Characterization of muscle actin genes in Drosophila virilis reveals significant molecular complexity in skeletal muscle types

2001 ◽  
Vol 10 (4) ◽  
pp. 333-340 ◽  
Author(s):  
T. L. Lovato ◽  
S. M. Meadows ◽  
P. W. Baker ◽  
J. C. Sparrow ◽  
R. M. Cripps
2015 ◽  
Vol 87 (4) ◽  
pp. 2055-2066 ◽  
Author(s):  
FERNANDA A. ALVES-COSTA ◽  
MAELI D.P. SILVA ◽  
ADRIANE P. WASKO

RESUMO Dois genes de α-actina do peixe Leporinus macrocephalus, referindo-se aos tecidos musculares branco e vermelho, foram isolados. Isoformas de actinas, que principalmente diferiram por uma substituição Ser/Ala155, podem ter uma significância funcional relacionada à interação entre actina e ATP. Um resíduo de Ala155, como observado na α-actina esquelética do músculo vermelho, resulta em uma diminuição da afinidade da actina pelo ATP, o que também pode estar associado à ação contrátil lenta desse tecido. Adicionalmente, uma substituição Phe/Ile262 na actina do músculo vermelho leva a uma variação na hidrofobicidade no "plug-D" da proteína, o que pode alterar sua estabilidade. Dados de qRT-PCR evidenciaram significante maior nível de actina RNAm em músculo branco, quando comparado ao músculo vermelho (T=105 Mann Whitney; p=<0,001). Este resultado pode estar relacionado às demandas energéticas do tecido muscular branco, com fibras de contração rápida e metabolismo glicolítico para fornecimento de energia. Os dados disponíveis sobre actinas musculares levam a propor que as α-actinas esqueléticas dos músculos branco e vermelho são geneticamente e funcionalmente distinguíveis em espécies de peixes, uma característica não encontrada em outros grupos de vertebrados.


Development ◽  
1985 ◽  
Vol 89 (Supplement) ◽  
pp. 125-136
Author(s):  
J. B. Gurdon ◽  
T. J. Mohun ◽  
S. Brennan ◽  
S. Cascio

The results summarized here have established the temporal and regional activation of three kinds of Xenopus actin genes. The cardiac and skeletal muscle actin genes are among the first cell-type-specific genes to be expressed in early development. The first transcripts to be synthesized by these genes appear to be correctly initiated, spliced, and at once translated into proteins. Both cardiac and skeletal actin genes are strongly transcribed in the axial skeletal muscle of embryos. The mechanism by which the cardiac actin gene is first transcribed in only the somite region of an embryo depends, at least in part, on materials already localized in the subequatorial region of a fertilized but uncleaved egg. Cells which acquire this material seem able to activate their cardiac actin genes without requiring normal contact with other cells.


1991 ◽  
Vol 260 (1) ◽  
pp. E1-E7 ◽  
Author(s):  
S. Azhar ◽  
J. C. Butte ◽  
R. F. Santos ◽  
C. E. Mondon ◽  
G. M. Reaven

We have examined insulin binding, autophosphorylation, and tyrosine kinase activity in detergent-solubilized and wheat germ agglutinin-purified insulin receptor preparations from four rat muscles of different fiber composition (i.e., tensor fascia latae, soleus, vastus intermedius, and plantaris). Insulin binding activity was similar in three of the four muscles but lower in tensor fascia latae. No significant differences were noted in the affinity of insulin for its receptor from various muscle types. Insulin receptor tyrosine kinase activity measured in the absence (basal) and presence of insulin (0.3-300 nM) was comparable in all muscle types (normalized to the amount of insulin bound). Insulin sensitivity, measured as the dose of insulin required for half-maximal activation of kinase activity, was also similar in all muscle types. Likewise, incubation of receptor preparations with [gamma-32P]ATP, Mn2+, and insulin (0.25-100 nM) resulted in a dose-dependent autophosphorylation of the beta-subunit (relative molecular weight approximately 95 kDa) with similar kinetics in all muscle types. In conclusion, these results show that the functional behavior of the insulin receptor autophosphorylation-kinase system (in vitro) is not changed by alterations in muscle fiber composition, indicating that differences in insulin sensitivity between different skeletal muscle types is probably not due to modulation of the insulin receptor phosphorylation system.


1985 ◽  
Vol 228 (2) ◽  
pp. 433-441 ◽  
Author(s):  
J C Cavadore ◽  
C Axelrud-Cavadore ◽  
P Berta ◽  
M C Harricane ◽  
J Haiech

A functional vascular smooth-muscle actin from bovine aorta was purified to homogeneity by an original method and was able to polymerize. Aortic actin is composed of two major isoforms and at least two minor ones. This actin was not phosphorylated by either cyclic AMP-dependent protein kinase or C kinase. The physical properties of aortic actin were found to be very similar to those of skeletal-muscle actin, except for amino acid composition (three tryptophan residues instead of four). The aortic actin and skeletal-muscle actin differ in the extent of activation of the Mg-dependent ATPase of skeletal-muscle myosin.


1998 ◽  
Vol 274 (6) ◽  
pp. E1018-E1026 ◽  
Author(s):  
Fadia Haddad ◽  
Anqi X. Qin ◽  
Samuel A. McCue ◽  
Kenneth M. Baldwin

This study examined nuclear thyroid receptor (TR) maximum binding capacity (Bmax), dissociation constant ( K d), and TR isoform (α1, α2, β1) mRNA expression in rodent cardiac, “fast-twitch white,” “fast-twitch red,” and “slow-twitch red” muscle types as a function of thyroid state. These analyses were performed in the context of slow-twitch type I myosin heavy-chain (MHC) expression, a 3,5,3′-triiodothyronine (T3)-regulated gene that displays varying responsiveness to T3 in the above tissues. Nuclear T3 binding analyses show that the skeletal muscle types express more TRs per unit DNA than cardiac muscle, whereas the latter has a lower K d than the former. Altered thyroid state had little effect on either cardiac Bmax or K d, whereas hypothyroidism increased Bmax in the skeletal muscle types without affecting its K d. Cardiac muscle demonstrated the greatest mRNA signal of TR-β1 compared with the other muscle types, whereas the TR-α1mRNA signals were more abundant in the skeletal muscle types, especially fast-twitch red. Hyperthyroidism increased the ratio of β1 to α1 and decreased the ratio of α2- to α1+β1-mRNA signal across the muscle types, whereas hypothyroidism caused the opposite effects. The nuclear T3affinity correlated significantly with the TR-β1 mRNA expression but not with TR-α1 mRNA expression. Collectively, these findings suggest that, despite a divergent pattern of TR mRNA expression in the different muscle types, these patterns follow similar qualitative changes under altered thyroid state. Furthermore, TR expression pattern cannot account for the quantitative and qualitative changes in type I MHC expression that occur in the different muscle types.


DNA ◽  
1986 ◽  
Vol 5 (3) ◽  
pp. 235-238 ◽  
Author(s):  
DAVID P. LEADER ◽  
IRENE GALL ◽  
PAUL CAMPBELL ◽  
ANNA MARIA FRISCHAUF

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