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Bonilla, A. M.

Publications and source records attributed to Bonilla, A. M..

2 recordsLinked to original sources

Involvement of monoaminergic and nitrergic pathways in the behavioral effects and acute toxicity of Gomphrena perennis L. tincture in mice

Gomphrena perennis L. possesses a rich phenolic profile and has demonstrated cardiovascular and anti-inflammatory activities; however, its neuropharmacological properties re-main unexplored. The behavioral effects, underlying mechanisms, and acute toxicity of Gomphrena perennis tincture (GphT) were investigated in mice. GphT showed no signs of acute toxicity. Furthermore, it did not alter the number of cross lines in the open field test (OFT), but it induced anxiogenic responses in the elevated plus-maze test (EPM) and the novelty-suppressed feeding test (NSFT), which were reversed by L-NAME, a non-selective nitric oxide synthases inhibitor. GphT also reduced immobility time in the forced swimming test (FST) and the tail suspension test (TST). This antidepressant-like effect was prevented by haloperidol (D1/D2 antagonist), ketanserin (5-HT2A/2C antagonist), L-NAME, and sildenafil (PDE5 inhibitor), while propranolol ({beta}-blocker), prazosin (1-an-tagonist), yohimbine (2-antagonist), and ondansetron (5-HT3-antagonist) did not modify it. Therefore, GphT produced anxiogenic and antidepressant-like effects without im-pairing locomotion. These effects involve dopaminergic and serotonergic pathways and depend on nitric oxide-mediated signaling, suggesting that GphT exerts a modulatory influence on interconnected neurochemical systems.

pharmacology and toxicology↗

Co-option of Plasmodium falciparum PP1 for egress from host erythrocytes

Asexual proliferation of the Plasmodium parasites that cause malaria follow a developmental program that alternates non-canonical intraerythrocytic replication with dissemination to new host cells. We carried out a functional analysis of the Plasmodium falciparum homolog of Protein Phosphatase 1 (PfPP1), a universally conserved cell cycle factor in eukaryotes, to investigate regulation of parasite proliferation. PfPP1 is indeed required for efficient replication, but is absolutely essential for egress of parasites from host red blood cells. A phosphoproteomic screen and chemical-genetic analysis provided evidence for a HECT E3 protein-ubiquitin ligase, as well as a fusion protein with guanylyl cyclase and phospholipid transporter domains, as functional targets of PfPP1. Extracellular phosphatidylcholine stimulates PfPP1-dependent egress. Parasite PfPP1 acts as a master regulator that can integrate multiple cell-intrinsic pathways with external signals to direct parasite egress from host cells.

microbiology↗