Faculty Collaboration Database

Myosin isoform heterogeneity in single smooth muscle cells. Comp Biochem Physiol B Biochem Mol Biol 1997 May;117(1):29-38

Date

05/01/1997

Pubmed ID

9180012

DOI

10.1016/s0305-0491(96)00312-4

Scopus ID

2-s2.0-0030906790 (requires institutional sign-in at Scopus site)   10 Citations

Abstract

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.

Author List

Eddinger TJ, Meer DP

Author

Thomas Eddinger PhD Bioological Sciences in the Biology department at Marquette University

MESH terms used to index this publication - Major topics in bold

Alternative Splicing
Animals
Exons
Humans
Models, Molecular
Muscle, Smooth
Muscle, Smooth, Vascular
Myosin Heavy Chains
Myosins
Polymerase Chain Reaction
RNA, Messenger
Transcription, Genetic