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Biomedical subjects

P Sandler

Publications and source records attributed to P Sandler.

8 recordsLinked to original sources
PubMed1991

Brain-derived cells contain a specific binding site for Gp120 which is not the CD4 antigen.

Infection with the human immunodeficiency virus (HIV-1) often produces a set of neuropsychiatric dysfunctions which have been termed the AIDS dementia complex. This complex appears due to the infection of brain cells by HIV-1. If so, brain cells might be expected to contain a binding site for the same viral envelope glycoprotein that enables HIV-1 to bind to other cells (e.g. CD4+ T-cells), gp120. The present study shows that the cells of the brain-derived U-138MG, U-373MG, SK-N-MC and SK-N-SH cell lines bind gp120 in an inhibitable fashion. Binding of gp120 to these cells is inhibited by the dyes Aurintricarboxylic acid (ATA) and Evans blue (EB), which are known to inhibit specific gp120 and HIV-1 binding, and block HIV-1 infection, in CD4-expressing cells. Binding is not inhibited by Aurin, a dye related to ATA but lacking its anti-HIV effects. As expected, anti-CD4 antibodies are ineffective in blocking gp120 binding to brain-derived cells. These results suggest that human brain-derived cells possess a specific binding site for gp120 that is not the CD4 antigen.

Antibodies, Monoclonal↗
PubMed1989

Erythromycin-induced ribosome stall in the ermA leader: a barricade to 5'-to-3' nucleolytic cleavage of the ermA transcript.

The Staphylococcus aureus ermA gene, whose product confers resistance to the macrolide-lincosamide-streptogramin B family of antibiotics, is induced at the level of translation by nanomolar concentrations of erythromycin. Erythromycin also specifically stabilizes ermA transcripts, and the induced stabilization requires in-phase translation of at least one of two small leader peptides in the 5' leader region of the transcript. Erythromycin-induced mRNA stabilization was tested in three constructions in which the ermA transcript was elongated by making insertions at the ermA transcription start. Whereas mRNA downstream of the leader peptide is stabilized by erythromycin, mRNA upstream is not. In the presence of erythromycin, specific mRNA decay intermediates in both the extended ermA genes and the wild-type ermA gene were detected by both Northern blotting and S1 nuclease mapping. The 5' ends of the intermediates map to the sequences that encode each of the two ermA leader peptides, suggesting that the intermediates are produced by stalled erythromycin-bound ribosomes acting as barricades to degradation by 5'-to-3' RNases. In addition, whereas erythromycin was found previously to stabilize ermA transcripts only physically, an ermC-cat-86 hybrid transcript was stabilized both physically and functionally by erythromycin.

Amino Acid Sequence↗
PubMed1988

Erythromycin-induced stabilization of ermA messenger RNA in Staphylococcus aureus and Bacillus subtilis.

Erythromycin-induced stabilization of ermA mRNA was studied in Staphylococcus aureus, its original host background, and in Bacillus subtilis, subcloned on plasmid vectors. By RNA blot analysis it was shown that 40 nM-erythromycin specifically increased the chemical half-life of ermA mRNA from 2.5 to 17.5 minutes whereas the half-life of cat-86 mRNA was not increased by erythromycin. While expression of ermA has been shown to be induced by erythromycin at the level of translation, our studies with three ermA constitutive mutants demonstrated that mRNA stabilization in growing cells occurred independently of induced gene expression, suggesting that the stabilized mRNA was not functional for protein synthesis. Studies of ermA/lacZ fusions demonstrated that the 5' end of the mRNA was sufficient to confer stabilization. Translation of specific amino acid codons in a leader peptide located at the extreme 5' end of the mRNA was required for the erythromycin-induced stabilization as a frameshift mutation introduced into the leader peptide determinant abolished stabilization. By S1 mapping, no differences were detected in the length of the 5' or 3' end of ermA mRNA with the addition of erythromycin, indicating that the stabilized transcript was not processed at its ends.

Bacillus subtilis↗
PubMed1981

Hyperlipidemia in children with chronic renal insufficiency.

Total serum cholesterol, phospholipids, and triglyceride levels, lipoprotein fractionation, and plasma parathormone levels were measured in a group of 31 nonnephrotic children with various levels of renal function and on hemodialysis. Group A served as controls and consisted of eight healthy children with glomerular filtration rate (GFR) greater than 110 ml/min/1.73 m2. Group B consisted of six children with GFR on 60 to 95 ml/min/1.73 m2. Group C consisted of nine children with GFR of 10 to 40 ml/min/1.73 m2, and group D consisted of eight children on maintenance hemodialysis with GFR of 0 to 5 ml/min/1.73 m2. Among the groups, there were no significant differences in total serum cholesterol and phospholipid levels. A significant (P less than 0.05) increase in triglyceride levels was observed in patient groups C and D. Lipoprotein fractionation revealed a significant increase (P less than 0.05) in the pre-beta lipoprotein levels (very low density lipoproteins) in patients in groups D with 63% of these patients demonstrating a type IV lipoprotein pattern. There were no significant differences observed in the beta lipoproteins (low-density lipoproteins). However, the alpha lipoproteins (high-density lipoproteins) decreased significantly (P less than 0.05) in patients whose GFR was below 40 ml/min/1.73 m2 (group C) as well as patients in group D. Absolute plasma parathormone levels did not significantly correlate with serum triglyceride levels did not significantly correlate with serum triglyceride levels and remained normal until after the onset of hemodialysis when they increased significantly in all patients.

Adolescent↗