Heathcote J G, Muhammed S, Smith E F, Grant M E
Ren Physiol. 1980;3(1-6):36-40. doi: 10.1159/000172739.
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 GMB, the latter has a more complex polypeptide composition the origin of which remains uncertain.
对大鼠晶状体囊膜和肾小球基底膜(GBM)胶原成分的生物合成进行了研究。完整的晶状体、分离的晶状体囊膜和分离的肾肾小球将[3H]脯氨酸掺入分子量约为180,000的含4-羟基[3H]脯氨酸的多肽中(在还原条件下分析)。这些多肽沉积在脱氧胆酸盐不溶性基底膜基质中,对应于完整的、非放射性基底膜的亚基。随着时间的推移,一部分新合成的胶原多肽组装成高分子量聚集体,这些聚集体通过赖氨酸和/或羟赖氨酸衍生的交联而稳定。尽管大鼠晶状体囊膜和GBM中的胶原生物合成模式相似,但后者的多肽组成更为复杂,其来源尚不确定。