Nitric Oxide, Cytochromes P450, and Sexual Steroid Hormones

Jack R. Jr. Lancaster (Curatore)

J.F. Parkinson (Curatore)

Springer-Verlag Berlin and Heidelberg GmbH & Co. KG, 2012

The discovery of mammalian nitric oxide (NO-) synthesis from I-ar- ginine has led to profound increases in our understanding of basic physiological and pathophysiological processes. This understanding has been achieved by major advances in several areas. Three major ni- tric oxide synthase (NOS) isoforms have been identified at the protein and gene level and their specific tissue localization has been linked to processes subject to regulation by NO-. The molecular basis for the di- verse effects of NO- on cell function has been shown to derive from its chemical reactivity with oxygen-containing species and both heme and non-heme iron-dependent enzymes. The potential regulation of heme- dependent enzymes such as cytochromes P450, guanylate cyclase, cy- clooxygenase, and mitochondrial cytochrome oxidase continues to emerge as a key area in NO- research. In addition, it has become clear that the expression of NOS isoforms and NO- release from cells is subject to regulation by sexual steroids and that, in tum, NO- has the potential to regulate steroid biosynthesis via inhibition of cytochromes P450 involved in steroidogenesis. These recent observations on interactions between the NO-/NOS and cytochrome P450/sexual steroid pathways have important implica- tions for understanding fundamental mechanisms involved in endocri- nological processes. They are also likely to lead to novel insights and novel therapeutic approaches for the management of pathophysiologi- cal conditions associated with alterations in sexual steroid hormones.

• Curatore: Jack R. Jr. Lancaster, J.F. Parkinson
• Editore: Springer-Verlag Berlin and Heidelberg GmbH & Co. KG
• Collana: Ernst Schering Foundation Symposium Proceedings
• Anno: 2012
• Rilegatura: Paperback / softback
• Pagine: 310 p.
• EAN: 9783662035054

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