scholarly journals The expression and functional activities of smooth muscle myosin and non-muscle myosin isoforms in rat prostate

2017 ◽  
Vol 22 (1) ◽  
pp. 576-588 ◽  
Author(s):  
Ping Chen ◽  
Jing Yin ◽  
Yu-ming Guo ◽  
He Xiao ◽  
Xing-huan Wang ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Smooth Muscle Myosin ◽  
Myosin Isoforms ◽  
Functional Activities ◽  
Rat Prostate ◽  
Muscle Myosin

scholarly journals MP17-19 THE EXPRESSION AND FUNCTIONAL ACTIVITIES OF SMOOTH MUSCLE MYOSIN AND NON-MUSCLE MYOSIN ISOFORMS IN RAT PROSTATE

2017 ◽  
Vol 197 (4S) ◽  
Author(s):  
Ping Chen ◽  
Jing Yin ◽  
Yuming Guo ◽  
Xinghuan Wang ◽  
Michael E DiSanto ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Smooth Muscle Myosin ◽  
Myosin Isoforms ◽  
Functional Activities ◽  
Rat Prostate ◽  
Muscle Myosin

REGIONAL ALTERATIONS IN THE EXPRESSION OF SMOOTH MUSCLE MYOSIN ISOFORMS IN RESPONSE TO PARTIAL BLADDER OUTLET OBSTRUCTION

2005 ◽  
Vol 173 (1) ◽  
pp. 302-308 ◽  
Author(s):  
ANITA S. MANNIKAROTTU ◽  
JOSEPH A. HYPOLITE ◽  
STEPHEN A. ZDERIC ◽  
ALAN J. WEIN ◽  
SAMUEL CHACKO ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Bladder Outlet Obstruction ◽  
Outlet Obstruction ◽  
Smooth Muscle Myosin ◽  
Myosin Isoforms ◽  
Partial Bladder Outlet Obstruction ◽  
Muscle Myosin

Pig brain homogenates contain smooth muscle myosin and cytoplasmic myosin isoforms

1989 ◽  
Vol 257 (1) ◽  
Author(s):  
Ute Gr�schel-Stewart ◽  
Elke Magel ◽  
Elke Paul ◽  
Anna-Corina Neidlinger
Keyword(s):  
Smooth Muscle ◽  
Smooth Muscle Myosin ◽  
Myosin Isoforms ◽  
Pig Brain ◽  
Muscle Myosin

505: Effect of Partial Outlet Obstruction on the Expression of Smooth Muscle Myosin Isoforms in Rat Ureter

2005 ◽  
Vol 173 (4S) ◽  
pp. 137-138
Author(s):  
Paul M. Milhoua ◽  
Philip T. Koi ◽  
Michael E. DiSanto ◽  
Arnold Melman
Keyword(s):  
Smooth Muscle ◽  
Outlet Obstruction ◽  
Smooth Muscle Myosin ◽  
Myosin Isoforms ◽  
Muscle Myosin

scholarly journals Smooth muscle myosin expression, isoform composition, and functional activities in rat corpus cavernosum altered by the streptozotocin-induced type 1 diabetes

2012 ◽  
Vol 302 (1) ◽  
pp. E32-E42 ◽  
Author(s):  
Xinhua Zhang ◽  
Nirmala D. Kanika ◽  
Arnold Melman ◽  
Michael E. DiSanto
Keyword(s):  
Smooth Muscle ◽  
Alternative Splicing ◽  
Corpus Cavernosum ◽  
Smooth Muscle Myosin ◽  
Organ Bath ◽  
Rt Pcr ◽  
Functional Activities ◽  
Muscle Myosin

Diabetes mellitus (DM) is a quite common chronic disease, and the prevalence of erectile dysfunction (ED) is three times higher in this large population. Although diabetes-related ED has been studied extensively, the actin-myosin contractile apparatus was not examined. The mRNAs encoding smooth muscle myosin (SMM) heavy chains (MHC) and essential light chains (LC17) exist as several different alternatively spliced isoforms with distinct contractile properties. Recently, we provided novel data that blebbistatin (BLEB), a specific myosin II inhibitor, potently relaxed corpus cavernosum smooth muscle (CCSM). In this study, we examine whether diabetes alters SMM expression, alternative splicing, and/or functional activities, including sensitivity to BLEB. By using streptozotocin (STZ)-induced 2-mo diabetic rats, functional activities were tested in vivo by intracavernous pressure (ICP) recording during cavernous nerve stimulation and in vitro via organ bath contractility studies. SMM isoform composition was analyzed by competitive RT-PCR and total SMM, myocardin, and embryonic SMM (SMemb) expression by real-time RT-PCR. Results revealed that the blood glucose level of STZ rats was 407.0 vs. 129.5 mg/dl (control). STZ rats exhibited ED confirmed by significantly increased CCSM contractile response to phenylephrine and decreased ICP response. For STZ rats, SM-B, LC17a and SM2 isoforms, total SMM, and myocardin expression increased, whereas SM-A, LC17b, and SM1 isoforms were decreased, with SMemb unchanged. BLEB was significantly more effective in relaxing STZ CCSM both in vitro and in vivo. Thus we demonstrated a novel diabetes-specific effect on alternative splicing of the SMM heavy chain and essential light chain genes to a SMM isoform composition favoring a heightened contractility and ED. A switch to a more contractile phenotype was supported further by total SMM expression increase. Moreover, the change in CCSM phenotype was associated with an increased sensitivity to BLEB, which may serve as a novel pharmacotherapy for ED.

scholarly journals The carboxyl-terminal isoforms of smooth muscle myosin heavy chain determine thick filament assembly properties

2002 ◽  
Vol 156 (1) ◽  
pp. 113-124 ◽  
Author(s):  
Arthur S. Rovner ◽  
Patricia M. Fagnant ◽  
Susan Lowey ◽  
Kathleen M. Trybus
Keyword(s):  
Smooth Muscle ◽  
Thick Filament ◽  
Smooth Muscle Myosin ◽  
Myosin Isoforms ◽  
Heavy Chains ◽  
Filament Assembly ◽  
Filament Structure ◽  
Alternatively Spliced ◽  
Muscle Myosin

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.

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
Keyword(s):  
Smooth Muscle ◽  
Smooth Muscle Myosin ◽  
Myosin Isoforms ◽  
Muscle Myosin ◽  
Phasic Smooth Muscle

Smooth muscle myosin heavy chains combine to form three native myosin isoforms

1993 ◽  
Vol 264 (5) ◽  
pp. H1653-H1662 ◽  
Author(s):  
A. E. Tsao ◽  
T. J. Eddinger
Keyword(s):  
Smooth Muscle ◽  
Sodium Dodecyl ◽  
Coiled Coil ◽  
Smooth Muscle Myosin ◽  
Polyacrylamide Gel ◽  
Myosin Isoforms ◽  
Myosin Heavy Chains ◽  
Polyacrylamide Gels ◽  
Heavy Chains ◽  
Muscle Myosin

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).

Nonmuscle and smooth muscle myosin isoforms in bovine endothelial cells

1990 ◽  
Vol 190 (1) ◽  
pp. 1-10 ◽  
Author(s):  
Anna C. Borrione ◽  
Anna Maria C. Zanellato ◽  
Luca Giuriato ◽  
Gianluigi Scannapieco ◽  
Paolo Pauletto ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Smooth Muscle ◽  
Smooth Muscle Myosin ◽  
Myosin Isoforms ◽  
Bovine Endothelial Cells ◽  
Muscle Myosin
Sign in / Sign up

Export Citation Format

Share Document