Identification of Ankrd2, a novel skeletal muscle gene coding for a stretch-responsive ankyrin-repeat protein.

@article{Kemp2000IdentificationOA,
  title={Identification of Ankrd2, a novel skeletal muscle gene coding for a stretch-responsive ankyrin-repeat protein.},
  author={T. Kemp and T. Sadusky and F. Saltisi and N. Carey and J. Moss and S. Y. Yang and D. Sassoon and G. Goldspink and G. Coulton},
  journal={Genomics},
  year={2000},
  volume={66 3},
  pages={
          229-41
        }
}
Mechanically induced hypertrophy of skeletal muscles involves shifts in gene expression leading to increases in the synthesis of specific proteins. Full characterization of the regulation of muscle hypertrophy is a prerequisite for the development of novel therapies aimed at treating muscle wasting (atrophy) in human aging and disease. Using suppression subtractive hybridization, cDNAs corresponding to mRNAs that increase in relative abundance in response to mechanical stretch of mouse skeletal… Expand
Characterization of human skeletal muscle Ankrd2.
TLDR
This paper studied the intracellular localization of the protein and its expression on differentiation using polyclonal and monoclonal antibodies produced to human Ankrd2 and found that in adult skeletal muscle AnkRD2 is found in slow fibers; however, not all of the slow fibers express Ankrd 2 at the same level. Expand
Identification of a novel stretch-responsive skeletal muscle gene (Smpx).
TLDR
A cDNA corresponding to an mRNA that exhibits increased expression in response to 7 days of passive stretch imposed on TA muscles in vivo is identified and it is hypothesized that it plays a role in skeletal muscle hypertrophy. Expand
Expression of Ankrd2 in fast and slow muscles and its response to stretch are consistent with a role in slow muscle function.
TLDR
It is suggested that Ankrd2, which is also a titin binding protein, is a stretch-response gene associated with slow muscle function and that it is part of a separate mechanotransduction system to the one that regulates muscle mass. Expand
Identification of a novel human ankyrin-repeated protein homologous to CARP.
TLDR
Protein sequence analysis revealed that Arpp is homologous (52.7% identity) to Carp which is shown to be involved in the regulation of the transcription of the cardiac ventricular myosin light chain 2 gene. Expand
Characterization of muscle ankyrin repeat proteins in human skeletal muscle.
TLDR
Data are not consistent with the proposal that Ankrd 2, per se, or pAnkrd 2-Ser99 mediates stretch-induced signaling in skeletal muscle, dissociating from titin and translocating to the nucleus, because the majority of these forms of AnkRD 2 are already free in the cytosol. Expand
Arpp, a New Homolog of Carp, Is Preferentially Expressed in Type 1 Skeletal Muscle Fibers and Is Markedly Induced by Denervation
TLDR
Immunohistochemical analysis and sequence analysis revealed that the murine Arpp (mArpp) gene is almost identical to the Ankrd2 gene, which has recently been isolated as a mouse gene induced in stretched skeletal muscle, suggesting that Arpp may function as a nuclear and sarcomeric protein. Expand
Structural and regulatory roles of muscle ankyrin repeat protein family in skeletal muscle.
TLDR
MKO mice showed a greater degree of torque loss after a bout of ECs compared with wild-type mice, although they recovered from the injury with the same or even improved time course, suggesting that the MARP family may play both important structural and gene regulatory roles in skeletal muscle. Expand
Profiling of skeletal muscle Ankrd2 protein in human cardiac tissue and neonatal rat cardiomyocytes
TLDR
The underlying basis for the functional investigation of Ankrd2 in the heart is provided and it is demonstrated that, apart from the sarcomere and nucleus, both proteins are localized to the intercalated disks of human cardiomyocytes. Expand
Identification of Serhl, a new member of the serine hydrolase family induced by passive stretch of skeletal muscle in vivo.
TLDR
Serhl's expression patterns and its response to passive stretch suggest that it may play a role in normal peroxisome function and skeletal muscle growth in response to mechanical stimuli. Expand
Ankrd2 in Mechanotransduction and Oxidative Stress Response in Skeletal Muscle: New Cues for the Pathogenesis of Muscular Laminopathies
TLDR
The main findings on the relationship of Ankrd2 with A-type lamins are reported and known and potential mechanisms involving defective AnkRD2-lamin A interplay in the pathogenesis of muscular laminopathies are discussed. Expand
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