Polycation-cell surface interactions and plasma membrane compartments in mammals. Interference of oligocation with polycationic condensation.
At lower concentrations, polyarginine, polylysine, protamine, histones H1, H2A, H2B and H3 cause lysis of human erythrocytes, whereas at higher concentrations inner histones are not hemolytic but induce only surface condensation and alterations in the cell-shape. Antibody coated erythrocytes treated with polyarginine result in ghost-like spheres having globular bodies 1 micron in diameter on the surface. Human fibroblasts and lymphocytes, and Ehrlich ascites cells treated with polyarginine also form surface globular bodies similar in size. Nucleate cell-polyarginine mixtures with lower polycation doses result in cytolysis, while higher polycation doses produce pyknosis of the cell surface accompanied by reorganization of a membrane-like structure. Changes in spectrofluorometric values result from 1,6-diphenyl-1,3, 5-hexatrien binding to cell lipids, match the plasma membrane alterations. Reciprocal shake incubation amplifies and/or conditions these polycation-induced alterations. The homogeneity of pyknotic surface bodies and the apparent polycationic membrane reorganization requiring oscillatory friction forces suggest the preexistence of a multizonal glycocalyx distribution corresponding to plasma membrane compartments. The possible role of this compartmentalization in receptor and membrane recycling, as well as the involvement of reversible catalytic-like polycation condensation in macromolecular changes are discussed.
D000818:Animals; D002286:Carcinoma, Ehrlich Tumor / Q000473:pathology; D002460:Cell Line; D002462:Cell Membrane / Q000187:drug effects / Q000648:ultrastructure*; D004622:Embryo, Mammalian; D004910:Erythrocyte Membrane / Q000187:drug effects / Q000648:ultrastructure*; D005347:Fibroblasts / Q000166:cytology; D006461:Hemolysis / Q000187:drug effects; D006657:Histones / Q000494:pharmacology*; D006801:Humans; D051379:Mice; D010455:Peptides / Q000494:pharmacology*; D011073:Polyamines / Q000494:pharmacology*; D011107:Polylysine / Q000494:pharmacology; D011479:Protamines / Q000494:pharmacology
D006657:Histones; D010455:Peptides; D011073:Polyamines; D011479:Protamines; D011107:Polylysine; C015462:polyarginine