In JoVE (1)
Articles by Trejeeve Martyn in JoVE
Calcification of Vascular Smooth Muscle Cells and Imaging of Aortic Calcification and Inflammation Caitlin O'Rourke*1, Georgia Shelton*1,2, Joshua D. Hutcheson3,4, Megan F. Burke2, Trejeeve Martyn1, Timothy E. Thayer2, Hannah R. Shakartzi1, Mary D. Buswell1, Robert E. Tainsh1, Binglan Yu1,4, Aranya Bagchi1,4, David K. Rhee2,4, Connie Wu1,2,4, Matthias Derwall5, Emmanuel S. Buys1,4, Paul B. Yu3,4, Kenneth D. Bloch1,2,4, Elena Aikawa3,4, Donald B. Bloch1,5,6, Rajeev Malhotra2,4 1Anesthesia Center for Critical Care Research of the Department of Anesthesia, Critical Care, and Pain Medicine, Massachusetts General Hospital, 2Cardiovascular Research Center and Cardiology Division of the Department of Medicine, Massachusetts General Hospital, 3 Vascular calcification is an important predictor of and contributor to human cardiovascular disease. This protocol describes methods for inducing calcification of cultured primary vascular smooth muscle cells and for quantifying calcification and macrophage burden in animal aortas using near-infrared fluorescence imaging.
Other articles by Trejeeve Martyn on PubMed
Adverse Effects of Hemorrhagic Shock Resuscitation with Stored Blood Are Ameliorated by Inhaled Nitric Oxide in Lambs* Critical Care Medicine. Nov, 2013 | Pubmed ID: 23887236 Transfusion of stored RBCs is associated with increased morbidity and mortality in trauma patients. Plasma hemoglobin scavenges nitric oxide, which can cause vasoconstriction, induce inflammation, and activate platelets. We hypothesized that transfusion of RBCs stored for prolonged periods would induce adverse effects (pulmonary vasoconstriction, tissue injury, inflammation, and platelet activation) in lambs subjected to severe hemorrhagic shock and that concurrent inhalation of nitric oxide would prevent these adverse effects.
Deletion of the Sequence Encoding the Tail Domain of the Bone Morphogenetic Protein Type 2 Receptor Reveals a Bone Morphogenetic Protein 7-specific Gain of Function PloS One. 2013 | Pubmed ID: 24116187 The bone morphogenetic protein (BMP) type II receptor (BMPR2) has a long cytoplasmic tail domain whose function is incompletely elucidated. Mutations in the tail domain of BMPR2 are found in familial cases of pulmonary arterial hypertension. To investigate the role of the tail domain of BMPR2 in BMP signaling, we generated a mouse carrying a Bmpr2 allele encoding a non-sense mediated decay-resistant mutant receptor lacking the tail domain of Bmpr2. We found that homozygous mutant mice died during gastrulation, whereas heterozygous mice grew normally without developing pulmonary arterial hypertension. Using pulmonary artery smooth muscle cells (PaSMC) from heterozygous mice, we determined that the mutant receptor was expressed and retained its ability to transduce BMP signaling. Heterozygous PaSMCs exhibited a BMP7‑specific gain of function, which was transduced via the mutant receptor. Using siRNA knockdown and cells from conditional knockout mice to selectively deplete BMP receptors, we observed that the tail domain of Bmpr2 inhibits Alk2‑mediated BMP7 signaling. These findings suggest that the tail domain of Bmpr2 is essential for normal embryogenesis and inhibits Alk2‑mediated BMP7 signaling in PaSMCs.
Inhibition of Bone Morphogenetic Protein Signal Transduction Prevents the Medial Vascular Calcification Associated with Matrix Gla Protein Deficiency PloS One. 2015 | Pubmed ID: 25603410 Matrix Gla protein (MGP) is reported to inhibit bone morphogenetic protein (BMP) signal transduction. MGP deficiency is associated with medial calcification of the arterial wall, in a process that involves both osteogenic transdifferentiation of vascular smooth muscle cells (VSMCs) and mesenchymal transition of endothelial cells (EndMT). In this study, we investigated the contribution of BMP signal transduction to the medial calcification that develops in MGP-deficient mice.