Effect of vitamin B6 deficiency on the crosslink formation of collagen

With the recent advances m collagen chemistry it became apparent that the mitial stage m the crosshnk formation of collagen 1s the enzymic syntheas of aldehydes by removal of e-amino groups of certam lysine and hydroxyiy~ne resrdues [ 1,2]. Tlus enzyme named Iysyl oxidase, one of the amine oxidases, has been purified to hrgh specriic activity and shown to be actrve upon both lysyl and hydroxylysyl groups in collagen and elastin [3,4]. It is well known that amine oxidases contain copper, and some of them require pyridoxal phosphate for their activity [5-73. It can be mferred therefore that vitamin B6 is also required for enzymic actrnty of lysyl oxidase. Thrs posstbrhty has been reinforced by the findings that partial purificatron of lysyl oxrdase from cartilage of chick embryos inJected wrth [G-3H]py~do~ne hydroc~onde revealed a smgle peak of ra&oactrvrty comadmg with a single peak of enzyme activity, and lysyl oxrdase actrvrty was mhrbrted after mcubatron wrth rsomcotmic acid hydrazide [8]. In order to gam further mformatron on thus pos~b~ty, we have lnvestlgated aldehyde and crosshnk formation of skin and bone collagens from vitamm B6-deficient rats.