Electrophoretic analysis of myosin heavy chain isoform patterns in extraocular muscles of the rat

Asmussen, G; Traub, Irmtrud; Pette, Dirk

doi:10.1016/0014-5793(93)80738-g

Cited by 28 publications

(21 citation statements)

References 16 publications

(6 reference statements)

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“…Even though EOM contains a large number of slow muscle fibers, it is still considered one of the fastest muscles in the vertebrate body (15). One-dimensional electrophoresis previously showed that in EDL, a fast isoform (MYH4) accounted for ϳ45% of all MYH, whereas in EOM fast MYH (MYH4 and MYH13) accounts for 75% (13,18,38). Considering the higher amount of fast MYH in EOM, the elevated expression level of SLIM in EOM correlates well.…”

Section: Table II Proteomics Profile Of Extraocular Muscle Versus Extmentioning

confidence: 91%

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Quantitative Proteomics Profiling of Sarcomere Associated Proteins in Limb and Extraocular Muscle Allotypes

Fraterman

Zeiger

Khurana

et al. 2007

Molecular & Cellular Proteomics

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The sarcomere is the major structural and functional unit of striated muscle. Approximately 65 different proteins have been associated with the sarcomere, and their exact composition defines the speed, endurance, and biology of each individual muscle. Past analyses relied heavily on electrophoretic and immunohistochemical techniques, which only allow the analysis of a small fraction of proteins at a time. Here we introduce a quantitative labelfree, shotgun proteomics approach to differentially quantitate sarcomeric proteins from microgram quantities of muscle tissue in a fast and reliable manner by liquid chromatography and mass spectrometry. The high sequence similarity of some sarcomeric proteins poses a problem for shotgun proteomics because of limitations in subsequent database search algorithms in the exclusive assignment of peptides to specific isoforms. Therefore multiple sequence alignments were generated to improve the identification of isoform specific peptides. This methodology was used to compare the sarcomeric proteome of the extraocular muscle allotype to limb muscle. Extraocular muscles are a unique group of highly specialized muscles with distinct biochemical, physiological, and pathological properties. We were able to quantitate 40 sarcomeric proteins; although the basic sarcomeric proteins in extraocular muscle are similar to those in limb muscle, key proteins stabilizing the connection of the Z-bands to thin filaments and the costamere are augmented in extraocular muscle and may represent an adaptation to the eccentric contractions known to normally occur during eye movements. Furthermore, a number of changes are seen that closely relate to the unique nature of extraocular muscle. Molecular & Cellular Proteomics 6:728 -737, 2007.

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Section: Table II Proteomics Profile Of Extraocular Muscle Versus Extmentioning

confidence: 91%

“…Previous one-dimensional gel electrophoresis approaches failed to resolve all MYH present in EOM because of their close mass range (13,14), and most data concerning protein abundance were gained by immunohistochemistry (12).…”

Section: Table I Correlation With Microarray Datamentioning

confidence: 99%

Quantitative Proteomics Profiling of Sarcomere Associated Proteins in Limb and Extraocular Muscle Allotypes

Fraterman

Zeiger

Khurana

et al. 2007

Molecular & Cellular Proteomics

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“…2) as previously described (1). Because MyHC-IIa is the main MyHC isoform in type 2A fibers (9), and MyHC-IIa is a major constituent of extraocular muscles (13), which were involved in all affected family members, the MyHC-IIa was regarded a very strong candidate gene for the disease.…”

Section: Resultsmentioning

confidence: 99%

“…Accordingly, mutations in ␤ cardiac͞slow MyHC have been reported to affect slow, type 1, muscle fiber structure and function (5,6). (vi) External ophthalmoplegia is compatible with a pathogenic mutation affecting IIa MyHC because this is a major isoform of myosin in extraocular muscle (13). (vii) Targeted disruption of fast MyHC genes in mice causes myopathy with muscle weakness and disorganization of myofilaments (18), and point mutations in MyHC genes cause muscle dysfunction in Drosophila, Caenorhabditis elegans, and Dictyostelium (16).…”

Section: Discussionmentioning

confidence: 99%

Autosomal dominant myopathy: Missense mutation (Glu-706 → Lys) in the myosin heavy chain IIa gene

Martinsson

Oldfors

Darín

et al. 2000

Proc. Natl. Acad. Sci. U.S.A.

138

102

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We here report on a human myopathy associated with a mutation in a fast myosin heavy chain (MyHC) gene, and also the genetic defect in a hereditary inclusion body myopathy. The disorder has previously been described in a family with an ''autosomal dominant myopathy, with joint contractures, ophthalmoplegia, and rimmed vacuoles.'' Linkage analysis and radiation hybrid mapping showed that the gene locus (Human Genome Map locus name: IBM3) is situated in a 2-Mb region of chromosome 17p13, where also a cluster of MyHC genes is located. These include the genes encoding embryonic, IIa, IIx͞d, IIb, perinatal, and extraocular MyHCs. Morphological analysis of muscle biopsies from patients from the family indicated to us that the type 2A fibers frequently were abnormal, whereas other fiber types appeared normal. This observation prompted us to investigate the MyHC-IIa gene, since MyHC-IIa is the major isoform in type 2A fibers. The complete genomic sequence for this gene was deduced by using an ''in silico'' strategy. The gene, found to consist of 38 exons, was subjected to a complete mutation scan in patients and controls. We identified a missense mutation, Glu-706 3 Lys, which is located in a highly conserved region of the motor domain, the so-called SH1 helix region. By conformational changes this region communicates activity at the nucleotide-binding site to the neck region, resulting in the lever arm swing. The mutation in this region is likely to result in a dysfunctional myosin, compatible with the disorder in the family.

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“…MHCir displayed a lower mobility than MHC,,, (Fig. 2, lane 3), an isoform previously identified by SDS-PAGE in extraocular muscles of rabbit [21] and rat [22].…”

Section: Electrophoretic Analysesmentioning

confidence: 99%

Electrophoretically defined myosin heavy chain patterns of single human muscle spindles

et al. 1993

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At least four myosin heavy chain (MHC) isoforms were separated by SDS-PAGE in extracts of intrafusal fibers isolated by microdissection from human lumbrical muscles. The fastest migrating MHC represents a slow isoform. The slowest migrating MHC was identified as the embryonic MHC,,. A faint band, moving slightly faster than MHC,,,, most likely represents a neonatal/fetal MHC isoform. A prominent band, moving between the latter and the slow isoform is suggested to represent a hitherto unidentified, spindle-specific MHC isoform, MHC,, Human muscle; Intrafusal fiber; Muscle spindle; Myosin heavy chain isoform; Single fiber study

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Electrophoretic analysis of myosin heavy chain isoform patterns in extraocular muscles of the rat

Cited by 28 publications

References 16 publications

Quantitative Proteomics Profiling of Sarcomere Associated Proteins in Limb and Extraocular Muscle Allotypes

Quantitative Proteomics Profiling of Sarcomere Associated Proteins in Limb and Extraocular Muscle Allotypes

Autosomal dominant myopathy: Missense mutation (Glu-706 → Lys) in the myosin heavy chain IIa gene

Electrophoretically defined myosin heavy chain patterns of single human muscle spindles

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