title: Constitutive upregulations of titin-based signalling proteins in KY deficient muscles.
abstract: An increase in the expression of stretch/stress response elements in fast and slow muscles has been previously described in a transcriptional profiling of KY deficient muscles. Here, we have characterized the induction of this titin-based family of signalling proteins in ky/ky muscles at the protein level. Changes in expression of MLP, MARP2 and Xin have been related to the onset of dystrophic and adaptive changes that operate in ky/ky muscles. Our results indicate that induction of this set of genes is an early consequence of the interference caused by the absence of the KY protein. A search of muscle profiles of mouse models revealed such molecular hallmark only in muscles subjected to a single bout of eccentric contractions and specific titin mutants. Based on the role of this family as titin-based stress response molecules, it is suggested that titin structural/signalling instability is common to ky and titin mouse mutants and eccentric contractions.
authors.affiliation: MRC Mammalian Genetics Unit, Harwell OX11 0RD, UK.
authors.forename: Jane
authors.initials: J
authors.lastname: Beatham
authors.forename: Katja
authors.initials: K
authors.lastname: Gehmlich
authors.forename: Peter F M
authors.initials: PF
authors.lastname: van der Ven
authors.forename: Jaakko
authors.initials: J
authors.lastname: Sarparanta
authors.forename: Debbie
authors.initials: D
authors.lastname: Williams
authors.forename: Peter
authors.initials: P
authors.lastname: Underhill
authors.forename: Christian
authors.initials: C
authors.lastname: Geier
authors.forename: Dieter O
authors.initials: DO
authors.lastname: Fürst
authors.forename: Bjarne
authors.initials: B
authors.lastname: Udd
authors.forename: Gonzalo
authors.initials: G
authors.lastname: Blanco
mesh_terms: D000222:Adaptation, Physiological / Q000502:physiology; D000818:Animals; D064211:Connectin; D004268:DNA-Binding Proteins / Q000235:genetics / Q000378:metabolism; D060588:LIM Domain Proteins; D051379:Mice; D008817:Mice, Mutant Strains; D009124:Muscle Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D018482:Muscle, Skeletal / Q000378:metabolism; D009137:Muscular Dystrophy, Animal / Q000235:genetics* / Q000378:metabolism*; D009687:Nuclear Proteins / Q000235:genetics / Q000378:metabolism; D020411:Oligonucleotide Array Sequence Analysis; D010447:Peptide Hydrolases; D011494:Protein Kinases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D017434:Protein Structure, Tertiary; D015398:Signal Transduction / Q000502:physiology*; D014158:Transcription, Genetic / Q000502:physiology; D015854:Up-Regulation
chemical_list: D064211:Connectin; D004268:DNA-Binding Proteins; D060588:LIM Domain Proteins; D009124:Muscle Proteins; D009687:Nuclear Proteins; C118478:Xin protein, mouse; C090114:cysteine and glycine-rich protein 3; D011494:Protein Kinases; C506764:KY protein, mouse; D010447:Peptide Hydrolases