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The biosynthesis of the collagenous components of the rat lens capsule and glomerular basement membrane (GBM) has been investigated. Intact lenses, isolated lens capsules and isolated renal glomeruli incorporate [³H]proline into 4-hydroxy[³H]proline containing polypeptides of approximate molecular weight 180,000 (analysed under reducing conditions). These polypeptides are deposited in the deoxycholate-insoluble basement membrane matrix and correspond to subunits of the intact, non-radioactive basement membranes. With time a proportion of the newly synthesised collagenous polypeptides become assembled into high molecular weight aggregates which are stabilized by lysine-and/or hydroxylysine-derived cross-links. Despite the similar patterns of collagen biosynthesis in the rat lens capsule and GBM, the latter has a more complex polypeptide composition the origin of which remains uncertain.

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