scholarly journals Agaro-Oligosaccharides Prevent Myostatin Hyperexpression and Myosin Heavy Chain Protein Degradation in C2C12 Myotubes Induced by Tumor Necrosis Factor-<i>α</i>

CellBio ◽  
2018 ◽  
Vol 07 (02) ◽  
pp. 23-34
Author(s):  
Ikuya Shirai ◽  
Takehiko Sakai ◽  
Katsuhiro Shiba ◽  
Yuji Uzuhashi ◽  
Koji Karasawa
Keyword(s):  
Tumor Necrosis Factor ◽  
Protein Degradation ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Tumor Necrosis ◽  
C2c12 Myotubes ◽  
Myosin Heavy Chain Protein ◽  
Necrosis Factor

scholarly journals Irreversible Heavy Chain Transfer to Hyaluronan Oligosaccharides by Tumor Necrosis Factor-stimulated Gene-6

2012 ◽  
Vol 288 (1) ◽  
pp. 205-214 ◽  
Author(s):  
Mark E. Lauer ◽  
Tibor T. Glant ◽  
Katalin Mikecz ◽  
Paul L. DeAngelis ◽  
F. Michael Haller ◽  
...  
Keyword(s):  
Tumor Necrosis Factor ◽  
Heavy Chain ◽  
Tumor Necrosis ◽  
Chain Transfer ◽  
Necrosis Factor

scholarly journals Restoration of Overexpressed Variable Heavy Chain 2 Transcripts with Tumor Necrosis Factor Inhibitors in Ankylosing Spondylitis

2014 ◽  
Vol 41 (3) ◽  
pp. 613-614 ◽  
Author(s):  
DONG-HUYK SHEEN ◽  
JI-YOUNG KIM ◽  
SO YOUNG LEE ◽  
MI-KYOUNG LIM ◽  
SOO-JIN YOO ◽  
...  
Keyword(s):  
Ankylosing Spondylitis ◽  
Tumor Necrosis Factor ◽  
Heavy Chain ◽  
Tumor Necrosis ◽  
Tumor Necrosis Factor Inhibitors ◽  
Variable Heavy ◽  
Necrosis Factor

Tumor necrosis factor-α promotes the accumulation of neutrophils and macrophages in skeletal muscle

2006 ◽  
Vol 101 (5) ◽  
pp. 1394-1399 ◽  
Author(s):  
Jennifer M. Peterson ◽  
Kevin D. Feeback ◽  
Joel H. Baas ◽  
Francis X. Pizza
Keyword(s):  
Tumor Necrosis Factor ◽  
Tumor Necrosis ◽  
Tumor Necrosis Factor Α ◽  
Inflammatory Cell ◽  
Total Protein Content ◽  
Cross Sectional ◽  
Tnf Α ◽  
Myosin Heavy Chain Protein ◽  
Factor Α ◽  
Necrosis Factor

Tumor necrosis factor-α (TNF-α) has been associated with cachexia and is known to regulate multiple inflammatory cell (neutrophil and macrophage) responses. We tested the hypothesis that neutrophils and macrophages accumulate in the extensor digitorum longus (EDL) and soleus muscles of mice after chronic TNF-α administration. Murine recombinant TNF-α (∼100 μg·kg−1·day−1) in vehicle solution or vehicle solution alone (sham) was administered to C57BL/6 mice for 7 days via osmotic minipumps. In EDL muscles from TNF-α-treated mice, neutrophil and macrophage concentrations were elevated seven- and threefold, respectively, compared with sham mice. Neutrophil and macrophage concentrations were also elevated five- and twofold, respectively, in solei of TNF-α- relative to sham-treated mice. Treatment with TNF-α elevated ubiquitin content by ∼25% relative to sham values for both the EDL and soleus muscles; however, these elevations were not statistically significant. No differences were observed between TNF-α- and sham-treated mice in body weight, food consumption, muscle mass, myofiber cross-sectional area, carbonyl groups, total protein content, or relative abundance of myosin heavy chain protein. Furthermore, no overt signs of muscle injury or regeneration were observed in muscles from TNF-α-treated mice in either the EDL or soleus muscles. These observations suggest that 7 days of TNF-α administration promote muscle inflammation as indicated by the accumulation of neutrophils and macrophages without overt signs of atrophy, injury, or regeneration.

scholarly journals A tumor necrosis factor (TNF) receptor-IgG heavy chain chimeric protein as a bivalent antagonist of TNF activity.

1991 ◽  
Vol 174 (6) ◽  
pp. 1483-1489 ◽  
Author(s):  
K Peppel ◽  
D Crawford ◽  
B Beutler
Keyword(s):  
Tumor Necrosis Factor ◽  
Heavy Chain ◽  
Tumor Necrosis ◽  
Chinese Hamster Ovary Cells ◽  
Chimeric Protein ◽  
Extracellular Domain ◽  
Tnf Inhibitor ◽  
Tnf Receptor ◽  
Sequence Encoding ◽  
Necrosis Factor

Using a multistep polymerase chain reaction method, we have produced a construct in which a cDNA sequence encoding the extracellular domain of the human 55-kD tumor necrosis factor (TNF) receptor is attached to a sequence encoding the Fc portion and hinge region of a mouse IgG1 heavy chain through an oligomer encoding a thrombin-sensitive peptide linker. This construct was placed downstream from a cytomegalovirus promoter sequence, and expressed in Chinese hamster ovary cells. A secreted protein, capable of binding TNF and inactivating it, was produced by the transfected cells. Molecular characterization revealed that this soluble version of the TNF receptor was dimeric. Moreover, the protein could be quantitatively cleaved by treatment with thrombin. However, the monovalent extracellular domain prepared in this way has a greatly reduced TNF inhibitory activity compared with that of the bivalent inhibitor. Perhaps because of its high affinity for TNF, the chimeric protein is far more effective as a TNF inhibitor than are neutralizing monoclonal antibodies. This molecule may prove very useful as a reagent for the antagonism and assay of TNF and lymphotoxin from diverse species in health and disease, and as a means of deciphering the exact mechanism through which TNF interacts with the 55-kD receptor.

scholarly journals The molecular cloning and characterization of murine ferritin heavy chain, a tumor necrosis factor-inducible gene.

1988 ◽  
Vol 263 (25) ◽  
pp. 12638-12644 ◽  
Author(s):  
S V Torti ◽  
E L Kwak ◽  
S C Miller ◽  
L L Miller ◽  
G M Ringold ◽  
...  
Keyword(s):  
Tumor Necrosis Factor ◽  
Molecular Cloning ◽  
Heavy Chain ◽  
Tumor Necrosis ◽  
Ferritin Heavy Chain ◽  
Necrosis Factor ◽  
Inducible Gene
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