Purpose: Conjugation of bovine serum albumin (BSA) with riboflavin (BSA-riboflavin) increases its uptake into cultured epithelial cells. Our purpose was to determine whether transport of BSA-riboflavin across the intact distal pulmonary epithelium is also increased, and whether transcytosis plays a role.
Methods: In anesthetized rats, we instilled 3H-BSA-riboflavin or 3H-BSA into the trachea and measured their appearance in blood. In isolated, perfused rat lungs we measured the distal pulmonary epithelium permeability-surface area product (PS) for FITC-BSA or FITC-BSA-riboflavin.
Results: In intact rats we found 2.1 times more 3H-BSA-riboflavin than 3H-BSA appeared in blood 60 min after intratracheal instillation of the protein. In isolated, perfused rat lungs we found that BSA-riboflavin had double the PS of BSA (2.63 vs. 1.46 x 10(-5) cm3/sec). The addition of transcytosis inhibitors monensin or nocodazole (both 3 x 10(-5) M) reduced the BSA-riboflavin PS to that of BSA and had no effect on the PS of unconjugated BSA. Simultaneous measurements of 3H-sucrose PS showed no differences in paracellular transport among any of the experimental groups.
Conclusions: Conjugation with riboflavin increases the flux of BSA across the distal pulmonary epithelium. The increased transport appears to be due to transcytosis, which apparently does not play a significant role in the movement of unconjugated BSA across the distal pulmonary epithelium.