Effects of in vitro N-glucosylation on type-I collagen fibrillogenesis.

Acid-soluble collagen from rat tail tendon was glucosylated in vitro and fibrillogenesis parameters were determined first at 35 degrees C then at 4 degrees C. Increased lag phase and half time were shown to be related to the amount of non-enzymatically bound glucose, probably due to a decrease of hydrophobic interactions at this early stage of fibril formation. The absence of intermolecular cross-links and the partial redissolution of fibrils of 4 degrees C, as investigated both by turbidimetry and electron microscopy, suggests a defect in the maturation process in glucosylated collagen fibrils.