Down-regulation of genes in the lysosomal and ubiquitin-proteasome proteolytic pathways in calpain-3-deficient muscle.

[1]  A. Goldberg,et al.  Patterns of gene expression in atrophying skeletal muscles: response to food deprivation , 2002, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[2]  S. Wing,et al.  Ubiquitin-conjugating enzyme E214k/HR6B is dispensable for increased protein catabolism in muscle of fasted mice. , 2002, American journal of physiology. Endocrinology and metabolism.

[3]  J. Madelmont,et al.  Chemotherapy inhibits skeletal muscle ubiquitin-proteasome-dependent proteolysis. , 2002, Cancer research.

[4]  Keiji Tanaka,et al.  Torbafylline (HWA 448) inhibits enhanced skeletal muscle ubiquitin-proteasome-dependent proteolysis in cancer and septic rats. , 2002, The Biochemical journal.

[5]  D. Attaix,et al.  Identification of cathepsin L as a differentially expressed message associated with skeletal muscle wasting. , 2001, The Biochemical journal.

[6]  J. Beckmann,et al.  Pathophysiology of limb girdle muscular dystrophy type 2A: hypothesis and new insights into the IκBα/NF-κB survival pathway in skeletal muscle , 2001, Journal of Molecular Medicine.

[7]  A. Goldberg,et al.  What do we really know about the ubiquitin-proteasome pathway in muscle atrophy? , 2001, Current opinion in clinical nutrition and metabolic care.

[8]  A. Ciechanover,et al.  Mechanisms of ubiquitin-mediated, limited processingof the NF-κB1 precursor protein p105 , 2001 .

[9]  J. Beckmann,et al.  Loss of Calpain 3 Proteolytic Activity Leads to Muscular Dystrophy and to Apoptosis-Associated Iκbα/Nuclear Factor κb Pathway Perturbation in Mice , 2000, The Journal of cell biology.

[10]  A. Goldberg,et al.  Ubiquitin conjugation by the N-end rule pathway and mRNAs for its components increase in muscles of diabetic rats. , 1999, The Journal of clinical investigation.

[11]  J. Fischer,et al.  Sepsis stimulates release of myofilaments in skeletal muscle by a calcium‐dependent mechanism , 1999, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[12]  J. Beckmann,et al.  Calpain 3 deficiency is associated with myonuclear apoptosis and profound perturbation of the IκBα/NF-κB pathway in limb-girdle muscular dystrophy type 2A , 1999, Nature Medicine.

[13]  N. Forsberg,et al.  Role of calpain in skeletal-muscle protein degradation. , 1998, Proceedings of the National Academy of Sciences of the United States of America.

[14]  D. Taillandier,et al.  The Critical Role of the Ubiquitin-Proteasome Pathway in Muscle Wasting in Comparison to Lysosomal and Ca2+-Dependent Systems , 1998 .

[15]  G. Tiao,et al.  Sepsis-induced increase in muscle proteolysis is blocked by specific proteasome inhibitors. , 1998, The American journal of physiology.

[16]  K. Suzuki,et al.  Structure and physiological function of calpains. , 1997, The Biochemical journal.

[17]  C. Pickart.  Targeting of substrates to the 26S proteasome , 1997, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[18]  J. Beckmann,et al.  Chromosome 15-linked limb-girdle muscular dystrophy: Clinical phenotypes in Reunion Island and French metropolitan communities , 1996, Neuromuscular Disorders.

[19]  M. Glickman,et al.  The multiubiquitin-chain-binding protein Mcb1 is a component of the 26S proteasome in Saccharomyces cerevisiae and plays a nonessential, substrate-specific role in protein turnover , 1996, Molecular and cellular biology.

[20]  D. Balcerzak,et al.  Evidence for implication of muscle-specific calpain (p94) in myofibrillar integrity. , 1996, Cell growth & differentiation : the molecular biology journal of the American Association for Cancer Research.

[21]  S. E. Samuels,et al.  No alteration in gene expression of components of the ubiquitin proteasome proteolytic pathway in dystrophin‐deficient muscles , 1996, FEBS letters.

[22]  C. Guézennec,et al.  Coordinate activation of lysosomal, Ca 2+-activated and ATP-ubiquitin-dependent proteinases in the unweighted rat soleus muscle. , 1996, The Biochemical journal.

[23]  B. Beaufrère,et al.  Increased mRNA levels for components of the lysosomal, Ca2+-activated, and ATP-ubiquitin-dependent proteolytic pathways in skeletal muscle from head trauma patients. , 1996, Proceedings of the National Academy of Sciences of the United States of America.

[24]  D. Breuillé,et al.  Muscle wasting in a rat model of long-lasting sepsis results from the activation of lysosomal, Ca2+ -activated, and ubiquitin-proteasome proteolytic pathways. , 1996, The Journal of clinical investigation.

[25]  R. Mason.  Lysosomal metabolism of proteins. , 1996, Sub-cellular biochemistry.

[26]  S. Kashiwagi,et al.  Lysosomal enzyme activities in skeletal muscle of patients with neuromuscular diseases , 1995, Muscle & nerve.

[27]  A. Goldberg,et al.  Activation of the ATP-ubiquitin-proteasome pathway in skeletal muscle of cachectic rats bearing a hepatoma. , 1995, The American journal of physiology.

[28]  Isabelle Richard,et al.  Mutations in the proteolytic enzyme calpain 3 cause limb-girdle muscular dystrophy type 2A , 1995, Cell.

[29]  K. Campbell.  Three muscular dystrophies: Loss of cytoskeleton-extracellular matrix linkage , 1995, Cell.

[30]  J. Estrela,et al.  Increased ATP-ubiquitin-dependent proteolysis in skeletal muscles of tumor-bearing rats. , 1994, Cancer research.

[31]  W. Mitch,et al.  Acidosis and glucocorticoids concomitantly increase ubiquitin and proteasome subunit mRNAs in rat muscle. , 1994, The American journal of physiology.

[32]  A. Goldberg,et al.  Glucocorticoids activate the ATP-ubiquitin-dependent proteolytic system in skeletal muscle during fasting. , 1993, The American journal of physiology.

[33]  D. Béchet,et al.  Expression of lysosomal cathepsin B during calf myoblast-myotube differentiation. Characterization of a cDNA encoding bovine cathepsin B. , 1991, The Journal of biological chemistry.

[34]  R. Edwards,et al.  Effects of calcium on protein turnover of incubated muscles from mdx mice. , 1991, The American journal of physiology.

[35]  D. Béchet,et al.  Cimaterol reduces cathepsin activities but has no anabolic effect in cultured myotubes. , 1990, The American journal of physiology.

[36]  H. Kawasaki,et al.  Molecular cloning of a novel mammalian calcium-dependent protease distinct from both m- and mu-types. Specific expression of the mRNA in skeletal muscle. , 1989, The Journal of biological chemistry.

[37]  N. Rabbani,et al.  Calcium-activated neutral protease and its endogenous inhibitor in tissues of dystrophic and normal mice. , 1987, Biochemical medicine and metabolic biology.

[38]  P. Chomczyński,et al.  Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. , 1987, Analytical biochemistry.

[39]  B. Lowell,et al.  Evidence that lysosomes are not involved in the degradation of myofibrillar proteins in rat skeletal muscle. , 1986, The Biochemical journal.

[40]  N. Katunuma,et al.  Increases in cathepsins B and L and thiol proteinase inhibitor in muscle of dystrophic hamsters. Their localization in invading phagocytes. , 1984, Journal of biochemistry.

[41]  A. Goldberg,et al.  Does leucine, leucyl-tRNA, or some metabolite of leucine regulate protein synthesis and degradation in skeletal and cardiac muscle? , 1982, The Journal of biological chemistry.