Electrophoretic separation of reptilian skeletal and cardiac muscle myosin heavy chain isoforms: Dependence on gel format

2014 ◽  
Vol 35 (18) ◽  
pp. 2615-2620 ◽  
Author(s):  
Peter J. Reiser ◽  
Sabahattin Bicer
Keyword(s):  
Cardiac Muscle ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Myosin Heavy Chain Isoforms ◽  
Electrophoretic Separation ◽  
Muscle Myosin

Electrophoretic separation of bovine muscle myosin heavy chain isoforms

Meat Science ◽  
1999 ◽  
Vol 53 (1) ◽  
pp. 1-7 ◽  
Author(s):  
B. Picard ◽  
C. Barboiron ◽  
M.P. Duris ◽  
H. Gagniére ◽  
C. Jurie ◽  
...  
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Myosin Heavy Chain Isoforms ◽  
Electrophoretic Separation ◽  
Bovine Muscle ◽  
Muscle Myosin

Electrophoretic Separation of Myosin Heavy Chain Isoforms Using a Modified Mini Gel System

2012 ◽  
Vol 26 (12) ◽  
pp. 3461-3468 ◽  
Author(s):  
Michael D. Roberts ◽  
Vincent J. Dalbo ◽  
Kyle L. Sunderland ◽  
Chad M. Kerksick
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Myosin Heavy Chain Isoforms ◽  
Electrophoretic Separation ◽  
Gel System

Hypertensive renal damage: Modulation expression of smooth muscle myosin heavy chain isoforms

Nephrology ◽  
1997 ◽  
Vol 3 (3) ◽  
pp. 251-259
Author(s):  
Naoe SUZUKI ◽  
Kenjiro KIMURA ◽  
Ryozo NAGAI ◽  
Shigeyoshi OHBA ◽  
Naobumi MISE ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Renal Damage ◽  
Myosin Heavy Chain Isoforms ◽  
Smooth Muscle Myosin ◽  
Muscle Myosin

Expression and function of COOH-terminal myosin heavy chain isoforms in mouse smooth muscle

2007 ◽  
Vol 293 (1) ◽  
pp. C238-C245 ◽  
Author(s):  
Anne F. Martin ◽  
Sunita Bhatti ◽  
Gail J. Pyne-Geithman ◽  
Mariam Farjah ◽  
Vlasios Manaves ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Immunoblot Analysis ◽  
Myosin Heavy Chain Isoforms ◽  
Smooth Muscle Myosin ◽  
Tail Region ◽  
Protein Ratio ◽  
Muscle Myosin

Isoforms of the smooth muscle myosin motor, SM1 and SM2, differ in length at the carboxy terminal tail region. Their proportion changes with development, hormonal status and disease, but their function is unknown. We developed mice carrying the myosin heavy chain (MyHC) transgenes SM1, cMyc-tagged SM1, SM2, and V5-tagged SM2, and all transgenes corresponded to the SMa NH2-terminal isoform. Transgene expression was targeted to smooth muscle by the smooth muscle α-actin promoter. Immunoblot analysis showed substantial expression of the cMyc-tagged SM1 and V5-tagged SM2 MyHC protein in aorta and bladder and transgene mRNA was expressed in mice carrying unlabeled SM1 or SM2 transgenes. Despite significant protein expression of tagged MyHCs we found only small changes in the SM1:SM2 protein ratio. Significant changes in functional phenotype were observed in mice carrying unlabeled SM1 or SM2 transgenes. Force in aorta and bladder was increased (72 ± 14%, 92 ± 11%) in SM1 and decreased to 57 ± 1% and 80 ± 3% in SM2 transgenic mice. SM1 transgenic bladders had faster (1.8 ± 0.3 s) and SM2 slower (7.1 ± 0.5 s) rates of force redevelopment following a rapid step shortening. We hypothesize that small changes in the SM1:SM2 ratio could be amplified if they are associated with changes in thick filament assembly and underlie the altered contractility. These data provide evidence indicating an in vivo function for the COOH-terminal isoforms of smooth muscle myosin and suggest that the SM1:SM2 ratio is tightly regulated in smooth muscle tissues.

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