Document Type

Article

Language

eng

Publication Date

11-2002

Publisher

American Physiological Society

Source Publication

American Journal of Physiology - Cell Physiology

Source ISSN

0002-9513

Original Item ID

DOI: 10.1152/ajpcell.00154.2002

Abstract

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.

Comments

Accepted Version. American Journal of Physiology - Cell Physiology, Vol. 52, No. 5 (November 2002): C1376-1382. DOI. © 2002 American Physiological Society. Used with permission.

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

Download
mccarthy_4080acc.docx (298 kB)
ADA Accessible Version

Included in

Nursing Commons

Share

COinS