1. Segmental variations in the organization of the endoplasmic reticulum of the rat nephron
- Author
-
P. Gaffiero, Michel Bergeron, and Georges Thiery
- Subjects
Male ,Histology ,Nephron ,Endoplasmic Reticulum ,Bone canaliculus ,Pathology and Forensic Medicine ,Kidney Tubules, Proximal ,chemistry.chemical_compound ,medicine ,Animals ,Intercalated Cell ,Epithelial polarity ,Microvilli ,Endoplasmic reticulum ,Cell Membrane ,Rats, Inbred Strains ,Nephrons ,Cell Biology ,Rats ,Cell biology ,Microscopy, Electron ,medicine.anatomical_structure ,Tubule ,Osmium tetroxide ,chemistry ,Loop of Henle ,Ultrastructure ,Female - Abstract
The spatial organization of endoplasmic reticulum (ER) was examined in all segments of rat nephron. Tissues were fixed with glutaraldehyde, impregnated "en bloc" with osmium tetroxide, prepared for and examined by standard (80-100 kV) and high voltage (1 mEV) transmission electron microscopy. In all proximal tubule cells, ER forms a continuous and extensive network of canaliculi and abundant fenestrated saccules which surround mitochondria and cytoplasmic bodies; the cage-like structure of the fenestrated saccules was most evident around the spherical mitochondria of the S3 segment. In the cells of the distal straight and convoluted tubules, the network consists mostly of canaliculi with rare non-fenestrated saccules. The ER network of canaliculi is particularly rich in intercalated cells, in contrast with its rudimentary appearance in the adjacent principal cells of the collecting tubule. In fact, in these cells there are few isolated ER cisternae and they are rarely impregnated. The nuclear envelope is well impregnated in most cells throughout the various segments. Segmental variations in ER organization and its relative abundance are most likely related to the well, established functional heterogeneity of the nephron segments. Moreover, the extensive and unique organization among mitochondria, ER and the basolateral membrane suggests that these three organelles function as a unit which is related to active electrolyte transport. In addition, because of its transepithelial organization, ER may well constitute a transcellular pathway for molecules.
- Published
- 1987