RESUMEN
Awake surgery has been applied for various surgical procedures with positive outcomes; however, in neurosurgery, the technique has traditionally been reserved for cranial surgery. Awake surgery for the spine (ASFS) is an alternative to general anesthesia (GA). As early studies report promising results, ASFS is progressively gaining more interest from spine surgeons. The history defining the range of adverse events facing patients undergoing GA has been well described. Adverse reactions resulting from GA can include postoperative nausea and vomiting, hemodynamic instability and cardiac complications, acute kidney injury or renal insufficiency, atelectasis, pulmonary emboli, postoperative cognitive dysfunction, or malignant hyperthermia and other direct drug reactions. For this reason, many high-risk populations who have typically been poor candidates under classifications for GA could benefit from the many advantages of ASFS. This narrative review will discuss the significant historical components related to ASFS, pertinent mechanisms of action, protocol overview, and the current trajectory of spine surgery with ASFS.
RESUMEN
At the molecular level, the circadian clock is regulated by a time delayed transcriptional-translational feedback loop in which the core proteins interact with each other rhythmically to drive daily biological rhythms. The C-terminal domain of a key clock protein PER2 (PER2c) plays a critically important role in the loop, not only for its interaction with the binding partner CRY proteins but also for the CRY/PER complex's translocation from the cytosol to the nucleus. Previous circular dichroism (CD) spectroscopic studies have shown that mouse PER2c (mPER2c) is less structured in solution by itself but folded into stable secondary structures upon interaction with mouse CRYs. To understand the stability and folding of human PER2c (hPER2c), we expressed and purified hPER2c. Three oligomerization forms of recombinant hPER2c were identified and thoroughly characterized through a combination of biochemical and biophysical techniques. Different to mPER2c, both thermal unfolding DLS and CD analyses suggested that all forms of hPER2c have very stable secondary structures in solution by themselves with melting temperatures higher than the physiological body temperature, indicating that hPER2c does not require CRY to fold. Furthermore, we examined the effects of EDTA, salt concentration, and a reducing agent on hPER2c folding and oligomerization. The ability of hPER2c forming oligomers reflects the potential role of hPER2c in the assembly of circadian rhythm core protein complexes.