title: A role for anionic sites in epithelial architecture. Effects of cationic polymers on cell membrane structure.
abstract: The effects of several cationic polymers (poly-L-lysines, protamine, and histone) on rabbit gall bladder epithelial cells were studied to explore possible roles for negative sites in the membrane. The tissue was bathed for 30 min at 37 degrees C in Ringer's solutions containing from 0.1 to 100.0 microg/ml of cationic polymers, and subsequently was fixed with 1% OsO(4) and examined with the electron microscope. All cationic polymers, at appropriate concentrations, produced similar changes in membrane structure. Adjacent membranes frequently were fused. Membrane structures such as microvilli lost rigidity. Cell membranes showed an apparent increase in permeability as judged by osmotically traumatized cells. These results indicate that fixed anionic sites play significant roles in stabilizing epithelial membrane structures.
mesh_terms: D000818:Animals; D002448:Cell Adhesion / Q000187:drug effects; D002462:Cell Membrane / Q000187:drug effects*; D002463:Cell Membrane Permeability / Q000187:drug effects; D004847:Epithelial Cells; D004848:Epithelium / Q000187:drug effects; D005704:Gallbladder / Q000166:cytology; D006493:Heparin / Q000494:pharmacology; D006657:Histones / Q000494:pharmacology*; D008239:Lysine / Q000494:pharmacology*; D008854:Microscopy, Electron; D008933:Mitochondrial Swelling / Q000187:drug effects; D011108:Polymers / Q000494:pharmacology*; D011479:Protamines / Q000494:pharmacology*; D011817:Rabbits
chemical_list: D006657:Histones; D011108:Polymers; D011479:Protamines; D006493:Heparin; D008239:Lysine