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Biomedical subjects

Albert J Yee

Publications and source records attributed to Albert J Yee.

4 recordsLinked to original sources

Generalized peripheral nerve failure during thoracic spine surgery: a case report.

OBJECTIVE: Intra-operative systemic changes impairing peripheral nerve function are not commonly detected with electrophysiology. This case presentation illustrates how somatosensory evoked potential (SSEP) monitoring can detect global changes in peripheral nerve excitability during spine surgery. METHODS: A posterior thoracic spine fixation was performed on a young male with multiple traumatic injuries. Bilateral tibial nerve SSEPs were intraoperatively recorded, along with the right median nerve SSEP for control. RESULTS: A rapid, progressive loss of tibial and median nerve potentials (followed by cortical SSEP loss) occurred 90 min after anaesthetic induction. Oxygenation and fluid volume were adequate throughout the case, despite mean airway resistance being elevated (33 cmH(2)0) and blood pressure being low (80/45 mmHg). Corresponding to the decrease in peripheral nerve responses was a drop in end-tidal CO(2) partial pressure (PaCO(2)) from 37 to 25 mmHg. Approximately, 100 min later, the peripheral and cortically generated SSEPs recovered in 2 of 3 limbs monitored. On emergence from anesthesia it was clear that the patient had bitten and kinked the endotracheal tube thus increasing the airway resistance. Ventilation difficulties were magnified with the patient's prone position. Post-operatively there were no sensorimotor deficits. CONCLUSIONS: Somatosensory evoked potential monitoring during spine surgery can detect uncommon generalized nerve conduction block, and further alert surgical teams to a systemic impairment. This was discovered to result from a compromised endotracheal tube. This can apply in various monitoring situations, as the changes affecting the SSEPs were not related to surgical manipulation.

Adult↗

The interaction of versican with its binding partners.

Versican belongs to the family of the large aggregating chondroitin sulfate proteoglycans located primarily within the extracellular matrix (ECM). Versican, like other members of its family, has unique N- and C-terminal globular regions, each with multiple motifs. A large glycosaminoglycan-binding region lies between them. This review will begin by outlining these structures, in the context of ECM proteoglycans. The diverse binding partners afforded to versican by virtue of its modular design will then be examined. These include ECM components, such as hyaluronan, type I collagen, tenascin-R, fibulin-1, and -2, fibrillin-1, fibronectin, P- and L-selectins, and chemokines. Versican also binds to the cell surface proteins CD44, integrin beta 1, epidermal growth factor receptor, and P-selectin glycoprotein ligand-1. These multiple interactors play important roles in cell behaviour, and the roles of versican in modulating such processes are discussed.

Animals↗

Patterns of collapse in thoracolumbar burst fractures.

OBJECTIVE: Functional outcomes of neurologically intact patients with burst fractures may be dependent on final kyphosis at the end of treatment. Conservative treatment is indicated if an acceptable sagittal alignment of the spine can be anticipated. Thoracolumbar burst fractures are often grouped as a single entity where, in fact, anatomically distinct areas of the spine may behave differently owing to different biomechanical factors. The goal of this work was to evaluate differential behavior in terms of final kyphosis in anatomically distinct regions of the spine following stable burst fractures. METHODS: Prospective analysis of kyphosis in 60 patients treated conservatively for traumatic thoracolumbar burst fracture was conducted. Initial trauma supine radiographs were measured for initial kyphosis (Ki). Final kyphosis (Kf) in the upright patient was measured at the end of treatment. The Ki and Kf were plotted on a scatter graph; with use of linear regression analysis, a mathematical model was created to define a relationship between Ki and Kf based on anatomic level of the spine. RESULTS: The thoracolumbar spine behaved in two independent patterns with respect to Kf. Kf at the thoracolumbar junction (T11-L1) had a collapse pattern that could be approximated most accurately with the equation Kf = Ki + 0.5 Ki. At the midlumbar spine, L2-L3 level, a best-fit model for collapse was Kf = Ki + 4 degrees . CONCLUSION: In this cohort of patients, fractures that were categorized as "stable" and not requiring surgery were studied for the purpose of determining differential collapse patterns in anatomically distinct areas of the lumbar spine. We have demonstrated that the thoracolumbar junction and the midlumbar spine behave differently biomechanically and recommend that these two anatomic levels be studied independently for research purposes.

Adult↗

Structure and function of aggrecan.

Aggrecan is the major proteoglycan in the articular cartilage. This molecule is important in the proper functioning of articular cartilage because it provides a hydrated gel structure (via its interaction with hyaluronan and link protein) that endows the cartilage with load-bearing properties. It is also crucial in chondroskeletal morphogenesis during development. Aggrecan is a multimodular molecule expressed by chondrocytes. Its core protein is composed of three globular domains (G1, G2, and G3) and a large extended region (CS) between G2 and G3 for glycosaminoglycan chain attachment. G1 comprises the amino terminus of the core protein. This domain has the same structural motif as link protein. Functionally, the G1 domain interacts with hyaluronan acid and link protein, forming stable ternary complexes in the extracellular matrix. G2 is homologous to the tandem repeats of G1 and of link protein and is involved in product processing. G3 makes up the carboxyl terminus of the core protein. It enhances glycosaminoglycan modification and product secretion. Aggrecan plays an important role in mediating chondrocyte-chondrocyte and chondrocyte-matrix interactions through its ability to bind hyaluronan.

Aggrecans↗