Intracellular pathways of endocytosed transferrin and non-specific tracers in epithelial cells lining the rete testis of the rat.
The uptake and pathway of different markers and ligands for fluid-phase, adsorptive and receptor mediated endocytosis were analyzed in the epithelial cells lining the rete testis after their infusion into the lumen of these anastomotic channels. At 2 min after injection, diferric transferrin bound to colloidal gold was seen attached to the apical plasma membrane and to the membrane of endocytic coated and uncoated pits and vesicles. The injection of transferrin-gold in the presence of a 100-fold excess of unconjugated diferric transferrin revealed no binding or internalization of transferrin-gold. Similarly, apotransferrin-gold was neither bound to the apical plasma membrane nor internalized by these cells. These results thus indicate the presence of specific binding sites for diferric transferrin. At 5 min, internalized diferric transferrin-gold reached endosomes. At 15 and 30 min, the endosomes were still labeled but at these time intervals the transferrin-gold also appeared in tubular elements connected to or associated with these bodies or seen in close proximity to the apical plasma membrane. At 60 and 90 min, most of the transferrin-gold was no longer present in these organelles and was seen only exceptionally in secondary lysosomes. These results thus suggest that the tubular elements may be involved in the recycling of transferrin back to the lumen of the rete testis. The coinjection of transferrin-gold and the fluid-phase marker native ferritin revealed that both proteins were often internalized in the same endocytic pit and vesicle and shared the same endosome.(ABSTRACT TRUNCATED AT 250 WORDS)
D000818:Animals; D001692:Biological Transport; D004705:Endocytosis; D006651:Histocytochemistry; D006801:Humans; D007700:Kinetics; D008247:Lysosomes / Q000378:metabolism / Q000648:ultrastructure; D008297:Male; D051381:Rats; D011956:Receptors, Cell Surface / Q000378:metabolism*; D011990:Receptors, Transferrin; D012152:Rete Testis / Q000378:metabolism* / Q000648:ultrastructure; D013737:Testis / Q000378:metabolism*; D014168:Transferrin / Q000378:metabolism*
D011956:Receptors, Cell Surface; D011990:Receptors, Transferrin; D014168:Transferrin