scholarly journals Decreased expression of myogenic transcription factors and myosin heavy chains in Caenorhabditis elegans muscles developed during spaceflight

2006 ◽  
Vol 209 (18) ◽  
pp. 3695-3695 ◽  
Author(s):  
A. Higashibata
Keyword(s):  
Transcription Factors ◽  
Caenorhabditis Elegans ◽  
Myosin Heavy Chains ◽  
Heavy Chains

scholarly journals Immunochemical localization of myosin heavy chain isoforms and paramyosin in developmentally and structurally diverse muscle cell types of the nematode Caenorhabditis elegans.

1987 ◽  
Vol 105 (6) ◽  
pp. 2763-2770 ◽  
Author(s):  
J P Ardizzi ◽  
H F Epstein
Keyword(s):  
Caenorhabditis Elegans ◽  
Muscle Cell ◽  
Body Wall ◽  
Muscle Cells ◽  
Cell Types ◽  
The Body ◽  
Myosin Heavy Chains ◽  
Nematode Caenorhabditis Elegans ◽  
Heavy Chains ◽  
Pharyngeal Muscles

The nematode Caenorhabditis elegans contains two major groups of muscle cells that exhibit organized sarcomeres: the body wall and pharyngeal muscles. Several additional groups of muscle cells of more limited mass and spatial distribution include the vulval muscles of hermaphrodites, the male sex muscles, the anal-intestinal muscles, and the gonadal sheath of the hermaphrodite. These muscle groups do not exhibit sarcomeres and therefore may be considered smooth. Each muscle cell has been shown to have a specific origin in embryonic cell lineages and differentiation, either embryonically or postembryonically (Sulston, J. E., and H. R. Horvitz. 1977. Dev. Biol. 56:110-156; Sulston, J. E., E. Schierenberg, J. White, and J. N. Thomson. 1983. Dev. Biol. 100:64-119). Each muscle type exhibits a unique combination of lineage and onset of differentiation at the cellular level. Biochemically characterized monoclonal antibodies to myosin heavy chains A, B, C, and D and to paramyosin have been used in immunochemical localization experiments. Paramyosin is detected by immunofluorescence in all muscle cells. Myosin heavy chains C and D are limited to the pharyngeal muscle cells, whereas myosin heavy chains A and B are localized not only within the sarcomeres of body wall muscle cells, as reported previously, but to the smooth muscle cells of the minor groups as well. Myosin heavy chains A and B and paramyosin proteins appear to be compatible with functionally and structurally distinct muscle cell types that arise by multiple developmental pathways.

scholarly journals Myosin and paramyosin of Caenorhabditis elegans embryos assemble into nascent structures distinct from thick filaments and multi-filament assemblages

1993 ◽  
Vol 122 (4) ◽  
pp. 845-858 ◽  
Author(s):  
HF Epstein ◽  
DL Casey ◽  
I Ortiz
Keyword(s):  
Caenorhabditis Elegans ◽  
Functional Relationship ◽  
Immunofluorescence Microscopy ◽  
Myosin Heavy Chains ◽  
Wild Type ◽  
Linear Structures ◽  
Heavy Chains ◽  
Thick Filaments ◽  
Vertebrate Muscle ◽  
Charge Change

The organization of myosin heavy chains (mhc) A and B and paramyosin (pm) which are the major proteins of thick filaments in adult wild-type Caenorhabditis elegans were studied during embryonic development. As a probe of myosin-paramyosin interaction, the unc-15 mutation e73 which produces a glu342lys charge change in pm and leads to the formation of large paracrystalline multi-filament assemblages was compared to wild type. These three proteins colocalized in wild-type embryos from 300 to 550 min of development after first cleavage at 20 degrees C on the basis of immunofluorescence microscopy using specific monoclonal antibodies. Linear structures which were diversely oriented around the muscle cell peripheries appeared at 360 min and became progressively more aligned parallel to the embryonic long axis until distinct myofibrils were formed at 550 min. In the mutant, mhc A and pm were colocalized in the linear structures, but became progressively separated until they showed no spatial overlap at the myofibril stage. These results indicate that the linear structures represent nascent assemblies containing myosin and pm in which the proteins interact differently than in wild-type thick filaments of myofibrils. In e73, these nascent structures were distinct from the multi-filament assemblages. The overlapping of actin and mhc A in the nascent linear structures suggests their possible structural and functional relationship to the "stress fiber-like structures" of cultured vertebrate muscle cells.

Monospecific Antibodies against the Three Mammalian Fast Limb Myosin Heavy Chains

2000 ◽  
Vol 272 (1) ◽  
pp. 303-308 ◽  
Author(s):  
Christine A. Lucas ◽  
Lucia H.D. Kang ◽  
Joseph F.Y. Hoh
Keyword(s):  
Myosin Heavy Chains ◽  
Heavy Chains ◽  
Monospecific Antibodies

scholarly journals Carbonylation of myosin heavy chains in rat heart during diabetes

2010 ◽  
Vol 80 (2) ◽  
pp. 205-217 ◽  
Author(s):  
Chun-Hong Shao ◽  
George J. Rozanski ◽  
Ryoji Nagai ◽  
Frank E. Stockdale ◽  
Kaushik P. Patel ◽  
...  
Keyword(s):  
Rat Heart ◽  
Myosin Heavy Chains ◽  
Heavy Chains

scholarly journals Shortening velocity and myosin heavy chains of developing rabbit muscle fibers.

1985 ◽  
Vol 260 (27) ◽  
pp. 14403-14405 ◽  
Author(s):  
P J Reiser ◽  
R L Moss ◽  
G G Giulian ◽  
M L Greaser
Keyword(s):  
Muscle Fibers ◽  
Rabbit Muscle ◽  
Myosin Heavy Chains ◽  
Shortening Velocity ◽  
Heavy Chains

Modulation of Myosin Heavy Chains in Rat Laryngeal Muscle

2001 ◽  
Vol 111 (3) ◽  
pp. 472-477 ◽  
Author(s):  
Akihiro Shiotani ◽  
Hideki Nakagawa ◽  
Paul W. Flint
Keyword(s):  
Myosin Heavy Chains ◽  
Laryngeal Muscle ◽  
Heavy Chains
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