Myosin isoform heterogeneity in single smooth muscle cells

被引:9
作者
Eddinger, TJ
Meer, DP
机构
[1] Department of Biology, Marquette University, Milwaukee
[2] Department of Biology, Marquette University, WLS 109, Milwaukee, WI 53201-1881
来源
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY | 1997年 / 117卷 / 01期
关键词
smooth muscle; myosin; heavy chain isoforms; RT-PCR; quantitation; vascular; isozymes;
D O I
10.1016/S0305-0491(96)00312-4
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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. (C) 1997 Elsevier Science Inc.
引用
收藏
页码:29 / 38
页数:10
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