Altered Expression of Skeletal Muscle Myosin Isoforms in Cancer Cachexia

Document Type




Format of Original

8 p.

Publication Date



American Physiological Society

Source Publication

American Journal of Physiology - Cell Physiology

Source ISSN


Original Item ID

doi: 10.1152/ajpcell.00154.2002; Shelves: QP1 .A 5Storage S


Cachexia is commonly seen in cancer and is characterized by severe muscle wasting, but little is known about the effect of cancer cachexia on expression of contractile protein isoforms such as myosin. Other causes of muscle atrophy shift expression of myosin isoforms toward increased fast (type II) isoform expression. We injected mice with murine C-26 adenocarcinoma cells, a tumor cell line that has been shown to cause muscle wasting. Mice were killed 21 days after tumor injection, and hindlimb muscles were removed. Myosin heavy chain (MHC) and myosin light chain (MLC) content was determined in muscle homogenates by SDS-PAGE. Body weight was significantly lower in tumor-bearing (T) mice. There was a significant decrease in muscle mass in all three muscles tested compared with control, with the largest decrease occurring in the soleus. Although no type IIb MHC was detected in the soleus samples from control mice, type IIb comprised 19% of the total MHC in T soleus. Type I MHC was significantly decreased in T vs. control soleus muscle. MHC isoform content was not significantly different from control in plantaris and gastrocnemius muscles. These data are the first to show a change in myosin isoform expression accompanying muscle atrophy during cancer cachexia.


American Journal of Physiology - Cell Physiology, Vol. 52, No. 5 (November 2002): C1376-1382. DOI.

Donna O. McCarthy was affiliated with the University of Wisconsin - Madison at the time of publication.