Editorial Acesso aberto Revisado por pares

Nitric oxide signaling comes of age: 20 years and thriving

2007; Oxford University Press; Volume: 75; Issue: 2 Linguagem: Inglês

10.1016/j.cardiores.2007.05.023

ISSN

1755-3245

Autores

Santiago Lamas, Charles J. Lowenstein, Thomas A. Michel,

Tópico(s)

Renin-Angiotensin System Studies

Resumo

The lyrics of a famous tango state that “twenty years time is just nothing”. While this impression may broadly apply to different circumstances, such might not be the case for nitric oxide (NO). In the year 1987 two seminal contributions coming from independent laboratories [1,2] established the identity of the elusive endothelial derived relaxing factor reported by Bob Furchgott seven years earlier [3]. These laboratories showed that the chemical nature of “endothelium-derived relaxing factor” (EDRF) was identical to NO. The idea that NO could act as an activator of soluble guanylate cyclase had been proposed even earlier [4]. These four papers, together with the demonstration of l-arginine as substrate for the generation of NO [5], defined a pathway in endothelial cells which is now considered classical: the l-arginine-NO-cGMP pathway. Of importance, a considerable amount of information had already accumulated almost at the same time and had arrived at the same conclusions in non-vascular cells such as macrophages (see [6] for review). For the past twenty years, we have both witnessed and participated in an explosion of knowledge in the NO field, leading to the comprehension of the physiological and pathophysiological roles of NO in several organs and tissues, among which the cardiovascular system is “primus inter pares”. This Spotlight Issue is devoted to classical and non-classical targets of NO signaling in the cardiovascular system. One of the most cogent analyses of NO signaling in pathways independent from cGMP was published in 1992, in which Loscalzo and colleagues proposed that S -nitrosylation of albumin could represent an effective mechanism to deliver NO at distal sites [7]. Studies from the laboratories of Stamler, Loscalzo and others opened a new perspective related to the potential modification of protein function by S -nitros(yl)ation [8]. In this current … * Corresponding author. Centro de Investigaciones Biologicas-CSIC, Ramiro de Maeztu 9, Madrid, 28040, Spain. Tel.: +34 91 837 3112x4302, +34 64 941 8799 (mobile); fax: +34 91 536 0432. slamas{at}cib.csic.es

Referência(s)