scholarly journals Human Tonic and Phasic Smooth Muscle Myosin Isoforms Are Unresponsive to the Loop 1 Insert

2013 ◽  
Vol 2013 ◽  
pp. 1-6 ◽  
Author(s):  
Katalin Ajtai ◽  
Azad Mayanglambam ◽  
Yihua Wang ◽  
Thomas P. Burghardt
2005 ◽  
Vol 173 (1) ◽  
pp. 302-308 ◽  
Author(s):  
ANITA S. MANNIKAROTTU ◽  
JOSEPH A. HYPOLITE ◽  
STEPHEN A. ZDERIC ◽  
ALAN J. WEIN ◽  
SAMUEL CHACKO ◽  
...  

1989 ◽  
Vol 257 (1) ◽  
Author(s):  
Ute Gr�schel-Stewart ◽  
Elke Magel ◽  
Elke Paul ◽  
Anna-Corina Neidlinger

2017 ◽  
Vol 22 (1) ◽  
pp. 576-588 ◽  
Author(s):  
Ping Chen ◽  
Jing Yin ◽  
Yu-ming Guo ◽  
He Xiao ◽  
Xing-huan Wang ◽  
...  

2005 ◽  
Vol 173 (4S) ◽  
pp. 137-138
Author(s):  
Paul M. Milhoua ◽  
Philip T. Koi ◽  
Michael E. DiSanto ◽  
Arnold Melman

2002 ◽  
Vol 156 (1) ◽  
pp. 113-124 ◽  
Author(s):  
Arthur S. Rovner ◽  
Patricia M. Fagnant ◽  
Susan Lowey ◽  
Kathleen M. Trybus

The alternatively spliced SM1 and SM2 smooth muscle myosin heavy chains differ at their respective carboxyl termini by 43 versus 9 unique amino acids. To determine whether these tailpieces affect filament assembly, SM1 and SM2 myosins, the rod region of these myosin isoforms, and a rod with no tailpiece (tailless), were expressed in Sf 9 cells. Paracrystals formed from SM1 and SM2 rod fragments showed different modes of molecular packing, indicating that the tailpieces can influence filament structure. The SM2 rod was less able to assemble into stable filaments than either SM1 or the tailless rods. Expressed full-length SM1 and SM2 myosins showed solubility differences comparable to the rods, establishing the validity of the latter as a model for filament assembly. Formation of homodimers of SM1 and SM2 rods was favored over the heterodimer in cells coinfected with both viruses, compared with mixtures of the two heavy chains renatured in vitro. These results demonstrate for the first time that the smooth muscle myosin tailpieces differentially affect filament assembly, and suggest that homogeneous thick filaments containing SM1 or SM2 myosin could serve distinct functions within smooth muscle cells.


1993 ◽  
Vol 264 (5) ◽  
pp. H1653-H1662 ◽  
Author(s):  
A. E. Tsao ◽  
T. J. Eddinger

Two smooth muscle myosin heavy chains (MHC; SM1 and SM2) of approximately 204 and 200 kDa exist in smooth muscle cells and can be visualized on reducing sodium dodecyl sulfate (SDS)-polyacrylamide gels. Chymotryptic digestion of the native myosin molecule results in two fragments: heavy meromyosin (HMM) and light meromyosin (LMM). LMM is the alpha-helical coiled-coil carboxy terminal half of the molecule containing the difference peptide between SM1 and SM2. Electrophoresis of the LMM fragments on a reducing SDS-polyacrylamide gel resolves two subunits from the two MHC [LM1 from SM1 (approximately 100 kDa) and LM2 from SM2 (approximately 95 kDa), where LM1 and LM2 are LMM from SM1 and SM2, respectively]. CuCl2 oxidation of the LMM fragment forms intramolecular disulfide bonds between adjacent cysteines on the two LMM fragments. When the native LMM is oxidized with CuCl2 and run on a nonreducing SDS-polyacrylamide gel, three bands are observed, which migrate at approximately 195, 190, and 185 kDa (bands 1, 2, and 3). Excision of these bands and electrophoresis on a reducing SDS-polyacrylamide gel show their subunit composition. Band 1 is composed solely of LM1. Band 2 is composed of an equal ratio of LM1 and LM2, and band 3 is composed solely of LM2. Using a variety of biochemical procedures, along with nonreducing SDS-polyacrylamide gels, we interpret these results to indicate that there are three smooth muscle myosin isoforms that result from the various combinations of the two smooth muscle MHC (SM1 homodimer, SM1-SM2 heterodimer, and SM2 homodimer).


1990 ◽  
Vol 190 (1) ◽  
pp. 1-10 ◽  
Author(s):  
Anna C. Borrione ◽  
Anna Maria C. Zanellato ◽  
Luca Giuriato ◽  
Gianluigi Scannapieco ◽  
Paolo Pauletto ◽  
...  

2017 ◽  
Vol 197 (4S) ◽  
Author(s):  
Ping Chen ◽  
Jing Yin ◽  
Yuming Guo ◽  
Xinghuan Wang ◽  
Michael E DiSanto ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document