Acute spinal ligament disruption: MR imaging with anatomic correlation.

Disruption of spinal ligaments can lead to instability that jeopardizes the spinal cord and nerve roots. Magnetic resonance (MR) imaging can directly image spinal ligaments; however, the sensitivity with which this modality demonstrates ligament injury has, to the authors' knowledge, not been reported. On a biomechanical testing machine, 28 cadaveric spines were subjected to controlled injury that resulted in ligament tears.

The role of torsion in cervical spine trauma.

A dynamic servocontrolled torsion machine has been used to characterize cervical injury due to pure rotation of the head. Resultant force moment, torque, and applied rotation have been measured. Torque applied to the base of the skull resulted in injury to the atlantoaxial joint.

Preparation and characterization of dog pancreas microsomal membranes specifically depleted of protein disulphide-isomerase.

1. The selective release of protein disulphide-isomerase from dog pancreas and rat liver microsomal membranes was studied to throw light on the mechanisms of retention of this enzyme within the endoplasmic reticulum, and in order to prepare microsomal membranes specifically depleted of the enzyme. 2.

Induction of expression of protein disulphide-isomerase during lymphocyte maturation stimulated by bacterial lipopolysaccharide.

Protein disulphide-isomerase (PDI) activity, and the level of immunodetectable PDI protein, were monitored in splenic lymphocytes and in BCL1 cells during culture in the presence of various activating factors. Bacterial lipopolysaccharide stimulated induction of PDI in splenic B cells and BCL1 cells. The time-course and specificity of induction indicated that the increase in expression of PDI is closely coupled to the final stages of B cell differentiation into antibody-producing plasma cells.

Role of protein disulphide-isomerase in the expression of native proteins.

Formation of native disulphide bonds is a post-translational modification associated with the folding and assembly of secretory proteins. The process is catalysed within the lumen of the endoplasmic reticulum by the enzyme protein disulphide-isomerase (PDI), which is abundant in secretory cells and catalyses thiol: protein-disulphide interchange in vitro with very broad protein substrate specificity. The presence of PDI within microsomal vesicles is essential for efficient and rapid cotranslational disulphide bond formation during protein synthesis in vitro.