source: Journal of Clinical Pathology
The title of this paper has been chosen to contrast with the term ‘collagen diseases’ by which Klemperer and his colleagues (Klemperer et al., 1942) designated the group of diseases that included rheumatoid arthritis among others. In 1959 the basic lesion in osteolathyrism-an experimental condition produced in rats or chick embryos by treatment with the sweet pea seed ‘lathyrus factor’ (/3-aminopropionitrile (BAPN)) and signs that included slipped epiphyses, tendon avulsion, kyphoscoliosis, hernias, and rupture of the aorta-was shown to be a defect in the cross-linking of collagen (Levene and Gross, 1959). The mechanism was believed to be the blocking of aldehyde groups in the collagen molecule (Levene, 1962) and essential for normal cross-linking (Tanzer, 1973; Baileyet al., 1974). Shortly afterwards, Pinnell and Martin (1968) isolated the enzyme responsible for the normal formation of these aldehydic precursors of the cross links. This enzyme, called lysyl oxidase, required copper as an essential cofactor and acted byoxidativelydeaminating specific peptidyl lysine or hydroxylysine residues in the collagen molecule to produce aldehydes which subsequently formed either Schiff bases with amino groups in adjoining chains or condensed by the aldol reaction with adjoining aldehydic groups (Siegel et al., 1970; Siegel, 1974).
University of Cambridge
full text source