Studies on the Postnatal Development of the Rat Liver Plasma Membrane Following Maternal Ethanol Ingestion

Studies on the developing rat liver and on the structure and function of the postnatal rat liver plasma membrane were carried out following maternal consumption of alcohol during pregnancy and lactation. A developmental study of alcohol dehydrogenase (ADH) indicated that both the activity and certain kinetic properties of the enzyme from the progeny of alcohol-fed and pair-fed mothers were similar. Fatty liver, however, developed in the alcoholic progeny only after ADH appeared on day 19 of gestation. […]Des études ont été effectuées sur le développment du foie de rat et sur la structure et la fonction de la membrane cytoplasmique postnatale de foie de rat à la suite de l'ingestion maternelle d'alcool pendant les périodes de grossesse et de lactation. Une étude sur le développement de l'alcool déshydrogénase (ADH) n'a révelé aucune différence dans l'activité et certaines propriétés cinétiques de l'enzyme chez la progéniture d'animaux témoins et alcoolises. Néanmoins, une accumulation d'acides gras dans le foie des rats alcoolises a coïncidé avec l'apparition de l'ADH au dix-neuvième jour de la gestation. […

Identification of Retroviral Late Domains as Determinants of Particle Size

Retroviral Gag proteins, in the absence of any other viral products, induce budding and release of spherical, virus-like particles from the plasma membrane. Gag-produced particles, like those of authentic retrovirions, are not uniform in diameter but nevertheless fall within a fairly narrow distribution of sizes. For the human immunodeficiency virus type 1 (HIV-1) Gag protein, we recently reported that elements important for controlling particle size are contained within the C-terminal region of Gag, especially within the p6 sequence (L. Garnier, L. Ratner, B. Rovinski, S.-X. Cao, and J. W. Wills, J. Virol. 72:4667–4677, 1998). Deletions and substitutions throughout this sequence result in the release of very large particles. Because the size determinant could not be mapped to any one of the previously defined functions within p6, it seemed likely that its activity requires the overall proper folding of this region of Gag. This left open the possibility of the size determinant residing in a subdomain of p6, and in this study, we examined whether the late domain (the region of Gag that is critical for the virus-cell separation step) is involved in controlling particle size. We found that particles of normal size are produced when p6 is replaced with the totally unrelated late domain sequences from Rous sarcoma virus (contained in its p2b sequence) or equine infectious anemia virus (contained in p9). In addition, we found that the large particles released in the absence of p6 require the entire CA and adjacent spacer peptide sequences, whereas these internal sequences of HIV-1 Gag are not needed for budding (or proper size) when a late domain is present. Thus, it appears the requirements for budding are very different in the presence and absence of p6