Phenotypes of myopathy-related beta-tropomyosin mutants in human and mouse tissue cultures

Mutations in TPM2 result in a variety of myopathies characterised by variable clinical and morphological features. We used human and mouse cultured cells to study the effects of β-TM mutants. The mutants induced a range of phenotypes in human myoblasts, which generally changed upon differentiation t...

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Published in:PloS one 2013-09, Vol.8 (9), p.e72396
Main Authors: Abdul-Hussein, Saba, Rahl, Karin, Moslemi, Ali-Reza, Tajsharghi, Homa
Format: Article
Language:English
Subjects:
ACTIN CYTOSKELETON
Adaptor Proteins, Signal Transducing - metabolism
Amino acids
Animals
CAP DISEASE
Cell culture
Cells (Biology)
Cells, Cultured
Clinical Medicine
Cloning
Combinatorial analysis
COMPOSITION
Congenital diseases
CONGENITAL MYOPATHY
Cytomegalovirus
Cytoskeleton - metabolism
DISTAL ARTHROGRYPOSIS
Filaments
Gene Expression
GENE TPM2
Genes
Genetic aspects
Genetic Association Studies
Green Fluorescent Proteins - biosynthesis
Humans
IMMUNOELECTRON
ISOFORM
Klinisk medicin
Medical sciences
Medicin
Mice
MICROSCOPY
Morphology
Muscle contraction
Muscle Fibers, Skeletal - metabolism
Muscle Fibers, Skeletal - pathology
Muscle proteins
Muscles
Muscular Diseases - genetics
Muscular Diseases - pathology
Musculoskeletal system
Mutagenesis
Mutants
Mutation
Myoblasts
Myoblasts - metabolism
Myoblasts - pathology
Myopathy
Myotubes
NEMALINE MYOPATHY
Pathology
Phenotype
Phenotypes
Proteins
RARE CAUSE
Sarcomeres - metabolism
Sequestosome-1 Protein
SKELETAL-MUSCLE
Studies
Tissue culture
Tissue Culture Techniques
Tropomyosin
Tropomyosin - genetics
Tropomyosin - metabolism
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creator Abdul-Hussein, Saba
Rahl, Karin
Moslemi, Ali-Reza
Tajsharghi, Homa
description Mutations in TPM2 result in a variety of myopathies characterised by variable clinical and morphological features. We used human and mouse cultured cells to study the effects of β-TM mutants. The mutants induced a range of phenotypes in human myoblasts, which generally changed upon differentiation to myotubes. Human myotubes transfected with the E41K-β-TM(EGFP) mutant showed perinuclear aggregates. The G53ins-β-TM(EGFP) mutant tended to accumulate in myoblasts but was incorporated into filamentous structures of myotubes. The K49del-β-TM(EGFP) and E122K-β-TM(EGFP) mutants induced the formation of rod-like structures in human cells. The N202K-β-TM(EGFP) mutant failed to integrate into thin filaments and formed accumulations in myotubes. The accumulation of mutant β-TM(EGFP) in the perinuclear and peripheral areas of the cells was the striking feature in C2C12. We demonstrated that human tissue culture is a suitable system for studying the early stages of altered myofibrilogenesis and morphological changes linked to myopathy-related β-TM mutants. In addition, the histopathological phenotype associated with expression of the various mutant proteins depends on the cell type and varies with the maturation of the muscle cell. Further, the phenotype is a combinatorial effect of the specific amino acid change and the temporal expression of the mutant protein.
doi_str_mv 10.1371/journal.pone.0072396
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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>SWEPUB Högskolan i Skövde full text</collection><collection>SwePub</collection><collection>SwePub Articles</collection><collection>SWEPUB Freely available online</collection><collection>SWEPUB Högskolan i Skövde</collection><collection>SwePub Articles full text</collection><collection>SWEPUB Göteborgs universitet</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PloS one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Abdul-Hussein, Saba</au><au>Rahl, Karin</au><au>Moslemi, Ali-Reza</au><au>Tajsharghi, Homa</au><au>Palau, Francesc</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Phenotypes of myopathy-related beta-tropomyosin mutants in human and mouse tissue cultures</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2013-09-10</date><risdate>2013</risdate><volume>8</volume><issue>9</issue><spage>e72396</spage><pages>e72396-</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>Mutations in TPM2 result in a variety of myopathies characterised by variable clinical and morphological features. We used human and mouse cultured cells to study the effects of β-TM mutants. The mutants induced a range of phenotypes in human myoblasts, which generally changed upon differentiation to myotubes. Human myotubes transfected with the E41K-β-TM(EGFP) mutant showed perinuclear aggregates. The G53ins-β-TM(EGFP) mutant tended to accumulate in myoblasts but was incorporated into filamentous structures of myotubes. The K49del-β-TM(EGFP) and E122K-β-TM(EGFP) mutants induced the formation of rod-like structures in human cells. The N202K-β-TM(EGFP) mutant failed to integrate into thin filaments and formed accumulations in myotubes. The accumulation of mutant β-TM(EGFP) in the perinuclear and peripheral areas of the cells was the striking feature in C2C12. We demonstrated that human tissue culture is a suitable system for studying the early stages of altered myofibrilogenesis and morphological changes linked to myopathy-related β-TM mutants. In addition, the histopathological phenotype associated with expression of the various mutant proteins depends on the cell type and varies with the maturation of the muscle cell. Further, the phenotype is a combinatorial effect of the specific amino acid change and the temporal expression of the mutant protein.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>24039757</pmid><doi>10.1371/journal.pone.0072396</doi><tpages>e72396</tpages><oa>free_for_read</oa></addata></record>
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identifier ISSN: 1932-6203
ispartof PloS one, 2013-09, Vol.8 (9), p.e72396
issn 1932-6203
1932-6203
language eng
recordid cdi_plos_journals_1431404686
source Publicly Available Content Database (Proquest) (PQ_SDU_P3); PubMed Central (Open access)
subjects ACTIN CYTOSKELETON
Adaptor Proteins, Signal Transducing - metabolism
Amino acids
Animals
CAP DISEASE
Cell culture
Cells (Biology)
Cells, Cultured
Clinical Medicine
Cloning
Combinatorial analysis
COMPOSITION
Congenital diseases
CONGENITAL MYOPATHY
Cytomegalovirus
Cytoskeleton - metabolism
DISTAL ARTHROGRYPOSIS
Filaments
Gene Expression
GENE TPM2
Genes
Genetic aspects
Genetic Association Studies
Green Fluorescent Proteins - biosynthesis
Humans
IMMUNOELECTRON
ISOFORM
Klinisk medicin
Medical sciences
Medicin
Mice
MICROSCOPY
Morphology
Muscle contraction
Muscle Fibers, Skeletal - metabolism
Muscle Fibers, Skeletal - pathology
Muscle proteins
Muscles
Muscular Diseases - genetics
Muscular Diseases - pathology
Musculoskeletal system
Mutagenesis
Mutants
Mutation
Myoblasts
Myoblasts - metabolism
Myoblasts - pathology
Myopathy
Myotubes
NEMALINE MYOPATHY
Pathology
Phenotype
Phenotypes
Proteins
RARE CAUSE
Sarcomeres - metabolism
Sequestosome-1 Protein
SKELETAL-MUSCLE
Studies
Tissue culture
Tissue Culture Techniques
Tropomyosin
Tropomyosin - genetics
Tropomyosin - metabolism
title Phenotypes of myopathy-related beta-tropomyosin mutants in human and mouse tissue cultures
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