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find Keyword "Cytoskeletal protein" 3 results
  • Effect of Lung Volume Reduction Surgery on mRNA Expression Levels of Cytoskeletal Proteins in Diaphragmatic Muscle Tissues of Emphysematous Rabbits

    Objective To investigate the effect of lung volume reduction surgery (LVRS) on messenger RNA expression levels of cytoskeletal proteins in diaphragmatic muscle tissues of emphysematous rabbits. Methods A total of 40 rabbits were randomly divided into 4 groups (10 rabbits in each group) :normal control group, emphysema group, sham operation group and LVRS group. Rabbits in control group were intratracheally administered with 0.9% normal sodium, but those in other groups were intratracheally administered with 0.4% papain at the dose of 0.5 ml/kg and inhaled cigarette smoke to induce emphysema model. Then, rabbits in emphysema group were fed routinely, however, after median sternotomy , bilateral LVRS was performed in LVRS group but not in sham operation group. The mRNA expression levels of titin and nebulin in the diaphragmatic muscles of rabbits in each group were detected by reverse transcription-polymerase chain reaction(RT-PCR). Results Compared with control group, the mRNA expression levels of titin and nebulin in the rabbit diaphragm of emphysema groups and sham operation group decreased significantly (P〈0.01 ), so did those in LVRS group (P〈0.05). But it increased significantly in LVRS group compared with emphysema group and sham operation group (P〈0.05). Conclusion LVRS can increase the mRNA expression levels of titin and nebulin in diaphragmatic muscle tissues of emphysematous rabbits, which may be the associated mechanisms at the molecular level in restoring the functions of the emphysematous diaphragm by LVRS.

    Release date:2016-08-30 06:23 Export PDF Favorites Scan
  • PROMOTING EFFECT OF MASSAGE ON QUADRICEPS FEMORIS REPAIR OF RABBIT IN VIVO

    【Abstract】 Objective To investigate the effect of massage on quadriceps femoris repair and the expressions of Desmin and α-Actin in rabbits so as to explore the possible molecular mechanisms of massage in repair of muscle injury. Methods Twenty-seven New Zealand white rabbits, weighing (2.0 ± 0.5) kg, were randomly divided into 3 groups: groups A (n=3), B (n=12), and C (n=12). In group A, the rabbits were not treated as controls; in groups B and C, the rabbit models of quadriceps femoris injury were prepared by self-made beater. In group B, no massage therapy was given as nature recovery controls; in group C, RT-N2 intelligent massage device was used for massage therapy at 8 days after injury, at 3 000-3 100 r/min for 15 minutes, every day for 7 days or for 14 days. The quadriceps femoris specimens were taken from 6 rabbits of groups B and C at 14 days and 21 days, respectively. HE staining was employed to detect the histomorphological change. Immunohistochemistry staining and Western blot were used to detect Desmin and α-Actin expressions. The massage therapy effect was evaluated by the histomorphological change and Desmin and α-Actin expressions. Results All rabbits survived to the end of experiment in groups B and C. No histological change was found with regular order of muscle fibers and no connective tissue in group A; obvious tissue necrosis was seen with broken muscular fibers, muscle atrophy, and irregular order in group B; and in group C, the skeletal muscle morphology and muscle atrophy were obviously improved with regenerated muscle fibers when compared with group B. Immunohistochemistry staining showed that the Desmin and α-Actin expressions obviously reduced in groups B and C, which were significantly weaker than that in group A (P lt; 0.05); the Desmin and α-Actin expressions were significantly ber in group C than in group B (P lt; 0.05), and at 21 days than at 14 days in group C (P lt; 0.05). Western blot results showed that the Desmin and α-Actin expressions were significantly higher in group A than in groups B and C (P lt; 0.05), and the expressions were lowest at 14 days in group B. Conclusion The histomorphology and cytoskeletal structure can be significantly improved after massage, which may help to repair muscle injury by up-regulation of Desmin and α-Actin expressions.

    Release date:2016-08-31 04:22 Export PDF Favorites Scan
  • Effect of Dendritic Cells Allergized by K-ras Mutant Peptide on Expressions of CCL19, CCL22, and Fascin-1

    Objective To explore the effect of dendritic cells (DCs) allergized by K-ras mutant peptide on expressions of chemokines CCL19, CCL22, and cytoskeletal protein fascin-1. Methods DCs were derived from peripheral blood in the presence of granuloceyte/macrophage-colony stimulating factor, interleukin (IL) -4 in vitro. The DCs were collected on day 7 after culture, and were divided into non-K-ras mutant peptide group (addition of RPMI 1604 culture solution 50 μg/ml) and K-ras mutant peptide group (addition of K-ras mutant peptide 50 μg/ml). Phenotype was identified by flow cytometry. The morphological structure was observed by scanning and transmission electron microscopies, respectively. The expressions of IL-12, CCL19, and CCL22 were tested continuously by enzyme-linked immunosorbent assay (ELISA). The expression of cytoskeletal protein fascin-1 was determined by Western blot. Results ①The expressions of CD1a, CD80, and CD86 after loading K-ras mutant peptide were higher than that before loading K-ras mutant peptide (Plt;0.01). ②The DCs with petal-like and branch-like profections after loading were observed under scanning electron microscopy; The DCs with irregular shapes, branch-like or burr-like were showed under transmission electron microscopy. ③The expressions of IL-12, CCL19, and CCL22 in the Kras mutant peptide group were higher than those in the non-K-ras mutant peptide group at different times (6, 12, 24, and 48 h) after loading Kras mutant peptide (Plt;0.01). ④The expression of fascin-1 in the K-ras mutant peptide group was also higher than that in the non-K-ras mutant peptide group (Plt;0.01). Conclusion K-ras mutant peptide can promote DC to mature and improve the expression of chemokines and cytoskeletal protein which will strengthen DC migration.

    Release date:2016-09-08 10:55 Export PDF Favorites Scan
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