What is the cost of onychomycosis?
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Antifungal Agents↗
Biomedical subjects
R Sinclair
Publications and source records attributed to R Sinclair.
There is something wrong with my nail.
Nail problems are a frequent source of concern to patients and are a relatively common presenting complaint to general practitioners. While tinea unguium and psoriasis are the main causes of nail problems for the majority of patients, there are numerous other causes of nail dystrophies. This article aims to discuss some of the commoner causes of nail dystrophy. In addition it will give GPs an understanding of the anatomy and function of the nail and provide an approach to diagnosis based on morphology. Treatment will be dealt with in a subsequent article.
Humans↗
Treating common nail problems.
This article is a follow up to the article There is something wrong with my nail (AFP, June 1997). Conditions of the nail often pose diagnostic and management problems. The former issues were addressed in the previous article while this article focuses on current management options for this difficult range of conditions.
Humans↗
Practical cryosurgery.
Cryosurgery is a widely used modality for the treatment of superficial cutaneous lesions. It can be used for the treatment of benign, premalignant and malignant skin conditions.
Australia↗
Active site structure in cytochrome c peroxidase and myoglobin mutants: effects of altered hydrogen bonding to the proximal histidine.
The globins and peroxidases, while performing completely different chemistry, share features of the iron heme active site: a protoporphyrin IX prosthetic group is linked to the protein by the proximal histidine residue. X-ray absorption spectroscopy provides a method to determine the local structure of iron heme active sites in proteins. Our previous studies using X-ray absorption spectroscopy revealed a significant difference in the Fe-N epsilon bond length between the peroxidases and the globins [for a review, see Powers, L. (1994) Molecular Electronics and Molecular Electronic Devices, Vol. 3, p 211 CRC Press Inc., Boca Raton, FL]. Globins typically have an Fe-N epsilon distance close to 2.1 A while the Fe-N epsilon distance in the peroxidases is closer to 1.9 A. We have proposed [Sinclair, R., Powers, L., Bumpus, J., Albo, A., & Brock, B. (1992) Biochemistry 31, 4892] that strong hydrogen bonding to the proximal histidine is responsible for the shorter bond length in the peroxidases. Here we use site-specific mutagenesis to eliminate the strong proximal hydrogen bonding in cytochrome c peroxidase and to introduce strong proximal hydrogen bonding in myoglobin. Consistent with our hypothesis, elimination of the Asp235-His175 hydrogen bond in CcP results in elongation of Fe-N epsilon from approximately 1.9 to approximately 2.1 A. Conversely, introduction of a similar strong proximal hydrogen bond in myoglobin shortens Fe-N epsilon from approximately 2.1 to approximately 1.9 A. These results correlate well with other biochemical data.
Aspartic Acid↗
Anomalous moment and anisotropy behavior in Fe3O4 films.
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Journal Article↗
The structure-function relationship and reduction potentials of high oxidation states of myoglobin and peroxidase.
In these studies, we substitute electron-withdrawing (diacetyl) or -donating (diethyl) groups at the 2- and 4-positions of the heme in sperm whale Mb and HRP, and examine the structural and biochemical consequences. X-ray absorption spectroscopy shows that increased electron density at the heme results in an increased iron-pyrrole nitrogen average distance in both HRP and Mb, while decreased electron density results in shorter average distances. In HRP, the proximal ligand is constrained by a H-bonding network, and axial effects are manifested entirely at the distal site. Conversely, in Mb, where the proximal ligand is less constrained, axial effects are seen at the proximal side. In HRP, electron density at the heme iron depends linearly on pK3, a measure of the basicity of the porphyrin pyrrole nitrogens [Yamada, H., Makino, R., & Yamazaki, I. (1975) Arch. Biochem. Biophys. 169, 344-353]. Using diethyl substitution (pK3 = 5.8) and diacetyl substitution (pK3 = 3.3) in HRP and Mb, we measured the one-electron reduction potentials (E(O)') of HRP compounds I and II and ferryl Mb. Compound I showed a decreased E(O)' with increasing electron density at the heme (pK3), similar to E(O)' of ferric HRP. E(O)' of HRP compound II and ferryl Mb showed an opposite dependence. This behavior of E(O)', while initially surprising, can be explained by the apparent net positive charge on the iron porphyrin in each oxidation state of the hemoproteins.
Animals↗
Leukocyte hydrogen peroxide production in a surgical wound in mice. The effects of an amide local anaesthetic.
The oxygen metabolism of polymorphonuclear leukocytes (PMN) is of importance in local tissue repair processes. Amide local anaesthetics are commonly used to relieve surgical wound pain. The cellular effects of local anaesthetics in vivo is poorly described in the literature. However, interactions between amide local anaesthetics and the oxygen metabolism of leukocytes have been reported. To extend that knowledge, this paper investigates the influence of lidocaine treatment on the production of hydrogen peroxide (H2O2) by leukocyte oxygen metabolism. A soft tissue chamber model in the mouse was used, allowing measurements of the H2O2 production spontaneously and after phorbol myristate acetate (PMA) addition, from two different leukocyte pools. Exudate leukocytes were generally more reactive to PMA stimulation in comparison to tissue chamber adherent leukocytes. Topically administered lidocaine significantly influenced the number of leukocytes in the wound exudate at 24 h postoperatively. Exudate leukocytes, topically exposed to lidocaine, showed an enhanced H2O2 production in comparison to leukocytes receiving lidocaine systemically. At 6 days, the viability and the H2O2 production differed significantly between the group receiving topically applied lidocaine in comparison to placebo. We conclude that the wound healing process may be effected by topically applied lidocaine, administered in clinical doses, at least via interference with leukocyte oxygen metabolism.
Anesthetics, Local↗
The radial artery as a bypass graft.
The radial artery is being reintroduced into clinical practice to increase the number of arterial grafts for patients undergoing coronary artery bypass surgery. The radial artery is readily available from one or both forearms and removal is safe in patients who have a normal collateral circulation to the hand. Harvesting the radial artery with the adjacent veins using a minimal touch technique and vasodilators will prevent vasospasm and possibly early occlusion. A concern is that subclinical atheroma is present in many patients. The radial artery can be used as a single graft, anastomosed in a "Y" fashion with the internal mammary artery, or used as a sequential graft. The early mortality and complications are low. There are potential cost savings because the need for an incision in the leg is avoided, so that patients may be discharged early. The early results of radial artery grafting are encouraging. Further follow-up is required to determine the late patency and effects on survival of using the radial artery graft.
Aged↗
Postoperative pain relief by topical lidocaine in the surgical wound of hysterectomized patients.
BACKGROUND: To improve postoperative analgesia, local anesthetics have been administered perioperatively as infiltration or as aerosol in the surgical area. A previous study showed good analgesic effects by topical lidocaine in the wound in minor extraabdominal surgery (herniorraphy), while the same treatment in minor lower laparothomies did not improve postoperative analgesia. The present study investigated the effect of topical wound anesthesia using lidocaine aerosol on postoperative pain following major lower abdominal surgery. METHODS: Postoperative pain and analgesic requirements were studied in a double-blind randomized trial including 30 hysterectomized patients. Patients were randomized to receive single wound treatment either with lidocaine aerosol 500 mg (100 mg/ml; Xylocain aerosol, ASTRA, Sweden) (n = 15) or placebo aerosol (n = 15). Postoperative pain was evaluated by visual analogue scale (VAS). Requirements of opiate analgesics (buprenorphine) after surgery were monitored. RESULTS: Lidocaine aerosol induced a significantly (P < 0.001) better analgesia at rest (VAS) and a significant (P < 0.001) reduction in postoperative requirements of buprenorphine during the first 24 hours after surgery compared to placebo aerosol. Differences between the groups in pain scores (VAS) and buprenorphine requirements during the second postoperative day were not significant. Mean pain scores upon mobilization 24 h after surgery were significantly lower in the group receiving lidocaine aerosol (P < 0.05). The plasma lidocaine concentration 4 h after the administration of lidocaine was well below toxic level and plasma lidocaine was detectable 48 h postoperatively. No drug-related side effects were reported. CONCLUSION: A single dose of lidocaine aerosol topically administered in the surgical wound of hysterectomy patients improved analgesia during the first postoperative day with minimal risk of side effects.
Adult↗
Formation of a porphyrin pi-cation radical in the fluoride complex of horseradish peroxidase.
Horseradish peroxidase (HRP) was oxidized by IrCl6(2-) to a mixture of compounds I and II, the rate of oxidation and the ratio of the mixture being greatly affected by pH (Hayashi & Yamazaki, 1979). Oxidation of HRP by IrCl6(2-) in the presence of fluoride was significantly accelerated. This resulted in the formation of a new compound which is a ferric fluoride complex containing a porphyrin pi-cation radical. The spectrum of the new compound showed a decreased absorption band in the Soret region and a broad band at 570 nm; which was converted to that of the original ferric fluoride complex by addition of ascorbate or hydroquinone. Addition of cyanide slowed down the oxidation of HRP by IrCl6(2-), and the oxidation product was the same as that obtained in the absence of cyanide. Compound I was formed when H2O2 was added to HRP in the presence of fluoride or cyanide. The one-electron reduction potential (Eo') of the oxidized HRP-fluoride complex was measured at several pH values, the Eo' value at pH 7 being 861 +/- 4 mV. The ratio of delta Eo' to delta pH was 49 mV/pH unit.
Ascorbic Acid↗
X-ray absorption spectroscopy comparison of the active site structures of Phanerochaete chrysosporium lignin peroxidase isoenzymes H2, H3, H4, H5, H8, and H10.
The iron heme and its immediate environment can provide information that is pivotal to our understanding of the structural and mechanistic features that confer unusual properties to the heme peroxidases. X-ray absorption spectroscopy (XAS), which is ideally suited for the investigation of the local environment and electronic structure of the heme iron of hemeproteins, has been used to characterize a variety of lignin peroxidase and manganese-dependent peroxidase isoenzymes produced by the white rot fungus Phanerochaete chrysosporium. The data suggest no differences within the error in the first coordination shell of iron for the isoenzymes H2, H3, H4, H5, H8, and H10 examined in this study. The pyrrole nitrogens are at a distance of 2.05 +/- 0.015 A, and the proximal histidine nitrogens are at 1.93 +/- 0.02 A, while the sixth ligands are located at 2.17 +/- 0.03 A. Significant differences are observed in higher coordination shells which may be related to conformational differences in the heme.
Binding Sites↗
Development and evaluation of an ELISA using recombinant fusion protein to detect the presence of host antibody to equine arteritis virus.
A recombinant glutathione-S-transferase fusion protein expressing amino acids 55-98 of equine arteritis virus (EAV) GL (rGL 55-98) was tested in an ELISA for its ability to detect serum antibodies to EAV. Host antibodies induced following EAV infection bound the recombinant antigen by ELISA. The ELISA specificity and sensitivity were determined with a panel of equine sera including postinfection and postvaccination samples. A good correlation existed between EAV neutralizing antibody titers and ELISA absorbance values (r = 0.827). The sensitivity and specificity of the ELISA were 99.6 and 90.1%, respectively, compared with EAV neutralization test and the recombinant antigen did not crossreact in ELISA with equine sera directed against other common equine respiratory viruses. Three post-EAV infection equine sera raised against different EAV isolates reacted strongly in the ELISA, as did two equine sera raised against EAV vaccines, indicating that the viral epitope was conserved between the viruses tested. Following vaccination with an inactivated whole virus vaccine, antibody detected with the recombinant antigen ELISA preceded the development of a virus-neutralizing response. The study demonstrates the potential application of rGL 55-98 as a diagnostic antigen.
Animals↗
Solar nevogenesis: a surrogate for predicting a rise in incidence of malignant melanoma because of ozone depletion.
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Atmosphere↗
Hair abnormality diagnostic service.
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Diagnostic Services↗
Childhood condyloma accuminatum: association with genital and cutaneous human papillomavirus.
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Adult↗
An extended X-ray absorption fine structure investigation of the structure of the active site of lactoperoxidase.
Native lactoperoxidase, compound III, and the reduced forms (at pH 6 and 9) were studied using X-ray absorption spectroscopy (XAS). Native lactoperoxidase has four pyrrole nitrogen ligands at an average distance of 2.04 +/- 0.01 A, a proximal ligand at 1.91 +/- 0.02 A, and a sixth (distal) ligand at 2.16 +/- 0.03 A. Lactoperoxidase native enzyme has a first coordination shell structure that is similar to that of native lignin peroxidase [Sinclair, R., Yamazaki, I., Bumpus, J., Brock, B., Chang, C.-S., Albo, A., & Powers, L. (1992) Biochemistry 31, 4892-4900] and different from that of horseradish peroxidase [Chance, B., Powers, L., Ching, Y., Poulos, T., Schonbaum, G., Yamazaki, I., & Paul, K. (1984) Arch. Biochem. Biophys. 235, 596-611]. Similarly, lactoperoxidase compound III resembles lignin peroxidase compound III. The five-coordinated ferrous form was stable at pH 9, but at pH 6 it was rapidly converted to the six-coordinated form with a distal ligand at 2.18 +/- 0.03 A. No evidence typical of changes in spin state was obtained at the different pH values.
Absorptiometry, Photon↗