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Mean echo intensity and K values can reflect the extent of fibrosis in affected muscles and may be valuable for quantifying muscle fibrosis in clinical practice.

Negative-pressure wound therapy has recently gained popularity in chronic wound care. This study attempted to explore effects of different negative pressures on epithelial migration in the wound-healing process. The electric cell-substrate impedance sensing (ECIS) technique was used to create a 5 x 10(-4) cm(2) wound in the Madin-Darby canine kidney (MDCK) and human keratinocyte (HaCaT) cells. The wounded cells were cultured in a negative pressure incubator at ambient pressure (AP) and negative pressures of 75 mmHg (NP(75)), 125 mmHg (NP(125)), and 175 mmHg (NP(175)). The effective time (ET), complete wound healing time (T(max)), healing rate (R(heal)), cell diameter, and wound area over time at different pressures were evaluated. Traditional wound-healing assays were prepared for fluorescent staining of cells viability, cell junction proteins, including ZO-1 and E-cadherin, and actins. Amount of cell junction proteins at AP and NP(125) was also quantified. In MDCK cells, the ET (1.25 +/- 0.27 h), T(max) (1.76 +/- 0.32 h), and R(heal) (2.94 +/- 0.62 x 10(-4) cm(2)/h) at NP(125) were significantly (P < 0.01) different from those at three other pressure conditions. In HaCaT cells, the T(max) (7.34 +/- 0.29 h) and R(heal) (6.82 +/- 0.26 x 10(-5) cm(2)/h) at NP(125) were significantly (P < 0.01) different from those at NP(75). Prominent cell migration features were identified in cells at the specific negative pressure. Cell migration activities at different pressures can be documented with the real-time wound-healing measurement system. Negative pressure of 125 mmHg can help disassemble the cell junction to enhance epithelial migration and subsequently result in quick wound closure.

J. Neurochem. (2010) 113, 1230–1239. Abstract Albumin is the most abundant protein in both CSF and plasma, and albumin quotient is often used to assess the functions of brain barriers especially that of the blood‐CSF barrier [i.e. the choroid plexus (CP) which also secretes CSF]. In this study, we took albumin as a model molecule to investigate ageing‐related alterations in the CSF‐CP system in sheep. We found significant ageing‐related increases in the weight of lateral CP [122.4 ± 14.0 mg in the young, 198.6 ± 35.4 mg in the middle aged, 286.1 ± 25.1 mg in the old (p < 0.05)], in the CSF albumin as well as the albumin quotient. Albumin protein spots in old CSF displayed wider on 2D western immunoblotting images, and had higher densities on images of 2D large gels stained with Pro‐Q Emerald 488 compared to the young samples, suggesting ageing‐related post‐translational modification in the albumin. CSF secretion was reduced with age: 0.148 ± 0.013 mL/min/g in the young, 0.092 ± 0.02 mL/min/g in the middle aged, 0.070 ± 0.013 mL/min/g in the old (p < 0.05). The 125I‐BSA extraction was not different among the sheep groups, nor was altered by temperature reduction, monensin, nocodazole, anti‐transforming growth factor β receptor II antibody, as well as unlabelled albumins. In conclusion, elevation of albumin in old CSF is associated with reduced CSF secretion by the CP, which size increases with age. 125I‐BSA extract, reflecting the extracellular space rather than the active albumin uptake in the CP, is not different between ages. These early changes in health ageing may result in the accumulation and modifications of CSF proteins leading to neurotoxicity.

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