Literature DB >> 23424163

Loss of SPARC in mouse skeletal muscle causes myofiber atrophy.

Katsuyuki Nakamura1, Shin-Ichi Nakano, Takahiro Miyoshi, Keitaro Yamanouchi, Masugi Nishihara.   

Abstract

INTRODUCTION: The expression of secreted protein acidic and rich in cysteine (SPARC) in skeletal muscle decreases with age. Here, we examined the role of SPARC in skeletal muscle by reducing its expression.
METHODS: SPARC expression was suppressed by introducing short interfering RNA (siRNA) into mouse tibialis anterior muscle. Myofiber diameter, atrogin1, and muscle RING-finger protein 1 (MuRF1) expression, and tumor necrosis factor-α (TNFα) and transforming growth factor-β (TGFβ) signaling were then analyzed.
RESULTS: Reduced SPARC expression caused decreases in the diameter of myofibers, especially fast-type ones, accompanied by upregulation of atrogin1, but not MuRF1, at 10 days after siRNA transfection. The expression of TNFα and TGFβ and the phosphorylation status of p38 were not affected by SPARC knockdown, whereas Smad3 phosphorylation was increased at 2 days after siRNA transfection.
CONCLUSIONS: The loss of SPARC not only upregulates atrogin1 expression but also enhances TGFβ signaling, which may in turn cause muscle atrophy.
Copyright © 2013 Wiley Periodicals, Inc.

Entities:  

Keywords:  SPARC; Smad3; TGFβ; atrogin1; myofiber atrophy

Mesh:

Substances:

Year:  2013        PMID: 23424163     DOI: 10.1002/mus.23822

Source DB:  PubMed          Journal:  Muscle Nerve        ISSN: 0148-639X            Impact factor:   3.217


  14 in total

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10.  Reduced fibrillar collagen accumulation in skeletal muscle of secreted protein acidic and rich in cysteine (SPARC)-null mice.

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