Protein post-translational modifications after spinal cord injury.

Deficits in intrinsic neuronal capacities in the spinal cord, a lack of growth support, and suppression of axonal outgrowth by inhibitory molecules mean that spinal cord injury almost always has devastating consequences. As such, one of the primary targets for the treatment of spinal cord injury is to develop strategies to antagonize extrinsic or intrinsic axonal growth-inhibitory factors or enhance the factors that support axonal growth. Among these factors, a series of individual protein level disorders have been identified during the generation of axons following spinal cord injury. Moreover, an increasing number of studies have indicated that post-translational modifications of these proteins have important implications for axonal growth. Some researchers have discovered a variety of post-translational modifications after spinal cord injury, such as tyrosination, acetylation, and phosphorylation. In this review, we reviewed the post-translational modifications for axonal growth, functional recovery, and neuropathic pain after spinal cord injury, a better understanding of which may elucidate the dynamic change of spinal cord injury-related molecules and facilitate the development of a new therapeutic strategy for spinal cord injury.

Recurrence of non-cardiogenic pulmonary edema and sustained hypotension shock in cystic pheochromocytoma.

Pheochromocytoma is a rare neuroendocrine tumor which derives from chromaffin cells of the adrenal gland or relevant to sympathetic nerves and ganglia. The clinical features of pheochromocytoma are various. Paroxysmal episodes of serious hypertension, headache, palpitation, and diaphoresis are the typical manifestations (Bravo, 2004). Hypotension shock, pulmonary edema, and acute coronary syndrome induced by pheochromocytoma are uncommon (Malindretos et al., 2008; Batisse-Lignier et al., 2015). In this study, we present a rare case of cystic pheochromocytoma causing recurrent hypotension shock, non-cardiogenic pulmonary edema, and acute coronary syndrome, and the possible mechanisms are discussed.

Right ventricular apical obstruction in a patient with hypereosinophilia: Löffler endocarditis.

Idiopathic hypereosinophilic syndrome (HES) is a rare leukoproliferative systemic disorder characterized by sustained overproduction of eosinophils and poor prognosis. A case that a 67-year-old man with persistent symptoms of heart failure due to cardiac involvement in idiopathic HES is concentrated on. Echocardiography revealed the marked endocardial thickening of both ventricles with an apical obstruction of the right ventricle. Medical therapy, including low dose dopamine and furosemidum, was initiated with corticosteroids, imatinib and hydroxycarbamide. Remission of symptoms had persisted for only 3 weeks. As the count of eosinophils rebounded, the patient suffered with refractory heart failure, severe hypoxemia and acute renal insufficiency, eventually died 62 days after his hospitalization. The rechecking of his last MRI showed thrombus both in right atrium and superior vena cava, which indicated that he might have died of pulmonary embolism, besides the refractory heart failure and multiple organ failure.

Domain motions of class I release factor induced by binding with class II release factor from Euplotes octocarinatus.

The binding of both factors (eRF1 and eRF3) is essential for fast kinetics of the termination of protein translation. The C-terminal domain of eRF1 is known to interact with the C domain of eRF3. Eo-eRF1b contains two highly conserved tryptophan residues (W-11 and W-373), W-11 located in the Eo-eRF1b N domain and W-373 located in the Eo-eRF1b C domain. Fluorimetry was used to study the interactions of the proteins. When binding with Eo-eRF3Cm6, the emission peak of Eo-eRF1b is blue shifted, while the emission peak of Eo-eRF1bC has no notable change. Our results suggest that the eRF1-eRF3 interaction induces the N and C domain of eRF1b to become closer to each other.

The binding sites of class I release factor (eRF1) toward class II release factor (eRF3) in Euplotes octocarinatus.

The C domain of eRF1 interacts with the C domain of eRF3, and the binding of both factors is essential for fast kinetics of the termination of protein translation. Analysis by computational simulation demonstrated that several peptides involved in Eo-eRF1/Eo-eRF3 interaction directly. Among these peptides, the two motifs GVEDT and GFGG were highly conserved, while the fragment aa338-346 of Eo-eRF1a/b was variable. In additional, I290 and D293 of Eo-eRF1 were also highly conserved. By the site-directed mutagenesis and pull-down analysis, the amino acid D293 in Eo-eRF1bC domain was conformed playing an important role in eRF1-eRF3 interaction. Eo-eRF1a and Eo-eRF1b may select different manners to interact with Eo-eRF3. These studies contribute to the better understanding the mode of eRF1-eRF3 interaction.