Response to requests for genetic testing is not based on age alone.
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Adolescent↗
Biomedical subjects
R Glew
Publications and source records attributed to R Glew.
Serum cytosolic beta-glucosidase elevation and early ischemic injury to guinea pig small intestine.
BACKGROUND: The lack of an early, sensitive marker for intestinal ischemia has led to delay in diagnosis and worsended outcome for patients with acute onset of this condition. Our preliminary studies revealed that guinea pig cytosolic beta-glucosidase (CBG) is expressed predominantly in the small intestine, with lower levels in the liver and pancreas and undetectable levels in other organs. Cytosolic beta-glucosidase was investigated as a serum marker of small intestinal ischemia in a guinea pig model. METHODS: Guinea pigs underwent anesthesia, sham laparotomy, 30 minutes of mesenteric ischemia followed by 6 hours of reperfusion 6 hours of sustained mesenteric ischemia, or closed-loop small bowel obstruction. Serum samples were assayed for CBG activity. At the conclusion of the ischemia/reperfusion experiments, small bowel samples were assayed for residual enzyme activity, and paraffin sections were graded for the severity of histologic injury. RESULTS: Serum CBG activity rose rapidly after intestinal ischemia with and without reperfusion. Peak enzyme activities were elevated 23-fold for reperfused animals (P < .001) by 4 hours. For nonreperfused animals, peak serum CBG activities reached 29-fold above baseline and were significantly higher than the CBG activities of reperfused animals at 4 hours (P < .01) and at 6 hours (P < .05). Mucosal injury ranged from undetectable to moderate and corresponded in severity with both peak serum enzyme activity and decreased residual activity in the small bowel. In animals subjected to closed-loop obstruction, there was a mean increase of serum CBG of 9.2-fold from 4 to 6 hours after establishment of obstruction (P < .05). CONCLUSIONS: In the guinea pig model, CBG is a sensitive marker of ischemic injury caused by arterial occlusion or closed-loop obstruction of the small bowel.
Animals↗
Appraisal of percutaneous tracheostomy.
Two commercially available kits have been used to create 25 percutaneous tracheostomies, 20 using the Cook system and five using the Rapitrac system. The operation time and complication rates of these tracheostomies have been compared with those for 16 conventional tracheostomies performed for similar indications. Median operating times were 60 (range 30-105) min for conventional tracheostomy, 15 (range 8-70) min for Cook and 5 (range 3-15) min for Rapitrac systems (P less than 0.001). A significantly higher proportion of patients in the Rapitrac group had complications compared with the other two groups (P less than 0.05). The complication rate for the Cook group compared favourably with that for the conventional tracheostomy group. The Cook system of percutaneous tracheostomy is a simple, rapid and safe alternative to conventional tracheostomy.
Adult↗
Subacute Pasteurella osteomyelitis of the hand following dog bite.
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Adult↗
Effect of glutaraldehyde treatment on enzyme-loaded erythrocytes.
In principle, enzyme-loaded erythrocytes can be used as a vehicle for enzyme replacement therapy in lysosomal storage diseases. Glutaraldehyde treatment renders these erythrocytes more resistant to lysis without inactivating the enzymes that have been entrapped inside them. Glutaraldehyde treatment does not prevent ingestion of enzyme-loaded erythrocytes by macrophages in vitro so that these cells can be used to deliver enzymes to lysosomes. In vivo, the glutaraldehyde-treated cells are quickly removed from the circulation by the spleen or liver. The degree of glutaraldehyde treatment allows the erythrocytes to be targeted either to the spleen (low glutaraldehyde concentrations) or to the liver (higher glutaraldehyde concentrations).
Aldehydes↗
Enzyme loading of nucleated chicken erythrocytes.
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Animals↗
Protein-tyrosine phosphatase activity of Coxiella burnetii that inhibits human neutrophils.
Supernatants prepared from disrupted Coxiella burnetii possess acid phosphatase (ACP) activity that apparently accounts for the inhibition of the metabolic burst of formyl-Met-Leu-Phe(fMLP)-stimulated human neutrophils. Results are presented regarding purification and biochemical-biological characterization of the ACP. The highly purified enzyme, which exhibited an apparent M(r) of 91 K and optimal activity at pH 5.0, also inhibited neutrophils. The enzyme retained full activity at pH 4.5, 5.5, and 7.4, when incubated overnight at 0 degrees C and room temperature; at pH 5.5, it retained full activity after overnight incubation at 37 degrees C. Apparently, the enzyme contains asparagine-linked but not serine- or threonine-linked glycan residues since its treatment with N-glycosidase F (PNGase F) decreased its M(r) to 87 K and no changes were detected with O-glycosidase. The enzyme's capacity to hydrolyze phosphate from a number of phosphate-containing compounds was examined; five phosphocompounds were significantly hydrolyzed: 5'-CMP > fructose 1,6-diphosphate > tyrosine phosphate > 3'-AMP > 5'-AMP. The ACP also dephosphorylated (32)P-Raytide, a phosphotyrosine-containing peptide. Dephosphorylation of Raytide was inhibited by the following phosphatase inhibitors: sodium molybdate, potassium fluoride, sodium ortho-vanadate and D2, a heteropolymolybdate compound. These results indicate that C. burnetii ACP may play a role in disrupting tyrosine phosphorylation/dephosphorylation reactions associated with the signal transduction pathway culminating in the metabolic burst. Interestingly, Western blot analysis of ACP-inhibited neutrophils showed a marked increase in tyrosine phosphorylation of a 44 K protein as compared to uninhibited cells.
Acid Phosphatase↗