Scavenger receptors are multifunctional integral membrane proteins that mediate the endocytosis of many different macromolecular polyanions and also participate in host defence reactions and cell adherance. In Atlantic cod (Gadus morhua L.), two intravenously injected scavenger receptor ligands, [125I]tyramine-cellobiose-labelled formaldehyde-treated serum albumin (125I-TC-FSA) and 125I-labelled N-terminal propeptide of type I procollagen (125I-PINP), distributed mainly to the heart. Cellular uptake was visualized by injections of fluorescently labelled FSA (FITC-FSA), which was recovered in discrete vesicles in endocardial endothelial cells of both heart chambers. Studies in vitro showed that radioiodinated FSA and PINP were endocytosed and degraded very efficiently by cultured atrial endocardial endothelial cells. Moreover, uptake of 125I-FSA was Ca2+-independent. Out of a range of unlabelled ligands, only the scavenger receptor ligands FITC-FSA, polyinosinic acid and, to a varying extent, FSA, acetylated low-density lipoprotein (AcLDL) and PINP, were able to compete with radioiodinated FSA, PINP or AcLDL for uptake in isolated endocardial cells. From our findings, we conclude that the endocardial endothelial cells are major carriers of scavenger receptors in cod. In addition, our results strengthen the hypothesis that these cells in cod play the same important function as that established for the scavenger endothelial cells of the mammalian liver.
Internalization
of scavenger receptor ligands by cortical neurons