scholarly journals Intraspecific myosin light chain polymorphism in the white muscle of herring (Clupea harengus harengus, L.)

FEBS Letters ◽  
1990 ◽  
Vol 265 (1-2) ◽  
pp. 23-26 ◽  
Author(s):  
I. Martinez ◽  
R. Ofstad ◽  
R.L. Olsen
Author(s):  
I. A. Johnston ◽  
Z. Horne

The myotomes in yolk-sac larvae of the Atlantic herring (Clupea harengus: Teleostei) contain a single layer of small-diameter superficial muscle fibres surrounding an inner mass of around 280 larger-diameter muscle fibres. The fraction of muscle fibre volume occupied by mitochondria is dependent on temperature, and in larvae reared at 8°C was 41% for the superficial fibres, and 25% for the inner muscle fibres. The inner muscle fibres of larvae share some myofibrillar proteins with adult white muscle, but contain unique isoforms of myosin heavy chains, troponin T, troponin I and myosin light chain 2. A monoclonal antibody has been produced which is specific to myosin light chain 3 (MLC3). Immunocytochemical studies have shown that the expression of MLC3 is switched off in the superficial muscle fibres at the start of metamorphosis when larvae reach 28–30 mm total length (TL). Metamorphosis to the juvenile stage is complete in fish 35–40 mm TL and is also associated with the development of gill filaments and the production of presumptive slow muscle fibres which form externally to the larval superficial muscle fibres in the region of the lateral line nerve.


2001 ◽  
Vol 204 (17) ◽  
pp. 3009-3018 ◽  
Author(s):  
Katerina A. Moutou ◽  
Adelino V. M. Canario ◽  
Zissis Mamuris ◽  
Deborah M. Power

SUMMARY Two full-length cDNA clones encoding the skeletal myosin light chain 2 (MLC2; 1452bp) and myosin light chain 3 (MLC3; 972bp) were isolated from a cDNA library prepared from gilthead sea bream Sparus aurata larvae. The MLC2 cDNA encoded a predicted protein of 170 residues that was 79% identical to rabbit MLC2 over the entire length and 87% identical within the Ca2+-binding region. The deduced amino acid sequence of MLC3 was 153 residues in length and was 91% and 69% identical to the zebrafish and rabbit MLC3, respectively. Northern blot analysis revealed that in adults both transcripts were expressed in fast white muscle only. MLC2 appeared earlier in development: MLC2 transcripts were detectable from the beginning of segmentation, whereas MLC3 transcripts did not appear until 27h post-fertilisation. At this developmental stage, a second MLC2 transcript of 0.89 kilobase-pairs was present. MLCs exhibited a different age-related pattern of response to varied thyroidal states, which were experimentally induced by the administration of 1μgg−1bodymass of thyroxine (T4) or triiodothyronine (T3), or 5ngg−1bodymass of the hypothyroidal compound thiourea; MLC3 expression was not significantly affected, whereas levels of MLC2 transcripts were significantly elevated in the white muscle only of juvenile sea bream after administration of T4. Although the mechanism of thyroidal regulation of MLC expression remains unknown, the present results suggest that different regulatory mechanisms exist for different MLCs.


1984 ◽  
Vol 247 (5) ◽  
pp. C462-C471 ◽  
Author(s):  
R. L. Moore ◽  
J. T. Stull

The physiological properties of contraction-induced phosphate incorporation into the phosphorylatable light chain (P-light chain) of myosin were examined in fast-twitch white, fast-twitch red, and slow-twitch skeletal muscles in situ. Neural stimulation of rat gastrocnemius muscles between 0.5 and 100 Hz produced an increase in the phosphate content of the P-light chain from the white portion of the muscle, and the rate of P-light chain phosphorylation was frequency dependent. The extent of phosphorylation of P-light chain from the fast-twitch red portion of the gastrocnemius muscle was less. In contrast to fast-twitch skeletal muscle, only high-frequency stimulation (30-100 Hz) produced a small increase in the phosphate content of P-light chain from the slow-twitch soleus muscle. Fast white muscle contained 2.2 and 3.5 times more myosin light chain kinase activity than did the fast red and slow muscle, respectively. The rate of P-light chain dephosphorylation was four times faster in slow muscle than in fast white muscle. Thus the greater extent of phosphorylation of P-light chain in fast-twitch white skeletal muscle fibers may be due in part to the presence of more kinase and less phosphatase activities. Isometric twitch tension potentiation was correlated to the extent of phosphorylation of P-light chain from fast white muscle. The physiological consequences of P-light chain phosphorylation are likely to be of greatest importance in fast-twitch white muscle.


2006 ◽  
Vol 175 (4S) ◽  
pp. 53-53
Author(s):  
Andy Y. Chang ◽  
Stephen A. Zderic ◽  
Douglas A. Canning ◽  
Samuel Chacko

Circulation ◽  
1997 ◽  
Vol 96 (12) ◽  
pp. 4357-4363 ◽  
Author(s):  
Naoki Katsumata ◽  
Hiroaki Shimokawa ◽  
Minoru Seto ◽  
Toshiyuki Kozai ◽  
Tohru Yamawaki ◽  
...  

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