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    Millipore lhcnm2 human skeletal muscle cells
    Effects of CHC17 and CHC22 down-regulation on CI-MPR trafficking in human myoblasts reproduce effects in HeLa cells. (A–D) <t>LHCNM2</t> human skeletal muscle myoblasts were differentiated, treated with control siRNA (A and C) or siRNA targeting CHC22 (B) or CHC17 (D) and processed for immunofluorescence. Cells were double labeled using antibodies against CHC17 (green in merged insets), CHC22 (green in merged insets), and CI-MPR (red in merged insets) as indicated. Bars, 20 µm. (E) LHCNM2 cells were differentiated and treated with siRNA targeting CHC17 or CHC22 or control siRNA as indicated at the top of each lane. Whole-cell detergent lysates were separated by SDS-PAGE and immunoblotted with antibodies against the proteins indicated at the left. Immature (pro), intermediate (pre), and mature (mat) forms of Cathepsin D are indicated at the left. β-Actin serves as a loading control. (F) Quantification of CI-MPR levels in whole-cell detergent lysates from siRNA-treated cells generated as in E. Shown are levels ± SEM in the samples treated with the specific siRNA indicated under each bar compared with levels in cells treated with control siRNA in the same experiment ( n = 5). P-values for selected samples are indicated. (G) Quantification of preCathepsin D levels in whole-cell detergent lysates from siRNA treated cells generated as in E. Shown are levels ± SEM in the samples treated with the specific siRNA indicated under each bar compared with levels in cells treated with control siRNA in the same experiment ( n = 5). P-values for selected samples are indicated.
    Lhcnm2 Human Skeletal Muscle Cells, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Effects of CHC17 and CHC22 down-regulation on CI-MPR trafficking in human myoblasts reproduce effects in HeLa cells. (A–D) LHCNM2 human skeletal muscle myoblasts were differentiated, treated with control siRNA (A and C) or siRNA targeting CHC22 (B) or CHC17 (D) and processed for immunofluorescence. Cells were double labeled using antibodies against CHC17 (green in merged insets), CHC22 (green in merged insets), and CI-MPR (red in merged insets) as indicated. Bars, 20 µm. (E) LHCNM2 cells were differentiated and treated with siRNA targeting CHC17 or CHC22 or control siRNA as indicated at the top of each lane. Whole-cell detergent lysates were separated by SDS-PAGE and immunoblotted with antibodies against the proteins indicated at the left. Immature (pro), intermediate (pre), and mature (mat) forms of Cathepsin D are indicated at the left. β-Actin serves as a loading control. (F) Quantification of CI-MPR levels in whole-cell detergent lysates from siRNA-treated cells generated as in E. Shown are levels ± SEM in the samples treated with the specific siRNA indicated under each bar compared with levels in cells treated with control siRNA in the same experiment ( n = 5). P-values for selected samples are indicated. (G) Quantification of preCathepsin D levels in whole-cell detergent lysates from siRNA treated cells generated as in E. Shown are levels ± SEM in the samples treated with the specific siRNA indicated under each bar compared with levels in cells treated with control siRNA in the same experiment ( n = 5). P-values for selected samples are indicated.

    Journal: The Journal of Cell Biology

    Article Title: The clathrin heavy chain isoform CHC22 functions in a novel endosomal sorting step

    doi: 10.1083/jcb.200908057

    Figure Lengend Snippet: Effects of CHC17 and CHC22 down-regulation on CI-MPR trafficking in human myoblasts reproduce effects in HeLa cells. (A–D) LHCNM2 human skeletal muscle myoblasts were differentiated, treated with control siRNA (A and C) or siRNA targeting CHC22 (B) or CHC17 (D) and processed for immunofluorescence. Cells were double labeled using antibodies against CHC17 (green in merged insets), CHC22 (green in merged insets), and CI-MPR (red in merged insets) as indicated. Bars, 20 µm. (E) LHCNM2 cells were differentiated and treated with siRNA targeting CHC17 or CHC22 or control siRNA as indicated at the top of each lane. Whole-cell detergent lysates were separated by SDS-PAGE and immunoblotted with antibodies against the proteins indicated at the left. Immature (pro), intermediate (pre), and mature (mat) forms of Cathepsin D are indicated at the left. β-Actin serves as a loading control. (F) Quantification of CI-MPR levels in whole-cell detergent lysates from siRNA-treated cells generated as in E. Shown are levels ± SEM in the samples treated with the specific siRNA indicated under each bar compared with levels in cells treated with control siRNA in the same experiment ( n = 5). P-values for selected samples are indicated. (G) Quantification of preCathepsin D levels in whole-cell detergent lysates from siRNA treated cells generated as in E. Shown are levels ± SEM in the samples treated with the specific siRNA indicated under each bar compared with levels in cells treated with control siRNA in the same experiment ( n = 5). P-values for selected samples are indicated.

    Article Snippet: LHCNM2 human skeletal muscle cells ( ) were maintained in tissue culture flasks coated with rat-tail collagen in basal medium (4:1 DME/M199, 0.02 M Hepes, 0.03 µg/ml ZnSO4 , and 1.4 µg/ml vitamin B12) with 15% fetal bovine serum (FBS), 55 ng/ml dexamethasone, 2.5 ng/ml hepatocyte growth factor (Sigma-Aldrich), 50 U/ml penicillin, 50 µg/ml streptomycin, and 0.625 µg/ml fungizone (growth medium).

    Techniques: Immunofluorescence, Labeling, SDS Page, Generated

    CHC22 is present at variable levels in most cell types and does not participate in endocytosis. (A) Detergent lysates of 10 tissue culture cell lines (equalized for protein content) were separated by SDS-PAGE and immunoblotted with antibodies against proteins indicated at the left. Tissue sources for the cell lines were cervical epithelium (HeLa), mammary gland epithelium (MDA 231), epidermal epithelium (A431), kidney epithelium (HEK 293), foreskin fibroblast (HFF), hepatocellular carcinoma (HepG2), natural killer lymphocyte (NKL), rhabdomyosarcoma (JR1), and skeletal muscle (LHCNM2 and C2C12), with all derived from human samples except C2C12 (mouse). (B) Indicated amounts of recombinant protein fragments (in ng) of CHC17 (amino acids 1–1074, CHC17-TDD) or CHC22 (amino acids 1521–1640, CHC22-TXD) and of detergent lysates (in µg) of HeLa or LHCNM2 cells (designated at the far right) were separated by SDS-PAGE and analyzed sequentially on the same immunoblot, after stripping in between, with antibodies against the CHC for the entire row indicated at the left. Below, each plot shows the intensity of the immunoblotting signal (x-axis) versus the amount of recombinant protein (left y-axis, solid squares) or detergent lysate (right y-axis, solid triangles) analyzed. CHC amount in cell lysates was determined by intersection with the immunoblotting signals from the recombinant fragments used for antibody calibration, adjusting for fragment length. Measured ratios for CHC22 compared with CHC17 were 1:8 for LHCNM2 and 1:12 for HeLa. (C) Detergent lysates of HeLa cells treated with siRNA to deplete CHCs indicated at the top or with control siRNA were separated by SDS-PAGE and immunoblotted with antibodies against proteins indicated at the left. α-Tubulin (α-tub) serves as a loading control. (D–F) HeLa cells treated with control siRNA (D) or siRNA to deplete cells of CHC17 (E) and CHC22 (F) were incubated with fluorescent transferrin (green in merged insets) and internalization was allowed for 10 min. Cells were then fixed and processed for double immunofluorescence using antibodies against CHC17 (red in merged insets) or CHC22 (blue in merged insets) as indicated. Bars, 20 µm.

    Journal: The Journal of Cell Biology

    Article Title: The clathrin heavy chain isoform CHC22 functions in a novel endosomal sorting step

    doi: 10.1083/jcb.200908057

    Figure Lengend Snippet: CHC22 is present at variable levels in most cell types and does not participate in endocytosis. (A) Detergent lysates of 10 tissue culture cell lines (equalized for protein content) were separated by SDS-PAGE and immunoblotted with antibodies against proteins indicated at the left. Tissue sources for the cell lines were cervical epithelium (HeLa), mammary gland epithelium (MDA 231), epidermal epithelium (A431), kidney epithelium (HEK 293), foreskin fibroblast (HFF), hepatocellular carcinoma (HepG2), natural killer lymphocyte (NKL), rhabdomyosarcoma (JR1), and skeletal muscle (LHCNM2 and C2C12), with all derived from human samples except C2C12 (mouse). (B) Indicated amounts of recombinant protein fragments (in ng) of CHC17 (amino acids 1–1074, CHC17-TDD) or CHC22 (amino acids 1521–1640, CHC22-TXD) and of detergent lysates (in µg) of HeLa or LHCNM2 cells (designated at the far right) were separated by SDS-PAGE and analyzed sequentially on the same immunoblot, after stripping in between, with antibodies against the CHC for the entire row indicated at the left. Below, each plot shows the intensity of the immunoblotting signal (x-axis) versus the amount of recombinant protein (left y-axis, solid squares) or detergent lysate (right y-axis, solid triangles) analyzed. CHC amount in cell lysates was determined by intersection with the immunoblotting signals from the recombinant fragments used for antibody calibration, adjusting for fragment length. Measured ratios for CHC22 compared with CHC17 were 1:8 for LHCNM2 and 1:12 for HeLa. (C) Detergent lysates of HeLa cells treated with siRNA to deplete CHCs indicated at the top or with control siRNA were separated by SDS-PAGE and immunoblotted with antibodies against proteins indicated at the left. α-Tubulin (α-tub) serves as a loading control. (D–F) HeLa cells treated with control siRNA (D) or siRNA to deplete cells of CHC17 (E) and CHC22 (F) were incubated with fluorescent transferrin (green in merged insets) and internalization was allowed for 10 min. Cells were then fixed and processed for double immunofluorescence using antibodies against CHC17 (red in merged insets) or CHC22 (blue in merged insets) as indicated. Bars, 20 µm.

    Article Snippet: LHCNM2 human skeletal muscle cells ( ) were maintained in tissue culture flasks coated with rat-tail collagen in basal medium (4:1 DME/M199, 0.02 M Hepes, 0.03 µg/ml ZnSO4 , and 1.4 µg/ml vitamin B12) with 15% fetal bovine serum (FBS), 55 ng/ml dexamethasone, 2.5 ng/ml hepatocyte growth factor (Sigma-Aldrich), 50 U/ml penicillin, 50 µg/ml streptomycin, and 0.625 µg/ml fungizone (growth medium).

    Techniques: SDS Page, Multiple Displacement Amplification, Derivative Assay, Recombinant, Stripping Membranes, Incubation, Immunofluorescence

    Syntaxin 10 depletion partially phenocopies CHC22 depletion and is implicated in GLUT4 sequestration. (A–D) LHCNM2 human skeletal muscle myoblasts were differentiated, treated with control siRNA (A) or siRNA targeting STX10 (B and C) or CHC22 (D), and processed for immunofluorescence. Cells were double labeled using antibodies against STX10 (A, B, and D; green in merged insets), CHC22 (C; green in merged inset), and GLUT4 (red in merged insets) as indicated. Bars, 20 µm. (E–G) HeLa cells treated with control siRNA (E) or siRNA to deplete STX10 (F and G) levels were processed for immunofluorescence and labeled for STX10 (E and F; green in merged insets) and CI-MPR (E and F; red in merged insets) as indicated at the top. In G, fluorescent STxB (red in merged inset) in fresh medium was bound to cells for 30 min on ice, washed in PBS and chased for 60 min in fresh medium at 37°C, fixed, and processed for immunofluorescence using antibodies against GM130 (green in merged insets). (H) Detergent lysates of LHCNM2 cells treated with siRNA to deplete CHC17, CHC22, or STX10 or with control siRNA as indicated at the top were separated by SDS-PAGE and immunoblotted with antibodies against the proteins indicated at the left. α-Tubulin (α-tub) serves as a loading control. (I) Quantification of GLUT4 levels in detergent lysates of siRNA-treated cells generated as in H. Shown are levels ± SEM in the samples treated with the specific siRNA indicated under each bar compared with levels in cells treated with control siRNA in the same experiment ( n = 6). P-values for selected samples are indicated.

    Journal: The Journal of Cell Biology

    Article Title: The clathrin heavy chain isoform CHC22 functions in a novel endosomal sorting step

    doi: 10.1083/jcb.200908057

    Figure Lengend Snippet: Syntaxin 10 depletion partially phenocopies CHC22 depletion and is implicated in GLUT4 sequestration. (A–D) LHCNM2 human skeletal muscle myoblasts were differentiated, treated with control siRNA (A) or siRNA targeting STX10 (B and C) or CHC22 (D), and processed for immunofluorescence. Cells were double labeled using antibodies against STX10 (A, B, and D; green in merged insets), CHC22 (C; green in merged inset), and GLUT4 (red in merged insets) as indicated. Bars, 20 µm. (E–G) HeLa cells treated with control siRNA (E) or siRNA to deplete STX10 (F and G) levels were processed for immunofluorescence and labeled for STX10 (E and F; green in merged insets) and CI-MPR (E and F; red in merged insets) as indicated at the top. In G, fluorescent STxB (red in merged inset) in fresh medium was bound to cells for 30 min on ice, washed in PBS and chased for 60 min in fresh medium at 37°C, fixed, and processed for immunofluorescence using antibodies against GM130 (green in merged insets). (H) Detergent lysates of LHCNM2 cells treated with siRNA to deplete CHC17, CHC22, or STX10 or with control siRNA as indicated at the top were separated by SDS-PAGE and immunoblotted with antibodies against the proteins indicated at the left. α-Tubulin (α-tub) serves as a loading control. (I) Quantification of GLUT4 levels in detergent lysates of siRNA-treated cells generated as in H. Shown are levels ± SEM in the samples treated with the specific siRNA indicated under each bar compared with levels in cells treated with control siRNA in the same experiment ( n = 6). P-values for selected samples are indicated.

    Article Snippet: LHCNM2 human skeletal muscle cells ( ) were maintained in tissue culture flasks coated with rat-tail collagen in basal medium (4:1 DME/M199, 0.02 M Hepes, 0.03 µg/ml ZnSO4 , and 1.4 µg/ml vitamin B12) with 15% fetal bovine serum (FBS), 55 ng/ml dexamethasone, 2.5 ng/ml hepatocyte growth factor (Sigma-Aldrich), 50 U/ml penicillin, 50 µg/ml streptomycin, and 0.625 µg/ml fungizone (growth medium).

    Techniques: Immunofluorescence, Labeling, SDS Page, Generated