Format of Original
Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology
We review the current understanding of the myosin heavy chain (MHC) isoforms and show that the mRNA levels of smooth muscle (SM)1 and SM2 mimic the expressed levels of SM1 and SM2 protein. The reverse transcriptase-polymerase chain reaction technique has been shown to be sufficiently sensitive to examine SM-MHC expression at the single cell level. Most single smooth muscle cells isolated from adult rabbit carotid express both SM1 and SM2. However, expression of these SM-MHC isoforms at the cellular level is nonuniform and highly variable. This work provides a foundation for future investigations as to the possible unique functional characteristics of the SM-MHC isoforms, SM1 and SM2. This methodology may also prove useful when used with mechanical studies to determine the physiological significance of the alternatively spliced myosin isoforms, including the SM-MHC-head and LC17 isoforms.
Eddinger, Thomas J. and Meer, Daniel P., "Myosin Isoform Heterogeneity in Single Smooth Muscle Cells" (1997). Biological Sciences Faculty Research and Publications. 187.
ADA Accessible Version
Accepted version. Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, Vol. 117, No. 1 (May 1997): 29-38. DOI. © 1997 Elsevier. Used with permission.