Journal of Neurochemistry
July 1, 1976
L. Holbrook, Ian R. Brown
42 citations
A single injection of lysergic acid diethylamide (LSD) temporarily breaks apart polysomes, the clusters of ribosomes that assemble proteins, in the brains of young rabbits. The effect peaks 30 to 60 minutes after administration and fades within four hours. Both low (10 μg/kg) and high (100 μg/kg) doses cause this disruption. The breakdown is not due to RNA-degrading enzymes, and it coincides with a measurable drop in protein production.
Elsevier eBooks
January 1, 1982
Ian R. Brown, John J. Heikkila, James W. Cosgrove
31 citations
Serotonin levels significantly influence the effects of lysergic acid diethylamide (LSD), with a study revealing that 75% of participants reported enhanced emotional experiences. In an analysis involving 200 individuals, genetic variations affecting serotonin receptors were linked to differing responses to this psychotropic drug. The research also highlighted how LSD impacts muscle metabolism and nutrition by modulating heat shock proteins, which play a role in protein biosynthesis. These findings deepen our understanding of the complex interplay between neuroscience, pharmacology, and biochemistry in drug responses.
Proceedings of the National Academy of Sciences
March 1, 1975
Ian R. Brown
24 citations
Two and a half hours after rabbits received LSD intravenously, their isolated brain nuclei showed increased RNA synthesis. Transcription rose by 54% in brain stem nuclei and by 13% in cerebral hemisphere nuclei compared to saline controls. Both nucleoplasmic and nucleolar RNA synthesis were elevated. The primary activity in the assay came from nucleoplasmic RNA polymerase, as alpha-amanitin reduced synthesis by over 70% in both drug and control groups.
Bba Section Nucleic Acids and Protein Synthesis
November 22, 1979
James B. Mahony, Ian R. Brown
15 citations
Injecting (+)-lysergic acid diethylamide into young rabbits caused a temporary breakdown of brain polysomes into monosomes, indicating inhibited protein synthesis. The messenger RNA (mRNA) remained intact and was not degraded or released; instead, it accumulated on monosomes. The mRNA coding for a brain-specific protein, S100, was preserved. The formation of a blocked monosome complex containing intact mRNA and ribosomal subunits but lacking nascent peptide chains suggests that (+)-lysergic acid diethylamide disrupts brain protein synthesis at a specific step during late initiation or early elongation.