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Biomedical subjects

M E Peacock

Publications and source records attributed to M E Peacock.

5 recordsLinked to original sources

Angioedema as a complication in periodontal surgery: report of a case.

Angioedema is a diffuse swelling of the subcutaneous or submucosal tissues that occurs in both hereditary and non-hereditary forms. It can be a temporarily disfiguring condition, but not usually a serious one unless the airway is compromised. In the majority of cases, no underlying cause can be identified. In this report, a case of "idiopathic" angioedema that occurred while performing a periodontal surgical procedure is presented. This case is interesting because the patient was on long-term use of an angiotensin-converting enzyme [ACE] inhibitor for hypertension, and recent evidence has shown that ACE inhibitors suppress the breakdown of circulating bradykinins. With high plasma levels of bradykinins, a local anesthetic, periodontal surgical procedures, or even emotional stress may trigger an attack of angioedema. Practitioners should be aware of the pharmacologic side effects of ACE inhibitors and be prepared to handle an emergency if a patient's airway becomes compromised.

Angioedema

Phosphorylation of vitronectin by a protein kinase in human plasma. Identification of a unique phosphorylation site in the heparin-binding domain.

Incubation of human plasma with 27 nM [gamma-32P]ATP in the presence of 20 mM MnCl2 results in the phosphorylation of several proteins detected by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and autoradiography. About 60% of the incorporated radioactivity is found in a 75-kDa protein containing [32P] phosphoserine. The amino-terminal amino acid sequence of the purified 75-kDa [32P]phosphoprotein is identical to that of vitronectin (also termed serum spreading factor or complement S protein). Rabbit antiserum against vitronectin precipitates greater than 90% of the 75-kDa [32P]phosphoprotein from plasma. Reverse phase chromatography of [32P]vitronectin degraded sequentially with CNBr and chymotrypsin yields one major labeled peptide. The sequence of the peptide, Ser-Arg-Arg-Pro-[32PO4]Ser-Arg-Ala-Thr, corresponds to residues 374-381 which are located in the heparin-binding fragment of vitronectin identified by Suzuki et al. [1984) J. Biol. Chem. 259, 15307-15314). Vitronectin could potentially be phosphorylated in vivo with ATP released from injured cells or secreted by platelets activated during hemostasis.

Binding Sites

Molecular size of dermatan sulfate oligosaccharides required to bind and activate heparin cofactor II.

Heparin cofactor II (HCII) inhibits thrombin rapidly in human plasma in the presence of heparin or dermatan sulfate. To determine the minimum structure of dermatan sulfate required to activate HCII, the glycosaminoglycan was partially degraded by sequential treatment with periodate, [3H]borohydride, and sulfuric acid. Labeled oligosaccharide fragments were separated by gel filtration chromatography. Purified fragments were then applied to a column of HCII bound to concanavalin A-Sepharose, and bound oligosaccharides were eluted with a gradient of sodium chloride. Di-, tetra-, and hexasaccharide fragments did not bind to HCII, while 15% of the octasaccharides and up to 45% of larger fragments bound. Octasaccharides that bound to the HCII column had a greater negative charge than the run-through material based on anion-exchange chromatography, suggesting that they contained a greater number of sulfate groups per molecule. Fragments of dermatan sulfate containing a minimum of 12-14 sugar residues accelerated inhibition of thrombin by HCII. Fragments of this length that bound to the column of immobilized HCII had molar specific activities greater than those of the fragments that did not bind. These studies suggest that HCII is activated by dermatan sulfate fragments greater than or equal to 12 residues in length that contain a specific octasaccharide sequence required for binding to the inhibitor.

Animals

Threshold sensitivity and frequency specificity in auditory brainstem response audiometry.

Frequency-specific electric response audiometry can be performed on difficult to test young children if the child is sedated and proper choices are made of acoustic stimuli and recording parameters, although certain compromises are necessary. A very satisfactory sedative is secobarbital, administered intramuscularly in doses related to the weight of the child. As stimuli we recommend '2-1-2' tone bursts at 500, 1 000, 2 000, and 4 000 Hz: i.e., with a rise and fall of two periods and a plateau of one period of the modulated tone. A very robust and sensitive response that is not significantly modified by the sedation and is effective for all four frequencies is the P6-SN10 of the early brainstem sequence. To record this complex favorably requires a bandpass input filter of the Butterworth type with pass-band (at -3 dB) from 50 to 1 700 Hz and rejection rates of 24 dB/octave. With this combination, polarity of stimulus is unimportant and sweep time, rate of stimulation and number of responses averaged may be selected for convenience and simplicity. A routine that requires about an hour of testing time is described and the necessary correction factors are given for estimating a child's behavioral pure-tone thresholds. We believe that our threshold estimates are generally correct within 10 dB, and are sufficiently frequency-specific for proper selection of a hearing aid.

Acoustic Stimulation