Superficial Temporal Artery Island Flap Combined With Laser Hair Removal for Inadequate Skin Expansion Following Tissue Expansion: A Case Report of Congenital Melanocytic Nevus of the Forehead in an Adult.

Tissue expansion is a handy reconstructive technique for the head and neck region; however, its implementation requires careful planning and surgical experience. If tissue expansion is inadequate, forced closure results in wound tension and risks complications, such as postoperative deformity, wide scarring, and wound dehiscence. We report a case of adult forehead melanocytic nevus excision using a tissue expander (TE) where complications caused by insufficient tissue expansion were avoided by creating a flap using a dog ear. The patient was a male in his 20s who underwent surgery with a TE for a congenital melanocytic nevus sized 15 × 10 cm on the left forehead. Resection was performed by tissue expansion using two TEs; however, simple advancement flaps led to excessive wound tension, risk of elevation of the eyebrow on the affected side, and postoperative scarring. Hence, a superficial temporal artery fasciocutaneous island flap with left superficial temporal vessels as a pedicle was raised at the dog ear and moved to the site of strong tension, and the wound was closed without difficulty. Although postoperative laser hair removal was required, both the appearance and functional results were satisfactory. Using anatomical flaps obtained from the surroundings during tissue expansion helps avoid complications associated with forced wound closure.

An extracellular polysaccharide is involved in the aluminum tolerance of Pullulanibacillus sp. CA42, a newly isolated strain from the Chinese water chestnut growing in an actual acid sulfate soil area in Vietnam.

A novel aluminum-tolerant bacterial strain CA42 was isolated from the aquatic plant Eleocharis dulcis, which grows in a highly acidic swamp in Vietnam. Inoculation with CA42 allowed Oryza sativa to grow in the presence of 300 µM AlCl3 at pH 3.5, and biofilms were observed around the roots. Using 16S rRNA gene sequencing analysis, the strain was identified as Pullulanibacillus sp. CA42. This strain secreted large amounts of an extracellular polysaccharide (CA42 EPS). Results from structural analyses on CA42 EPS, namely methylation analysis and nuclear magnetic resonance (NMR), indicated that the chemical structure of CA42 EPS was a glycogen-like α-glucan. Purified CA42 EPS and the commercially available oyster glycogen adsorbed aluminum ions up to 15-30 µmol/g dry weight. Digestion treatments with α-amylase and pullulanase completely attenuated the aluminum ion-adsorbing activity of purified CA42 EPS and oyster glycogen, suggesting that the glycogen-like structure adsorbed aluminum ions and that its branching structure played an important role in its aluminum adsorbing activity. Furthermore, the aluminum tolerance of CA42 cells was attenuated by pullulanase treatment directly on the live CA42 cells. These results suggest that CA42 EPS adsorbs aluminum ions and is involved in the aluminum tolerance mechanism of Pullulanibacillus sp. CA42. Thus, this strain may be a potential plant growth-promoting bacterium in acidic soils. In addition, this study is the first to report a glycogen-like polysaccharide that adsorbs aluminum ions.

Common variant of leucine-rich repeat-containing 16A (LRRC16A) gene is associated with gout susceptibility.

Gout is a common disease resulting from hyperuricemia which causes acute arthritis. Recently, genome-wide association studies revealed an association between serum uric acid levels and a common variant of leucine-rich repeat-containing 16A (LRRC16A) gene. However, it remains to be clarified whether LRRC16A contributes to the susceptibility to gout. In this study, we investigated the relationship between rs742132 in LRRC16A and gout. A total of 545 Japanese male gout cases and 1,115 male individuals as a control group were genotyped. rs742132 A/A genotype significantly increased the risk of gout, conferring an odds ratio of 1.30 (95 % CI 1.05-1.60; p = 0.015). LRRC16A encodes a protein called capping protein ARP2/3 and myosin-I linker (CARMIL), which serves as an inhibitor of the actin capping protein (CP). CP is an essential element of the actin cytoskeleton, which binds to the barbed end of the actin filament and regulates its polymerization. In the apical membrane of proximal tubular cells in the human kidney, the urate-transporting multimolecular complex (urate transportsome) is proposed to consist of several urate transporters and scaffolding proteins, which interact with the actin cytoskeleton. Thus, if there is a CARMIL dysfunction and regulatory disability in actin polymerization, urate transportsome may be unable to operate appropriately. We have shown for the first time that CARMIL/LRRC16A was associated with gout, which could be due to urate transportsome failure.