作者: Teresa L. Wright , F.Joseph Roll , Albert L. Jones , Richard A. Weisiger
DOI: 10.1016/0016-5085(88)90435-0
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摘要: Hepatitis B virus binds avidly to albumin polymers, which in turn may mediate viral attachment liver cells. This hypothesis is critically dependent on prior results obtained using glutaraldehyde-polymerized human serum as a model for naturally occurring species. We used the perfused rat characterize uptake, cellular distribution, and metabolism of albumin. 125I-glutaraldehyde-polymerized was efficiently removed from perfusate by (29% extraction). However, few autoradiographic grains were located over hepatic parenchymal cells (6%). Instead, most appeared be endothelial (59%) or Kupffer (31%) Hepatic uptake strongly inhibited formaldehyde-treated monomeric albumin, known ligand scavenger receptor chemically modified proteins. After rapidly degraded released into (74% within 60 min). process blocked chloroquine leupeptin, suggesting that it involves lysosomal acid hydrolases. conclude cleared pathway. Glutaraldehyde-polymerized therefore appears poor predicting handling species bound hepatitis virions. Even if particles follow this pathway, would enter hepatocytes.