Consistent application of compression: An under-considered variable in the prevention of venous leg ulcers.

Venous leg ulcers, the most common leg ulcer, occur in patients with chronic venous insufficiency due to venous hypertension. Evidence supports the conservative treatment with lower extremity compression, ideally between 30-40 mm Hg. Pressures in this range provide enough force to partially collapse lower extremity veins without restricting arterial flow in patients without peripheral arterial disease. There are many options for applying such compression, and those who apply these devices have varying levels of training and backgrounds. In this quality improvement project, a single observer utilised a reusable pressure monitor to compare pressures applied using different devices by individuals in wound clinics with diverse training from specialties of dermatology, podiatry, and general surgery. Average compression was higher in the dermatology wound clinic (n = 153) compared to the general surgery clinic (n = 53) (35.7 ± 13.3 and 27.2 ± 8.0 mm Hg, respectively, p < 0.0001), and wraps applied by clinic staff (n = 194) were nearly twice as likely as a self-applied wrap (n = 71) to have pressures greater than 40 mm Hg (relative risk: 2.2, 95% confidence interval: 1.136-4.423, p = 0.02). Pressures were also dependent upon the specific compression device used, with CircAid®s (35.5 mm Hg, SD: 12.0 mm Hg, n = 159) providing higher average pressures than Sigvaris Compreflex (29.5 mm Hg, SD: 7.7 mm Hg, n = 53, p = 0.009) and Sigvaris Coolflex (25.2 mm Hg, SD: 8.0 mm Hg, n = 32, p < 0.0001). These results indicate that the device-provided pressure may be dependent on both the compression device and the background and training of the applicator. We propose that standardisation in the training of compression application and increased use of a point-of-care pressure monitor may improve the consistency of applied compression, thus improving adherence to treatment and outcomes in patients with chronic venous insufficiency.

Acral Amelanotic Melanoma Mimicking a Foot Ulcer.

Acral amelanotic melanoma can be difficult to diagnose and is often clinically aggressive. The present report describes a case of an acral amelanotic melanoma presenting as a non-healing wound after mimicking a plantar wart for two years. The decision to biopsy a borderline-suspicious lesion on the lower extremity in an elderly individual must be weighed carefully, as lower extremity biopsy carries a risk of poor wound healing and other complications. We discuss clinical and epidemiologic features that can assist in deciding when to perform a biopsy in this setting and can improve the early detection of acral amelanotic melanoma.

The l-isoaspartate modification within protein fragments in the aging lens can promote protein aggregation.

Transparency in the lens is accomplished by the dense packing and short-range order interactions of the crystallin proteins in fiber cells lacking organelles. These features are accompanied by a lack of protein turnover, leaving lens proteins susceptible to a number of damaging modifications and aggregation. The loss of lens transparency is attributed in part to such aggregation during aging. Among the damaging post-translational modifications that accumulate in long-lived proteins, isomerization at aspartate residues has been shown to be extensive throughout the crystallins. In this study of the human lens, we localize the accumulation of l-isoaspartate within water-soluble protein extracts primarily to crystallin peptides in high-molecular weight aggregates and show with MS that these peptides are from a variety of crystallins. To investigate the consequences of aspartate isomerization, we investigated two αA crystallin peptides 52LFRTVLDSGISEVR65 and 89VQDDFVEIH98, identified within this study, with the l-isoaspartate modification introduced at Asp58 and Asp91, respectively. Importantly, whereas both peptides modestly increase protein precipitation, the native 52LFRTVLDSGISEVR65 peptide shows higher aggregation propensity. In contrast, the introduction of l-isoaspartate within a previously identified anti-chaperone peptide from water-insoluble aggregates, αA crystallin 66SDRDKFVIFL(isoAsp)VKHF80, results in enhanced amyloid formation in vitro The modification of this peptide also increases aggregation of the lens chaperone αB crystallin. These findings may represent multiple pathways within the lens wherein the isomerization of aspartate residues in crystallin peptides differentially results in peptides associating with water-soluble or water-insoluble aggregates. Here the eye lens serves as a model for the cleavage and modification of long-lived proteins within other aging tissues.