Document Type
Article
Language
eng
Format of Original
9 p.
Publication Date
6-2007
Publisher
Karger
Source Publication
Journal of Vascular Research
Source ISSN
1018-1172
Abstract
Smooth muscle myosin heavy chains occur in 2 isoforms, SMA (slow) and SMB (fast). We hypothesized that the SMB isoform is predominant in the faster-contracting rat vena cava compared to thoracic aorta. We compared the time to half maximal contraction in response to a maximal concentration of endothelin-1 (ET-1; 100 nM), potassium chloride (KCl; 100 mM) and norepinephrine (NE; 10 µM). The time to half maximal contraction was shorter in the vena cava compared to aorta (aorta: ET-1 = 235.8 ± 13.8 s, KCl = 140.0 ± 33.3 s, NE = 19.8 ± 2.7 s; vena cava: ET-1 = 121.8 ± 15.6 s, KCl = 49.5 ± 6.7 s, NE = 9.0 ± 3.3 s). Reverse-transcription polymerase chain reaction supported the greater expression of SMB in the vena cava compared to aorta. SMB was expressed to a greater extent than SMA in the vessel wall of the vena cava. Western analysis determined that expression of SMB, relative to total smooth muscle myosin heavy chains, was 12.5 ± 4.9-fold higher in the vena cava compared to aorta, while SMA was 4.9 ± 1.2-fold higher in the aorta than vena cava. Thus, the SMB isoform is the predominant form expressed in rat veins, providing one possible mechanism for the faster response of veins to vasoconstrictors.
Recommended Citation
Rondelli, Catherine M.; Szasz, Irina T.; Kayal, Anas; Thakali, Keshari; Watson, Ralph E.; Rovner, Arthur S.; Eddinger, Thomas; Fink, Gregory D.; and Watts, Stephanie W., "Preferential Myosin Heavy Chain Isoform B Expression May Contribute to the Faster Velocity of Contraction in Veins versus Arteries" (2007). Biological Sciences Faculty Research and Publications. 2.
https://epublications.marquette.edu/bio_fac/2
Comments
Accepted version. Journal of Vascular Research, Vol. 44, No. 4 (June 2007): 264-272. DOI. © 2007 Karger. Used with permission.
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