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Tumour necrosis factor- (TNF-) plays a key role in the regulation of cardiac contractility. Although cardiomyocytes are known to express the TNF- receptors (TNFRs), the mechanism of TNF- signal transmission is incompletely understood. The aim of this study was to investigate whether the tumour suppressor Ras-association domain family protein 1 isoform A (RASSF1A) modulates TNF- signalling in cardiomyocytes.', "We used RASSF1A knockout (RASSF1A(-/-)) mice and wild-type (WT) littermates in this study. Acute stimulation with a low dose of TNF- (10 g/kg iv) increased cardiac contractility and intracellular calcium transients' amplitude in WT mice. In contrast, RASSF1A(-/-) mice showed a blunted contractile response. Mechanistically, RASSF1A was essential in the formation of the TNFR complex (TNFRC), where it functions as an adaptor molecule to facilitate the recruitment of TNFR type 1-associated death domain protein and TNFR-associated factor 2 to form the TNF- receptor complex. In the absence of RASSF1A, signal transmission from the TNF- receptor complex to the downstream effectors, such as cytoplasmic phospholipase A2 and protein kinase A, was attenuated leading to the reduction in the activation of calcium handling molecules, such as L-type Ca(2+) channel and ryanodine receptors.
Does the tumour suppressor Ras-association domain family protein 1A ( RASSF1A ) regulate TNF- signalling in cardiomyocytes?