title: Permeability changes of plasma and lysosomal membranes in HeLa cells infected with rabbit poxvirus.
abstract: Infection of HeLa-cell monolayer cultures with rabbit poxvirus induces a marked decrease in cell-associated protein and in the activities of lactate dehydrogenase, acid phosphatase, and beta-glucuronidase. This effect begins to occur around 10 hours post-infection (p.i.) and is accompanied by a concomitant rise of these enzyme activities in the culture medium. Only few cells detach from infected monolayers and these cannot account for protein release. Virion release can be inhibited at 4 degrees C, whereas protein release cannot and it seems therefore that these events do not happen by a common mechanism. Moreover, penetration studies with [14C]-sucrose indicate that protein release reflects a true increase in plasma membrane permeability. Using the Gomori stain for acid phosphatase, a release of the enzyme into the cytoplasm around 8 hours p.i. can be confirmed rendering a causative role of lysosomal hydrolases in the pathogenesis of the observed plasma membrane permeability changes possible but not proving it.
mesh_terms: D000135:Acid Phosphatase / Q000378:metabolism; D002462:Cell Membrane / Q000378:metabolism*; D002463:Cell Membrane Permeability; D005966:Glucuronidase / Q000378:metabolism; D006367:HeLa Cells; D007770:L-Lactate Dehydrogenase / Q000378:metabolism; D008247:Lysosomes / Q000378:metabolism*; D009363:Neoplasm Proteins / Q000378:metabolism; D011212:Poxviridae / Q000254:growth & development*; D013395:Sucrose / Q000378:metabolism; D013696:Temperature; D014616:Vaccinia virus / Q000254:growth & development*
chemical_list: D009363:Neoplasm Proteins; D013395:Sucrose; D007770:L-Lactate Dehydrogenase; D000135:Acid Phosphatase; D005966:Glucuronidase