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1.
Mol Cell ; 2024 Jul 26.
Artigo em Inglês | MEDLINE | ID: mdl-39084218

RESUMO

Cell size and growth are intimately related across the evolutionary scale, but whether cell size is important to attain maximal growth or fitness is still an open question. We show that growth rate is a non-monotonic function of cell volume, with maximal values around the critical size of wild-type yeast cells. The transcriptome of yeast and mouse cells undergoes a relative inversion in response to cell size, which we associate theoretically and experimentally with the necessary genome-wide diversity in RNA polymerase II affinity for promoters. Although highly expressed genes impose strong negative effects on fitness when the DNA/mass ratio is reduced, transcriptomic alterations mimicking the relative inversion by cell size strongly restrain cell growth. In all, our data indicate that cells set the critical size to obtain a properly balanced transcriptome and, as a result, maximize growth and fitness during proliferation.

2.
Food Chem ; 154: 246-54, 2014 Jul 01.
Artigo em Inglês | MEDLINE | ID: mdl-24518339

RESUMO

Betalains are natural pigments characteristic of plants of the order Caryophyllales. In this work, the role of betalains in the anti-inflammatory activity described for plant extracts is analysed in terms of the inactivation of the enzymes involved in the biochemical response (lipoxygenase and cyclooxygenase). Pure natural betalains and semi-synthetic analogues are demonstrated to promote a significant reduction of the enzymes activity. Reactions were followed spectrophotometrically and by HPLC-DAD. Phenethylamine-betaxanthin was the most potent in the inactivation of cyclooxygenase, with a reduction of 32% of the control activity at 125µM, while the natural pigment betanidin and a betalain analogue derived from indoline resulted as the most potent inactivators of lipoxygenase, with IC50 values of 41.4 and 40.1µM, respectively. Molecular docking studies revealed that betalains interact with the lipoxygenase amino acids involved in substrate binding and with Tyr-385 and Ser-530 close to the cyclooxygenase active site, interfering in enzyme catalysis.


Assuntos
Betalaínas/química , Inibidores de Ciclo-Oxigenase/química , Inibidores de Lipoxigenase/química , Lipoxigenase/química , Extratos Vegetais/química , Prostaglandina-Endoperóxido Sintases/química , Beta vulgaris/química , Betalaínas/síntese química , Inibidores de Ciclo-Oxigenase/síntese química , Ativação Enzimática , Humanos , Cinética , Inibidores de Lipoxigenase/síntese química , Simulação de Acoplamento Molecular , Estrutura Molecular , Extratos Vegetais/síntese química
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