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, 2007a). TSP1 is typically not detectable via Western immunoblots or immunofluorescent histology in normal human vessels (Canfield et al., 2002). However, there is now increasing data demonstrating the pathogenic role of both TSP1 and CD47 in human CVD. Immunohistochemical studies have demonstrated increased TSP1 within the intima of systemic arteries from patients with atherosclerosis, and in renal vessels affected by chronic vascular rejection (Canfield et al., 2002). TSP1 also localized to primary coronary atherosclerotic plaques (Riessen et al., 1998). Not surprisingly, as a secreted protein, only a minor proportion of TSP1 Tryptophan synthase was located intracellularly in diseased arteries (Riessen et al., 1998). TSP1 mRNA has been detected in myocardial biopsies, is increased in biopsies from cardiac allografts, and Alectinib correlated with allograft vasculopathy and rejection (Zhao et al., 2001). Microarray analysis of peripheral blood samples in patients following myocardial infarction identified TSP1 as a potential biomarker of ensuing left ventricular failure (LVF) (defined as left ventricle ejection fraction PI3K signaling pathway factor for coronary artery disease) in newborns from affected parents (Andraweera et al., 2011). Additionally, umbilical cord blood endothelial cells from low birth weight infants (also known to be at risk for cardiovascular disease) were found to overexpress TSP1 and this was associated with decreased angiogenic activity in these cells (Ligi et al., 2011). Together, these results suggest a transgenerational role for TSP1 in controlling vascular responses. New evidence has also linked TSP1 to human PAH. Two distinct TSP1 SNPs have been identified in familial PAH, which are hypothesized to alter transcription factor binding and/or modify pulmonary vascular smooth muscle and endothelial cell growth (Maloney et al., 2012).