The effects of the interaction of myosin essential light chain isoforms with actin in skeletal muscles.

In order to compare the ability of different isoforms of myosin essential light chain to interact with actin, the effect of the latter protein on the proteolytic susceptibility of myosin light chains (MLC-1S and MLC-1V - slow specific and same as ventricular isoform) from slow skeletal muscle was examined. Actin protects both slow muscle essential light chain isoforms from papain digestion, similarly as observed for fast skeletal muscle myosin (Nieznanska et al., 1998, Biochim. Biophys. Acta 1383: 71). The effect of actin decreases as ionic strength rises above physiological values for both fast and slow skeletal myosin, confirming the ionic character of the actin-essential light chain interaction. To better understand the role of this interaction, we examined the effect of synthetic peptides spanning the 10-amino-acid N-terminal sequences of myosin light chain 1 from fast skeletal muscle (MLC-1F) (MLCFpep: KKDVKKPAAA), MLC-1S (MLCSpep: KKDVPVKKPA) and MLC-1V (MLCVpep: KPEPKKDDAK) on the myofibrillar ATPase of fast and slow skeletal muscle. In the presence of MLCFpep, we observed an about 19% increase, and in the presence of MLCSpep about 36% increase, in the myofibrillar ATPase activity of fast muscle. On the other hand, in myofibrillar preparations from slow skeletal muscle, MLCSpep as well as MLCVpep caused a lowering of the ATPase activity by about 36%. The above results suggest that MLCSpep induces opposite effects on ATPase activity, depending on the type of myofibrils, but not through its specific N-terminal sequence - which differs from other MLC N-terminal peptides. Our observations lead to the conclusion that the action of different isoforms of long essential light chain is similar in slow and fast skeletal muscle. However the interaction of essential light chains with actin leads to different physiological effects probably depending on the isoforms of other myofibrillar proteins.

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Assignment of the human fast skeletal muscle myosin alkali light chains gene (MLC1F/MLC3F) to 2q 32.1-2qter

Human Genetics ◽

10.1007/bf00291237 ◽

1988 ◽

Vol 78 (1) ◽

pp. 65-70 ◽

Cited By ~ 11

Author(s):

Odile Cohen-Haguenauer ◽

Paul J. R. Barton ◽

Nguyen Van Cong ◽

Stéphane Serero ◽

Marie-Sylvie Gross ◽

...

Keyword(s):

Skeletal Muscle ◽

Light Chains ◽

Fast Skeletal Muscle ◽

Skeletal Muscle Myosin ◽

Muscle Myosin

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Properties of the non-specific calcium-binding sites of rabbit skeletal-muscle myosin

Biochemical Journal ◽

10.1042/bj1850265 ◽

1980 ◽

Vol 185 (1) ◽

pp. 265-268 ◽

Cited By ~ 10

Author(s):

J Wikman-Coffelt

Keyword(s):

Skeletal Muscle ◽

Light Chain ◽

Binding Sites ◽

Calcium Binding ◽

Light Chains ◽

Binding Properties ◽

Skeletal Muscle Myosin ◽

Heavy Chains ◽

Calcium Binding Sites ◽

Muscle Myosin

The non-specific Ca2+-binding sites of skeletal-muscle myosin are located on the light chains; with the dissociation of light chains there is a corresponding decrease in the number of Ca2+-binding sites on light-chain-deficient myosin. The released light chains have a decreased binding affinity. Myosin heavy chains indirectly influence the Ca2+-binding properties of light chains by increasing the affinity of light chains for bivalent cations; this influence varies with pH. Because of light-chain dissociation at low Ca2+ and/or Mg2+ concentrations, anomalies may exist when analyses of non-specific Ca2+-binding properties of myosin are assessed by dialysis equilibrium.

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Influence of the regulatory light chain of fast skeletal muscle myosin on its interaction with actin in the presence and absence of ATP

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology ◽

10.1016/0167-4838(85)90176-1 ◽

1985 ◽

Vol 832 (1) ◽

pp. 80-88 ◽

Cited By ~ 8

Author(s):

R. Cardinaud ◽

Irena Ka̧kol

Keyword(s):

Skeletal Muscle ◽

Light Chain ◽

Regulatory Light Chain ◽

Fast Skeletal Muscle ◽

Skeletal Muscle Myosin ◽

Presence And Absence ◽

Muscle Myosin

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Order-disorder structural transitions in synthetic filaments of fast and slow skeletal muscle myosins under relaxing and activating conditions.

Acta Biochimica Polonica ◽

10.18388/abp.2000_3954 ◽

2000 ◽

Vol 47 (4) ◽

pp. 1007-1017 ◽

Cited By ~ 3

Author(s):

Z A Podlubnaya ◽

S L Malyshev ◽

K Nieznański ◽

D Stepkowski

Keyword(s):

Skeletal Muscle ◽

Ordered Structure ◽

Structural Transitions ◽

Fast Skeletal Muscle ◽

Skeletal Muscle Myosin ◽

Slow Skeletal Muscle ◽

Random Arrangement ◽

Vertebrate Muscle ◽

Myosin Filaments ◽

Muscle Myosin

In the previous study (Podlubnaya et al., 1999, J. Struc. Biol. 127, 1-15) Ca2+-induced reversible structural transitions in synthetic filaments of pure fast skeletal and cardiac muscle myosins were observed under rigor conditions (-Ca2+/+Ca2+). In the present work these studies have been extended to new more order-producing conditions (presence of ATP in the absence of Ca2+) aimed at arresting the relaxed structure in synthetic filaments of both fast and slow skeletal muscle myosin. Filaments were formed from column-purified myosins (rabbit fast skeletal muscle and rabbit slow skeletal semimebranosusproprius muscle). In the presence of 0.1 mM free Ca2+, 3 mM Mg2+ and 2 mM ATP (activating conditions) these filaments had a spread structure with a random arrangement of myosin heads and subfragments 2 protruding from the filament backbone. Such a structure is indistinguishable from the filament structures observed previously for fast skeletal, cardiac (see reference cited above) and smooth (Podlubnaya et al., 1999, J. Muscle Res. Cell Motil. 20, 547-554) muscle myosins in the presence of 0.1 mM free Ca2+. In the absence of Ca2+ and in the presence of ATP (relaxing conditions) the filaments of both studied myosins revealed a compact ordered structure. The fast skeletal muscle myosin filaments exhibited an axial periodicity of about 14.5 nm and which was much more pronounced than under rigor conditions in the absence of Ca2+ (see the first reference cited). The slow skeletal muscle myosin filaments differ slightly in their appearance from those of fast muscle as they exhibit mainly an axial repeat of about 43 nm while the 14.5 nm repeat is visible only in some regions. This may be a result of a slightly different structural properties of slow skeletal muscle myosin. We conclude that, like other filaments of vertebrate myosins, slow skeletal muscle myosin filaments also undergo the Ca2+-induced structural order-disorder transitions. It is very likely that all vertebrate muscle myosins possess such a property.

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Structure and function of fish fast skeletal muscle myosin light chains

Fisheries Science ◽

10.2331/fishsci.68.sup2_1499 ◽

2002 ◽

Vol 68 (sup2) ◽

pp. 1499-1502 ◽

Cited By ~ 1

Author(s):

SHOICHIRO ISHIZAKI ◽

YASUYUKI MASUDA ◽

MUNEHIKO TANAKA ◽

SHUGO WATABE

Keyword(s):

Skeletal Muscle ◽

Structure And Function ◽

Light Chains ◽

Myosin Light Chains ◽

Fast Skeletal Muscle ◽

Skeletal Muscle Myosin ◽

And Function ◽

Muscle Myosin

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Effects of pH on myofibrillar ATPase activity in fast and slow skeletal muscle fibers of the rabbit

Biophysical Journal ◽

10.1016/s0006-3495(94)80727-1 ◽

1994 ◽

Vol 67 (6) ◽

pp. 2404-2410 ◽

Cited By ~ 24

Author(s):

E.J. Potma ◽

I.A. van Graas ◽

G.J. Stienen

Keyword(s):

Skeletal Muscle ◽

Atpase Activity ◽

Muscle Fibers ◽

Myofibrillar Atpase ◽

Slow Skeletal Muscle ◽

Skeletal Muscle Fibers ◽

Myofibrillar Atpase Activity ◽

Effects Of Ph

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The expression of the regulatory myosin light chain 2 gene during mouse embryogenesis

Development ◽

10.1242/dev.118.3.919 ◽

1993 ◽

Vol 118 (3) ◽

pp. 919-929 ◽

Cited By ~ 1

Author(s):

A. Faerman ◽

M. Shani

Keyword(s):

Skeletal Muscle ◽

Light Chain ◽

Myosin Light Chain ◽

Fast Skeletal Muscle ◽

Mouse Embryogenesis ◽

Skeletal Muscle Myosin ◽

Adult Mice ◽

Regulatory Myosin Light Chain ◽

Myosin Light Chain 2 ◽

Muscle Groups

The fast skeletal muscle myosin light chain 2 (MLC2) gene is expressed specifically in skeletal muscles of newborn and adult mice, and has no detectable sequence homology with any of the other MLC genes including the slow cardiac MLC2 gene. The expression of the fast skeletal muscle MLC2 gene during early mouse embryogenesis was studied by in situ hybridization. Serial sections of embryos from 8.5 to 12.5 days post coitum (d.p.c.) were hybridized to MLC2 cRNA and to probes for the myogenic regulatory genes MyoD1 and myogenin. The results revealed different temporal and spatial patterns of hybridization for different muscle groups. MLC2 transcripts were first detected 9.5 d.p.c. in the myotomal regions of rostral somites, already expressing myogenin. Surprisingly, at the same stage, a weak MLC2 signal was also detected in the cardiomyocytes. The cardiac expression was transient and could not be detected at later stages while the myotomal signal persisted and spread to the more caudal somites, very similar to the expression of myogenin. Beginning from 10.5 d.p.c., several extramyotomal premuscle cells masses have been demarcated by MyoD1 expression. MLC2 transcripts were detected in only one of these cell masses. Although, transcripts of myogenin were detected in all these cell masses, the number of expressing cells was significantly lower than that observed for MyoD1. By 11.5 d.p.c., all three hybridization signals colocalized in most extramyotomal muscle-forming regions, with the exception of the diaphragm and the hindlimb buds, where only few cells expressed MLC2 and more cells expressed MyoD1 than myogenin. At 12.5 d.p.c., all three studied genes displayed a similar spatial pattern of expression in most muscle-forming regions. However, in some muscles, the MyoD1 signal spread over more cells compared to myogenin or MLC2. Our results are consistent with the suggestion that multiple myogenic programs exist for myoblasts differentiating in the myotome and extramyotomal regions.

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