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JCI online early table of contents: Sept. 13, 2010
Date:9/13/2010

(fH), a negative regulator of the complement pathway. Consistent with this, studies in animal models have linked DDD to activation of complement. In this paper, Santiago Rodriguez de Crdoba and colleagues, at the Centro de Investigaciones Biolgicas, Madrid, identified a familial case of DDD linked to a gain of function mutation in the C3 gene that rendered the protein resistant to cleavage and inactivation by fH. The authors believe that this finding will be important in the treatment of human patients, as it suggests that fH replacement will be ineffective in those patients with DDD that carry C3 mutations. Furthermore, this work reveals the structural properties of C3 that are relevant to its inactivation, and thus may be critical in the development of therapeutics.

TITLE:

Human C3 mutation reveals a mechanism of dense deposit disease pathogenesis and provides insights into complement activation and regulation

AUTHOR CONTACT:
Santiago Rodrguez de Crdoba,
Centro de Investigaciones Biolgicas, Madrid, Spain.
Phone: 34.918373112; Fax: 34.915360432; E-mail: SRdeCordoba@cib.csic.es.

View this article at: http://www.jci.org/articles/view/43343?key=10a2d12b59b663b040c1


CARDIOLOGY Taking fatty acid oxidation to heart

The heart generates most of its energy by burning fats (or lipids) through a process called fatty acid oxidation (FAO). Despite this reliance on fat for energy, increased lipid accumulation in the heart can lead to reduced heart function in patients with obesity and type 2 diabetes. The proteins PPAR-alpha and PPAR-gamma are thought to play a role in promoting lipid accumulation and FAO in fat tissue, and increased expression and activation of PPAR-alpha and -gamma in the heart leads to cardiomyopathy, i.e., weakening of the heart muscle.


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