title: Glomerular permeability in the bullfrog Rana catesbeiana.
abstract: Filtration studies suggest similar size pores in the glomerular filters of mammals and amphibians. However, the glomerular wall in the bullfrog exhibits several structural features not found in mammals. The subendothelial space of the basement membrane is often greatly enlarged and infiltrated by cellular elements. The lamina densa of the basement membrane shows extensive variation in thickness and packing of its filaments. On the other hand, the epithelial slits in the bullfrog are closed by a slit diaphragm which appears similar in size and structure to the slit diaphragm in mammals. Horse spleen ferritin, a protein with a hydrodynamic radius of 61 A, was used as an ultrastructural tracer to determine whether the highly variable structure of the basement membrane renders this layer more permeable than its mammalian counterpart. Within 10 min after intravenous injection, ferritin was found throughout the basement membrane and often in clusters within the subepithelial layer adjacent to the slit diaphragm. Virtually no ferritin was found within the urinary space, podocytes, or cells of the proximal tubule. Ferritin distribution was the same in both superficial glomeruli and more deeply lying glomeruli regardless of the method of fixation. These results indicate that in the bullfrog the slit diaphragm is a principal filtration barrier to ferritin and thus to smaller plasma proteins.
mesh_terms: D000818:Animals; D001001:Anura; D001485:Basement Membrane / Q000648:ultrastructure; D002196:Capillaries / Q000648:ultrastructure; D002199:Capillary Permeability; D004727:Endothelium / Q000648:ultrastructure; D005293:Ferritins / Q000378:metabolism; D007678:Kidney Glomerulus / Q000098:blood supply / Q000502:physiology / Q000648:ultrastructure*; D011892:Rana catesbeiana
chemical_list: D005293:Ferritins