Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UMLS:C0026850 (muscular dystrophy)
 5,870 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In order to understand the mechanism of defective myofibrilogenesis in muscular dystrophy, we have used the genomic cloned DNA specific for myosin light chain 2A (MLC 2A) to check its expression. The fusion of a partial digest of lambda LC5, containing the upstream sequence of MLC 2A gene with the expression vector of PSVOCAT has already been reported. Using this CAT-fused recombinant containing 1.6 kb of MLC 2A gene, we were able to detect the promoter activity in normal heart cells, H9C2 cell line whereas a restricted expression of MLC 2A gene was noticed in muscular dystrophic muscle cells from heart and skeletal. We have also measured the transient transfection efficiency by contransfecting with the plasmid LacZ. Simultaneous assay of beta-galactosidase and CAT in the cell extract was performed. With beta-galactosidase as control, we confirmed that the promoter activity of MLC 2A gene is inhibited in muscular dystrophy though there is a normal rate of transfection occurred.
 ...
PMID:Restricted expression of cardiac myosin light chain 2A gene in muscular dystrophic condition. 190 50

We examined serum cardiac myosin light chain I (LCI), serum creatine kinase (CK) levels and left ventricular function in patients with muscular dystrophy and secondary cardiac involvement. LCI levels were determined by a two-site immunoradiometric assay method in 25 patients with muscular dystrophy and 10 normal subjects. This study included 15 patients with Duchenne muscular dystrophy (DMD), 8 patients with Fukuyama type congenital muscular dystrophy (FCMD) and 2 sisters with non-Fukuyama type congenital muscular dystrophy (nFCMD). We measured the value of left ventricular fractional shortening (FS) using echocardiography. All patients with DMD and FCMD showed moderate or severe skeletal muscle weakness. The mean values of LCI were significantly higher in patients with DMD (11.0 +/- 8.3 ng/ml, p less than 0.01) and in patients with FCMD (1.6 +/- 1.4 ng/ml, p less than 0.05) than in normal subjects (0.3 +/- 0.2 ng/ml). In patients with DMD, LCI level correlated closely with CK level (r = 0.81, p less than 0.01) but not with FS (r = 0.35, n.s.). In patients with FCMD, LCI level correlated significantly with CK level (r = 0.75, p less than 0.05) but not with FS (r = 0.44, n.s.). Close correlation between LCI and CK levels was thought to result from the cross reaction between cardiac LCI and myosin light chains of skeletal muscle in the assay method we used. Two siblings with nFCMD showed mild skeletal muscle weakness. A 22-year-old sister with mild left ventricular dysfunction (FS = 0.41) showed high level of CK (4794/U/L) and mild elevation of LCI (7.3 ngml).(ABSTRACT TRUNCATED AT 250 WORDS)
 ...
PMID:[Clinical significance of serum cardiac myosin light chain I in patients with muscular dystrophy]. 225 17

Backcross and F2 analyses have been carried out to determine the genetic basis of inheritance of three myosin light chain-1 variants present in the fast white muscle fibers of the domestic chicken. Two of the variants (types I and II) were described previously [Rushbrook, J. I., Yuan, A. I., and Stracher, A. (1982). Muscle Nerve 5:505], while the existence of the third (type III) is reported here. The results are consistent with an autosomal and allelic origin for the variants. A test linkage backcross to the muscular dystrophy gene am was found to be negative. This is the twelfth negative linkage result for the am gene.
 ...
PMID:Myosin light chain-1: genetic analysis of three variants found in fast white chicken muscle and investigation of linkage with the muscular dystrophy gene. 399 57

Evidence is presented from electrophoresis and peptide-mapping for the existence of two major allelic forms of myosin light chain-1 in the fast white muscle fibers of domestic chickens. One form predominates in birds of White Leghorn stock, the other in birds of New Hampshire Red stock. The two light chain-1 forms were invariant during development. Variability was not detected in light chains-2 or -3. The distribution of the two forms in two strains homozygous for the am gene for muscular dystrophy--Connecticut dystrophic and line 413--and their controls, White Leghorn and line 412, respectively, while clearly unrelated to avian dystrophy, emphasizes the heterogeneity in background genes of these non-inbred lines and indicates caution in their use in studies of avian dystrophy.
 ...
PMID:Two major allelic forms of myosin light chain-1 in strains of normal and dystrophic chickens. 714 7

Knowledge regarding cellular fusion and nuclear reprogramming may aid in cell therapy strategies for skeletal muscle diseases. An issue with cell therapy approaches to restore dystrophin expression in muscular dystrophy is obtaining a sufficient quantity of cells that normally fuse with muscle. Here we conferred fusogenic activity without transdifferentiation to multiple non-muscle cell types and tested dystrophin restoration in mouse models of muscular dystrophy. We previously demonstrated that myomaker, a skeletal muscle-specific transmembrane protein necessary for myoblast fusion, is sufficient to fuse 10T 1/2 fibroblasts to myoblasts in vitro. Whether myomaker-mediated heterologous fusion is functional in vivo and whether the newly introduced nonmuscle nuclei undergoes nuclear reprogramming has not been investigated. We showed that mesenchymal stromal cells, cortical bone stem cells, and tail-tip fibroblasts fuse to skeletal muscle when they express myomaker. These cells restored dystrophin expression in a fraction of dystrophin-deficient myotubes after fusion in vitro. However, dystrophin restoration was not detected in vivo although nuclear reprogramming of the muscle-specific myosin light chain promoter did occur. Despite the lack of detectable dystrophin reprogramming by immunostaining, this study indicated that myomaker could be used in nonmuscle cells to induce fusion with muscle in vivo, thereby providing a platform to deliver therapeutic material.-Mitani, Y., Vagnozzi, R. J., Millay, D. P. In vivo myomaker-mediated heterologous fusion and nuclear reprogramming.
 ...
PMID:In vivo myomaker-mediated heterologous fusion and nuclear reprogramming. 2782 7