Muscle strength and foot pressure vary depending on the type of foot pain.

This study compared muscle strength and foot pressure among patients with metatarsalgia, patients with plantar fasciitis, and healthy controls. A total of 31 patients with foot pain (14 metatarsalgia and 17 plantar fasciitis) and 29 healthy controls participated in the study. The strengths of the plantar flexor and hip muscles were measured using isokinetic and handheld dynamometers, respectively. Foot pressure parameters, including the pressure-time integral (PTI) and foot arch index (AI), were assessed using pedobarography. Compared with the healthy control group, plantar flexor strength was significantly reduced in the affected feet of the metatarsalgia and plantar fasciitis groups (F = 0.083, all p < 0.001); however, hip strength was significantly decreased only in the affected feet of the metatarsalgia group (F = 20.900, p < 0.001). Plantar flexor (p < 0.001) and hip (p = 0.004) strength were significantly lower in the metatarsalgia group than in the plantar fasciitis group. The PTI was lower in the forefeet of the affected feet in the metatarsalgia (p < 0.001) and plantar fasciitis (p = 0.004) groups. Foot AI (p < 0.001) was significantly reduced only in the metatarsalgia group. These results suggest the need to consider the evaluation of muscle strength and foot pressure in both feet for the diagnosis and treatment of foot pain.

Functional expression and characterization of recombinant NADPH-P450 reductase from Malassezia globosa.

Malassezia globosa is a common pathogenic fungus that causes skin diseases including dandruff and seborrheic dermatitis in humans. Analysis of its genome identified a gene (MGL_1677) coding for a putative NADPH-P450 reductase (NPR) to support the fungal cytochrome P450 enzymes. The heterologously expressed recombinant M. globosa NPR protein was purified, and its functional features were characterized. The purified protein generated a single band on SDS-PAGE at 80.74 kDa and had an absorption maximum at 452 nm, indicating its possible function as an oxidized flavin cofactor. It evidenced NADPH-dependent reducing activity for cytochrome c or nitroblue tetrazolium. Human P450 1A2 and 2A6 were able to successfully catalyze the O-deethylation of 7- ethoxyresorufin and the 7-hydroxylation of coumarin, respectively, with the support of the purified NPR. These results demonstrate that purified NPR is an orthologous reductase protein that supports cytochrome P450 enzymes in M. globosa.

Induction of steroid sulfatase expression by tumor necrosis factor-α through phosphatidylinositol 3-kinase/Akt signaling pathway in PC-3 human prostate cancer cells.

Steroid sulfatase (STS) is responsible for the hydrolysis of aryl and alkyl steroid sulfates and has a pivotal role in regulating the formation of biologically active estrogens. STS may be considered a new promising drug target for treating estrogen-mediated carcinogenesis. However, the molecular mechanism of STS expression is not well-known. To investigate whether tumor necrosis factor (TNF)-α is able to regulate gene transcription of STS, we studied the effect of TNF-α on STS expression in PC-3 human prostate cancer cells. RT-PCR and Western blot analysis showed that TNF-α significantly induced the expression of STS mRNA and protein in a concentration- and time-dependent manner. Treatment with TNF-α resulted in a strong increase in the phosphorylation of Akt on Ser-473 and when cells were treated with phosphatidylinositol (PI) 3-kinase inhibitors such as LY294002 or wortmannin, or Akt inhibitor (Akt inhibitor IV), induction of STS mRNA expression by TNF-α was significantly prevented. Moreover, activation of Akt1 by expressing the constitutively active form of Akt1 increased STS expression whereas dominant-negative Akt suppressed TNF-α-mediated STS induction. We also found that TNF-α is able to increase STS mRNA expression in other human cancer cells such as LNCaP, MDA-MB-231, and MCF-7 as well as PC-3 cells. Taken together, our results strongly suggest that PI 3-kinase/Akt activation mediates induction of human STS gene expression by TNF-α in human cancer cells.