ArticleNeurochemical research1999
Effects of lead on adenylate cyclase activity in rat cerebral cortex.
Article in Neurochemical research, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
2 citing papers in PubMed, 9 citations in OpenAlex.
- Lead and calcium crosstalk tempted acrosome damage and hyperpolarization of spermatozoa: signaling and ultra-structural evidences.Biological research · 2024Article
- Metal toxicity at the synapse: presynaptic, postsynaptic, and long-term effects.Journal of toxicology · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lead decreased in a dose dependent manner the basal AC activity in membranes of rat cerebral cortex (IC50 = 2.5 +/- 0.1 microM). In membranes preincubated under basal conditions, AC activity was stimulated by approximately two and fourfold by 10 microM Gpp(NH)p or forskolin, respectively. Under basal conditions, lead (3 microM) inhibited enzyme activity up to 50%, but was not able to inhibit the Gpp(NH)p- or the forskolin-stimulated AC activity. However, in membranes preincubated with Gpp(NH)p (10 microM), lead (3 microM) had no significant effect on enzyme activity, but it partly blocked the stimulation of AC activity elicited by forskolin (10 microM). In membranes preincubated with 10 microM lead, the addition of 10 microM Gpp(NH)p or forskolin in the incubation medium did not stimulate AC activity. However, when added together in the incubation medium Gpp(NH)p + forskolin produced an increase in enzyme activity. In membranes preincubated with 10 microM lead + 10 microM Gpp(NH)p, Gpp(NH)p (10 microM) or forskolin (10 microM) added alone or in combination to the incubation medium did not stimulate AC activity. Moreover, under these latter conditions lead had no further effect on enzyme activity. These results indicate that lead may interact with G-proteins and with the catalytic subunit of cerebral cortical AC to produce inhibition of the enzyme activity.
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