Journal: Journal of Cachexia, Sarcopenia and Muscle

Article Title: p62/SQSTM1 but not LC3 is accumulated in sarcopenic muscle of mice

doi: 10.1002/jcsm.12045

Figure Lengend Snippet: Serial cryosections of the quadriceps muscle of 3‐month‐old and 24‐month‐old mice. p62/SQSTM1 and LC3 immunoreactivity was visualized using FITC‐conjugated or Rhodamine‐conjugated antibodies. In young quadriceps muscle, immunofluorescence labelling showed that p62/SQSTM1 was present in the membrane and at a low level in the cytosol of several muscle fibres (A and C). Marked increases of p62/SQSTM1 immunoreactivity were observed in the membrane and the cytosol of aged muscle fibres (D). No apparent difference in LC3 immunoreactivity was observed in the muscle between 3‐month‐old and 24‐month‐old mice (B and E). p62/SQSTM1‐positive muscle fibres exhibit significant smaller cross‐sectional area than p62/SQSTM1‐negative fibres in the muscle of aged mice ( H ). White circles and squares indicate the same fibres on different immuno images (A–F). White arrows denote the muscle fibres possessing p62/SQSTM1. Bar = 50 µm.

Article Snippet: After being washed in PBS, sections were incubated with anti‐rabbit fluorescein isothiocyanate (FITC)‐conjugated (1:100 final dilution; Rockland Immunochemicals, Inc., USA) and anti‐goat Rhodamine‐conjugated (1:100 final dilution; Chemicon International Inc., USA) secondary antibodies.

Techniques: Immunofluorescence, Membrane

Journal:

Article Title: Molecular Crowding Inhibits Intramolecular Breathing Motions in Proteins

doi: 10.1016/j.jmb.2007.07.075

Figure Lengend Snippet: WAXS as a function of 1/d. (a) WAXS from bovine met hemoglobin. The figure is a superposition of 21 traces from solutions prepared at concentrations of 1; 2; 8.2; 10.2; 12.8; 16; 20; 25; 30; 35; 40; 47; 55; 64; 87; 102; 119; 162; 189; 257; and 300 mg/ml. (b) WAXS from hen egg white lysozyme. The figure is a superposition of 24 traces from scattering from solutions prepared at concentrations of 1; 2; 4.1; 8.2; 10.2; 12.8; 16; 20; 25; 30; 35; 47; 55; 64; 75; 87; 102; 119; 139; 162; 189; 220; 257; and 300 mg/ml. Data from solutions of 55-300 mg/ml were nearly indistinguishable. Data from 1 and 2 mg/ml solutions are readily identified due to their increased statistical fluctuations. Scaling of patterns indicated that under the conditions used, hemoglobin had a solubility of approximately 250 mg/ml and lysozyme a solubility of approximately 150 mg/ml. Scattering from solutions prepared at concentrations greater than this were virtually identical as judged by scaling, estimated excluded volume and intensity distribution.

Article Snippet: Bovine erythrocyte hemoglobin (Calbiochem, EMD Biosciences, Inc., San Diego, CA), equine myoglobin, bovine serum albumin (Sigma, St. Louis, MO) and hen egg white avidin (Affiland S.A., Ans-liege, Belgium) were diluted in phosphate-buffered saline without calcium and magnesium (Biowhittaker, Cambrex, Rockland, ME) to a final concentrated solution as indicated in the figure legend, then serially diluted to the noted concentrations.

Techniques: Solubility