Efficacy of Nd-YAG laser for treatment of pyogenic granuloma on the fingers and toes.

Pyogenic granuloma (PG) is a common benign vascular proliferation which often occurs on the head, neck, hands, and feet. Among the various treatment options for PG, surgical excision is the most effective treatment which offers the lowest overall recurrence rates and also provides the exact diagnosis. However, it could have difficulties to do the surgery when lesions are located on the fingers and toes, especially very near to the nails, so laser may be a very good alternative choice. In this article, we evaluated the clinical efficacy and safety of neodymium-yttrium aluminum garnet (Nd:YAG) laser for treatment of PG located on the fingers and toes. Twenty-one patients with 21 PGs located on the fingers and toes were treated by multispot Nd-YAG laser. We chose monopulse (pulse width 10.5-13.5 ms; energy 100-125 J/cm2); treatment interval was 3-4 weeks. All lesions disappeared after one or two treatments. There was no apparent scar formation, no impact on the function of the fingers and toes, no damage to nail growth, and no recurrence in more than 12-month follow-up. Nd-YAG is an effective and safety treatment option for treatment of PG located on the fingers and toes.

The major nucleoside triphosphatase in pea (Pisum sativum L.) nuclei and in rat liver nuclei share common epitopes also present in nuclear lamins.

The major nucleoside triphosphatase (NTPase) activities in mammalian and pea (Pisum sativum L.) nuclei are associated with enzymes that are very similar both biochemically and immunochemically. The major NTPase from rat liver nuclei appears to be a 46-kD enzyme that represents the N-terminal portion of lamins A and C, two lamina proteins that apparently arise from the same gene by alternate splicing. Monoclonal antibody (MAb) G2, raised to human lamin C, both immunoprecipitates the major (47 kD) NTPase in pea nuclei and recognizes it in western blot analyses. A polyclonal antibody preparation raised to the 47-kD pea NTPase (pc480) reacts with the same lamin bands that are recognized by MAb G2 in mammalian nuclei. The pc480 antibodies also bind to the same lamin-like bands in pea nuclear envelope-matrix preparations that are recognized by G2 and three other MAbs known to bind to mammalian lamins. In immunofluorescence assays, pc480 and anti-lamin antibodies stain both cytoplasmic and nuclear antigens in plant cells, with slightly enhanced staining along the periphery of the nuclei. These results indicate that the pea and rat liver NTPases are structurally similar and that, in pea nuclei as in rat liver nuclei, the major NTPase is probably derived from a lamin precursor by proteolysis.