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Identification and Characterization of Homocysteine Responsive Endoplasmic Reticulum Resident Ubiquitin‐like Domain Member 2 (Herpud2) in Skeletal Muscle
Author(s) -
Arcaro Alexandra,
Hewitt Lillian,
Waddell David
Publication year - 2019
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2019.33.1_supplement.700.21
Subject(s) - endoplasmic reticulum , myogenesis , muscle atrophy , biology , denervation , protein degradation , skeletal muscle , myocyte , endoplasmic reticulum associated protein degradation , microbiology and biotechnology , ubiquitin , atrophy , endocrinology , gene , unfolded protein response , biochemistry , genetics
Skeletal muscle atrophy is a physiological condition that is caused by disparate conditions, including immobilization, denervation, spinal cord injury and corticosteroids and results in decreased muscle size and strength. To better characterize the molecular genetic events of neurogenic atrophy, a previous study isolated gastrocnemius muscle from mice following 3 days and 14 days of sciatic nerve denervation. The gene expression profile in the denervated muscle tissue was then analyzed by microarray and compared to control muscle tissue to identify novel neurogenic atrophy‐induced genes. The microarray data revealed for the first time that Homocysteine Responsive Endoplasmic Reticulum Resident Ubiquitin‐like Domain Member 2 (Herpud2) is expressed in skeletal muscle and is differentially regulated in response to denervation. Herpud2 is related to Herpud1, which has previously been shown to play a role in endoplasmic reticulum‐associated degradation (ERAD) of unfolded ER proteins via retrotranslocation to the cytoplasm and degradation by ubiquitin‐proteasome system. To confirm that Herpud2 is expressed in muscle cells, we cloned the Herpud2 cDNA from cultured cells and performed quantitative PCR (qPCR) to assess Herpud2 expression levels in both proliferating and differentiated muscle cells and the results demonstrate that Herpud2 expression levels are lower in proliferating myoblasts compared to differentiated myotubes. Furthermore, Western blot analysis confirmed that Herpud2 is expressed in cultured muscle cells at the protein level. The discovery that Herpud2 is differentially expressed in response to neurogenic atrophy helps further our understanding of the molecular genetic events of muscle wasting and may eventually lead to the identification of new therapeutic targets for the treatment and prevention of atrophy. Support or Funding Information The work was support by University of North Florida Transformational Learning Opportunity grants and a University of North Florida Foundation Board Grant to D.W. This abstract is from the Experimental Biology 2019 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .