epsilon(gamma-Glutamyl)lysine crosslinks are concentrated in a non-collagenous microfibrillar fraction of cartilage.
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.
Bowness
J M
JM
Department of Biochemistry and Molecular Biology, University of Manitoba, Faculty of Medicine, Winnipeg, Canada. Bowness@cc.umanitoba.ca
Tarr
A H
AH
D000818:Animals; D002356:Cartilage / Q000737:chemistry*; D004151:Dipeptides / Q000737:chemistry* / Q000378:metabolism; D000071837:Fibrillins; D008840:Microfilament Proteins / Q000737:chemistry; D011817:Rabbits; D012995:Solubility; D011503:Transglutaminases / Q000378:metabolism
D004151:Dipeptides; D000071837:Fibrillins; D008840:Microfilament Proteins; C001299:epsilon-(gamma-glutamyl)-lysine; D011503:Transglutaminases