In vitro formation of intramolecular crosslinks in tropocollagen

Abstract

Administration of penicillamine (β,β, dimethyl cysteine) to rats causes a disturbance of collagen metabolism that resembles lathyrism (Nimni and Bavetta, 1965). The neutral salt soluble collagen which accumulates in rats treated with penicillamine consists almost exclusively of α components (Nimni, 1965), but once extracted from tissues and purified, it forms stable fibers at 37°C ( Deshmukh and Nimni, 1969a). This contrasts with lathyritic collagen which forms unstable fibers that redissolve in cold neutral salt solutions ( Gross, 1963). This fundamental difference in behavior suggested that the soluble collagen extracted from the penicillamine treated animals should be capable of generating stable intramolecular as well as intermolecular crosslinks. The present communication describes the formation of intramolecular crosslinks in vitro , which in turn, suggests a suitable model for the further study of the biosynthesis and characterization of this type of crosslink.