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Biomedical subjects

R Betz

Publications and source records attributed to R Betz.

At least 37 records · Page 2Linked to original sources
PubMed1997

Let the market work.

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Centers for Medicare and Medicaid Services, U.S.↗
PubMed1996

Semirigid instrumentation in the management of lumbar spinal conditions combined with circumferential fusion. A multicenter study.

STUDY DESIGN: Patients with the diagnosis of degenerative disc conditions or spondylolisthesis undergoing circumferential fusion with posterior pedicle screw fixation using a semirigid rod were reviewed. OBJECTIVES: To determine the effectiveness of this approach in achieving a spinal fusion and satisfactory clinical outcome, and to determine the complications associated with the procedure. SUMMARY OF BACKGROUND DATA: The use of instrumentation to stabilize the lumbar motion segments and thereby enhance the fusion rate has been proposed in a number of studies. Semirigid fixation was believed to be effective in achieving these objectives without concern for stress-shielding, which was suggested by some authors using rigid fixation systems. METHODS: Patients who required spinal fusion with anterior and posterior approaches because of specific lumbar pathology or previous surgeries were selected. The surgery consisted of an anterior interbody fusion using allograft, followed by a posterolateral fusion and pedicle screw fixation. Fusion was determined by continuity of trabecular bridging, and outcomes were determined by pain reduction and return to previous levels of activity. Fusion was considered solid if the two posterolateral areas were fused (Zones one and two), if the anterior interbody area was fused (Zone three), or if all three zones were fused. Complications were documented during and after surgery. RESULTS: Sixty-two percent of patients had previous surgery with 25% of these patients having a diagnosis of pseudarthrosis. Fifty-five percent of patients had two or more levels fused, and 43% were heavy smokers. Ninety-seven percent of patients had successful fusions. Pain was significantly reduced on a pain analogue scale from 7.1 to 2.1 in the back and from 5.8 to 1.5 in the leg (p < 0.006 and 0.0001, respectively). Fifty-nine percent of patients returned to their previous level of activity, and 18% returned to lighter work or job retraining, for a total of 77% returning to the same or lighter levels of activity. Complications included metal failure, 4.9%; neurologic deficit, 1.2%; deep infection, 1.2%; deep venous thrombosis, 4.9%; and vascular injury, 2.4%. Fatal pulmonary embolus occurred in one patient. CONCLUSION: This technique produces a satisfactory fusion rate (97%) and a good clinical outcome based on pain reduction and return to a satisfactory level of activity (77%). It is associated with few, but significant, complications that compare well with other reported series in a difficult group of patients. This procedure should be reserved for patients who are considered to be at high risk for not achieving spinal fusion.

Adolescent↗
PubMed1996

Effects of functional electrical stimulation on the joints of adolescents with spinal cord injury.

Nineteen adolescent subjects with complete spinal cord injuries resulting in paraplegia or tetraplegia participated in a functional electrical stimulation (FES) program consisting of computerized, controlled exercise and/or weight bearing. The effects of stimulated exercise and standing/walking on the lower extremity joints were prospectively studied. Plain radiographs and MRIs were obtained prior to and following completion of the exercise and standing and walking stages. In addition, the joints of five subjects were studied with synovial biopsies, arthroscopy, and the analysis of serum and synovial fluid for a 550 000 dalton cartilage matrix glycoprotein (CMGP). Pre-exercise joint abnormalities secondary to the spinal cord injury improved following the stimulation program. None of the subjects developed Charcot joint changes. Upon standing with FES, one subject with poor hip coverage prior to participation developed hip subluxation which required surgical repair. No other detrimental clinical effects occurred in the lower extremity joints of subjects participating in an FES program over a 1-year period.

Adolescent↗
PubMed1996

Managed care backlash.

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Health Maintenance Organizations↗
PubMed1996

Health informatics.

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Computer Communication Networks↗
PubMed1995

A periplasmic insulin-cleaving proteinase (ICP) from Acinetobacter calcoaceticus sharing properties with protease III from Escherichia coli and IDE from eucaryotes.

A periplasmic insulin-cleaving proteinase (ICP), purified to its electrophoretic homogeneity in the SDS-PAGE from the Gram-negative bacterium Acinetobacter calcoaceticus, was examined and compared in its properties with the protease III (protease Pi, pitrilysin, EC 3.4.99.44) of Escherichia coli and the insulin-destroying proteinase (IDE, insulinase, EC 3.4.99.45) from eucaryotes. The enzyme was proven to be a metalloprotease like protease III and IDE, as was shown by the inhibitory effects exerted by EDTA and o-phenanthroline. Furthermore, dialysis against EDTA and o-phenanthroline led to a complete loss of activity, which could be restored by addition of Co2+, and, to a lesser extent, but at a lower metal ion concentration by Zn2+. Similar to protease III and IDE, ICP prefers the cleavage of small polypeptides (insulin, insulin B-chain, glucagon) to the cleavage of proteins (casein, human serum albumin, globin) and was inactive against synthetic amino acid derivates (esters, p-nitranilides, and furoylacroleyl substrates) of subtilisin, thermolysin, trypsin, and chymotrypsin. The peptide-bond-specificity of the ICP in the cleavage of the oxidized insulin B-chain was investigated and the results were compared to the specificity of protease III of E. coli, IDE, protease-24,11, and thermolysin. Cleavage sites in the oxidized insulin B-chain generated by ICP are Asn3-Gln4, His10-Leu11, Ala14-Leu15, Leu17-Val18, Gly23-Phe24, Phe24-Phe25, and Phe25-Tyr26. Principally, ICP cleaves between hydrophobic amino acids and amides. The ICP shares one of the only two cleavage sites with the protease III and four sites with the IDE.

Acinetobacter calcoaceticus↗