
  • Microfilament Proteins
  • epsilon-(gamma-glutamyl)-lysine
  • Transglutaminases