title: Co- and post-transcriptional regulation of Rbm5 and Rbm10 in mouse cells as evidenced by tissue-specific, developmental and disease-associated variation of splice variant and protein expression levels.
abstract: BACKGROUND
  Expression and function of the two RNA binding proteins and regulators of alternative splicing, RBM5 and RBM10, have largely been studied in human tissue and cell lines. The objective of the study described herein was to examine their expression in mouse tissue, in order to lay the framework for comprehensive functional studies using mouse models.
  
  
  METHODS
  All RNA variants of Rbm5 and Rbm10 were examined in a range of normal primary mouse tissues. RNA and protein were examined in differentiating C2C12 myoblasts and in denervated and dystonin-deficient mouse skeletal muscle.
  
  
  RESULTS
  All Rbm5 and Rbm10 variants examined were expressed in all mouse tissues and cell lines. In general, Rbm5 and Rbm10 RNA expression was higher in brain than in skin. RNA expression levels were more varied between cardiac and skeletal muscle, depending on the splice variant: for instance, Rbm10v1 RNA was higher in skeletal than cardiac muscle, whereas Rbm10v3 RNA was higher in cardiac than skeletal muscle. In mouse brain, cardiac and skeletal muscle, RNA encoding an approximately 17kDa potential paralogue of a small human RBM10 isoform was detected, and the protein observed in myoblasts and myotubes. Expression of Rbm5 and Rbm10 RNA remained constant during C2C12 myogenesis, but protein levels significantly decreased. In two muscle disease models, neither Rbm10 nor Rbm5 showed significant transcriptional changes, although significant specific alternative splicing changes of Rbm5 pre-mRNA were observed. Increased RBM10 protein levels were observed following denervation.
  
  
  CONCLUSIONS
  The varied co-transcriptional and post-transcriptional regulation aspects of Rbm5 and Rbm10 expression associated with mouse tissues, myogenesis and muscle disease states suggest that a mouse model would be an interesting and useful model in which to study comprehensive functional aspects of RBM5 and RBM10.
authors.affiliation: School of Life Science, University of Skovde, 541 28 Skovde, Sweden.
authors.forename: Bartholomew
authors.initials: B
authors.lastname: Ozuemba
authors.affiliation: Biomolecular Sciences Program, Laurentian University, 935 Ramsey Lake Road, Sudbury, ON, P3E 2C6, Canada.
authors.forename: Twinkle J
authors.initials: TJ
authors.lastname: Masilamani
authors.affiliation: Biomolecular Sciences Program, Laurentian University, 935 Ramsey Lake Road, Sudbury, ON, P3E 2C6, Canada.
authors.forename: Julie J
authors.initials: JJ
authors.lastname: Loiselle
authors.affiliation: AMRIC, Health Sciences North, 41 Ramsey Lake Road, Sudbury, ON, P3E 5J1, Canada.
authors.forename: Benjamin
authors.initials: B
authors.lastname: Koenderink
authors.affiliation: School of Human Kinetics, Laurentian University, 935 Ramsey Lake Road, Sudbury, ON, P3E 2C6, Canada.
authors.forename: Kaitlin A
authors.initials: KA
authors.lastname: Vanderbeck
authors.affiliation: AMRIC, Health Sciences North, 41 Ramsey Lake Road, Sudbury, ON, P3E 5J1, Canada.
authors.forename: Jose
authors.initials: J
authors.lastname: Knee
authors.affiliation: Biomolecular Sciences Program, Laurentian University, 935 Ramsey Lake Road, Sudbury, ON, P3E 2C6, Canada; School of Human Kinetics, Laurentian University, 935 Ramsey Lake Road, Sudbury, ON, P3E 2C6, Canada.
authors.forename: Céline
authors.initials: C
authors.lastname: Larivière
authors.affiliation: Biomolecular Sciences Program, Laurentian University, 935 Ramsey Lake Road, Sudbury, ON, P3E 2C6, Canada; AMRIC, Health Sciences North, 41 Ramsey Lake Road, Sudbury, ON, P3E 5J1, Canada; Division of Medical Sciences, Northern Ontario School of Medicine, Laurentian University, 935 Ramsey Lake Road, Sudbury, ON, P3E 2C6, Canada; Department of Chemistry and Biochemistry, Laurentian University, 935 Ramsey Lake Road, Sudbury, ON, P3E 2C6, Canada; Department of Medicine, Division of Medical Oncology, University of Ottawa, Ottawa, ON, Canada. Electronic address: lsutherland@amric.ca.
authors.forename: Leslie C
authors.initials: LC
authors.lastname: Sutherland
mesh_terms: D017398:Alternative Splicing / Q000235:genetics*; D000818:Animals; D002352:Carrier Proteins / Q000235:genetics; D002460:Cell Line; D003598:Cytoskeletal Proteins / Q000235:genetics; D000071821:Dystonin; D015870:Gene Expression / Q000235:genetics; D005786:Gene Expression Regulation / Q000235:genetics*; D051379:Mice; D024510:Muscle Development / Q000235:genetics; D018482:Muscle, Skeletal / Q000378:metabolism; D032383:Myocytes, Cardiac / Q000378:metabolism; D009419:Nerve Tissue Proteins / Q000235:genetics; D016133:Polymerase Chain Reaction; D020033:Protein Isoforms / Q000096:biosynthesis / Q000235:genetics*; D016601:RNA-Binding Proteins / Q000096:biosynthesis / Q000235:genetics*; D051381:Rats; D014158:Transcription, Genetic / Q000235:genetics
chemical_list: D002352:Carrier Proteins; D003598:Cytoskeletal Proteins; C095667:Dst protein, mouse; D000071821:Dystonin; D009419:Nerve Tissue Proteins; D020033:Protein Isoforms; C531317:RBM10 protein, mouse; C585457:RBM5 protein, mouse; D016601:RNA-Binding Proteins
keywords: C2C12; Denervation; Gene expression; Mouse; Primary tissue; RBM10; RBM5