Ventrolateral regionalization of Xenopus laevis mesoderm is characterized by the expression of alpha-smooth muscle actin

Development ◽  
1992 ◽  
Vol 115 (4) ◽  
pp. 1165-1173 ◽  
Author(s):  
J.P. Saint-Jeannet ◽  
G. Levi ◽  
J.M. Girault ◽  
V. Koteliansky ◽  
J.P. Thiery
Keyword(s):  
Smooth Muscle Actin ◽  
Smooth Muscles ◽  
Treated Animal ◽  
Mesoderm Induction ◽  
High Concentration ◽  
Alpha Smooth Muscle Actin ◽  
Lateral Plate ◽  
Amphibian Embryo ◽  
Actin Isoform ◽  
Actin Expression

Mesodermal patterning in the amphibian embryo has been extensively studied in its dorsal aspects, whereas little is known regarding its ventrolateral regionalization due to a lack of specific molecular markers for derivatives of this type of mesoderm. Since smooth muscles (SM) are thought to arise from lateral plate mesoderm, we have analyzed the expression of an alpha-actin isoform specific for SM with regard to mesoderm patterning. Using an antibody directed against alpha-SM actin that recognized specifically this actin isoform in Xenopus, we have found that the expression of alpha-SM actin is restricted to visceral and vascular SM with a transient expression in the heart. The overall expression of the alpha-SM actin appears restricted to the ventral aspects of the differentiating embryo. alpha-SM actin expression appears to be activated following mesoderm induction in animal cap derivatives. Moreover, at the gastrula stage, SM precursor cells are regionalized since they will only differentiate from ventrolateral marginal zone explants. Using the animal cap assay, we have found that alpha-SM actin expression is specifically induced in treated animal cap with bFGF or a low concentration of XTC-MIF, which induce ventral structures, but not with a high concentration of XTC-MIF, which induces dorsal structures. Altogether, these results establish that alpha-SM actin is a reliable marker for ventrolateral mesoderm. We discuss the importance of this novel marker in studying mesoderm regionalization.

scholarly journals Modulation of actin isoform expression before the transition from experimental compensated pressure-overload cardiac hypertrophy to decompensation

2009 ◽  
Vol 296 (5) ◽  
pp. H1625-H1632 ◽  
Author(s):  
Roberta Berni ◽  
Monia Savi ◽  
Leonardo Bocchi ◽  
Francesca Delucchi ◽  
Ezio Musso ◽  
...  
Keyword(s):  
Mechanical Performance ◽  
Smooth Muscle Actin ◽  
Pressure Overload ◽  
Calcium Transients ◽  
Alpha Smooth Muscle Actin ◽  
Aortic Banding ◽  
Lv Mass ◽  
Actin Isoform ◽  
Contraction And Relaxation ◽  
Kinetics Of

In a rat model of long-lasting pressure-overload hypertrophy, we investigated whether changes in the relative expression of myocardial actin isoforms are among the early signs of ventricular mechanical dysfunction before the transition toward decompensation. Forty-four rats with infrarenal aortic banding (AC rats) were studied. Hemodynamic parameters were measured 1 mo (AC1 group; n = 20) or 2 mo (AC2; n = 24) after aortic ligature. Then subgroups of AC1 and AC2 left ventricles (LV) were used to evaluate 1) LV anatomy and fibrosis (morphometry), 2) expression levels (immunoblotting) and spatial distribution (immunohistochemistry) of alpha-skeletal actin (α-SKA), alpha-cardiac actin (α-CA), and alpha-smooth muscle actin (α-SMA), and 3) cell mechanics and calcium transients in enzimatically isolated myocytes. Although the two AC groups exhibited a comparable degree of hypertrophy (+30% in LV mass; +20% in myocyte surface) and a similar increase in the amount of fibrosis compared with control animals (C group; n = 22), a worsening of LV mechanical performance was observed only in AC2 rats at both organ and cellular levels. Conversely, AC1 rats exhibited enhanced LV contractility and preserved cellular contractile behavior associated with increased calcium transients. Alpha-SKA expression was upregulated (+60%) in AC1. In AC2 ventricles, prolonged hypertension also induced a significant increase in α-SMA expression, mainly at the level of arterial vessels. No significant differences among groups were observed in α-CA expression. Our findings suggest that α-SKA expression regulation and wall remodeling of coronary arterioles participate in the development of impaired kinetics of contraction and relaxation in prolonged hypertension before the occurrence of marked histopathologic changes.

Isolation and characterization of six different chicken actin genes

1984 ◽  
Vol 4 (11) ◽  
pp. 2498-2508
Author(s):  
K S Chang ◽  
W E Zimmer ◽  
D J Bergsma ◽  
J B Dodgson ◽  
R J Schwartz
Keyword(s):  
Dna Sequences ◽  
Genomic Dna ◽  
Genomic Library ◽  
Smooth Muscle Actin ◽  
Actin Gene ◽  
Muscle Actin ◽  
Repeated Dna ◽  
Alpha Smooth Muscle Actin ◽  
Actin Genes ◽  
Actin Isoform

Genes representing six different actin isoforms were isolated from a chicken genomic library. Cloned actin cDNAs as well as tissue-specific mRNAs enriched in different actin species were used as hybridization probes to group individual actin genomic clones by their relative thermal stability. Restriction maps showed that these actin genes were derived from separate and nonoverlapping regions of genomic DNA. Of the six isolated genes, five included sequences from both the 5' and 3' ends of the actin-coding area. Amino acid sequence analysis from both the NH2- and COOH-terminal regions provided for the unequivocal identification of these genes. The striated isoforms were represented by the isolated alpha-skeletal, alpha-cardiac, and alpha-smooth muscle actin genes. The nonmuscle isoforms included the beta-cytoplasmic actin gene and an actin gene fragment which lacked the 5' coding and flanking sequence; presumably, this region of DNA was removed from this gene during construction of the genomic library. Unexpectedly, a third nonmuscle chicken actin gene was found which resembled the amphibian type 5 actin isoform (J. Vandekerckhove, W. W. Franke, and K. Weber, J. Mol. Biol., 152:413-426). This nonmuscle actin type has not been previously detected in warm-blooded vertebrates. We showed that interspersed, repeated DNA sequences closely flanked the alpha-skeletal, alpha-cardiac, beta-, and type 5-like actin genes. The repeated DNA sequences which surround the alpha-skeletal actin-coding regions were not related to repetitious DNA located on the other actin genes. Analysis of genomic DNA blots showed that the chicken actin multigene family was represented by 8 to 10 separate coding loci. The six isolated actin genes corresponded to 7 of 11 genomic EcoRI fragments. Only the alpha-smooth muscle actin gene was shown to be split by an EcoRI site. Thus, in the chicken genome each actin isoform appeared to be encoded by a single gene.

Alpha-smooth muscle actin expression enhances cell traction force

2007 ◽  
Vol 64 (4) ◽  
pp. 248-257 ◽  
Author(s):  
Jianxin Chen ◽  
Hongxia Li ◽  
Nirmala SundarRaj ◽  
James H.-C. Wang
Keyword(s):  
Smooth Muscle ◽  
Smooth Muscle Actin ◽  
Traction Force ◽  
Muscle Actin ◽  
Alpha Smooth Muscle Actin ◽  
Cell Traction ◽  
Actin Expression

Alpha-smooth muscle actin expression by fibroblasts is not a marker of hypertrophic scars in vitro

1998 ◽  
Vol 16 ◽  
pp. S129
Author(s):  
Gianni Gerlini ◽  
Francesca Prignano ◽  
Nicola Pimpinelli ◽  
Lorenzo Borgognoni ◽  
Umberto Maria Reali ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Smooth Muscle Actin ◽  
Muscle Actin ◽  
Hypertrophic Scars ◽  
Alpha Smooth Muscle Actin ◽  
Actin Expression

The hepatitis C virus core protein indirectly induces alpha-smooth muscle actin expression in hepatic stellate cells via interleukin-8

2010 ◽  
Vol 52 (5) ◽  
pp. 635-643 ◽  
Author(s):  
Sophie Clément ◽  
Stéphanie Pascarella ◽  
Stéphanie Conzelmann ◽  
Carmen Gonelle-Gispert ◽  
Kévin Guilloux ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Hepatitis C ◽  
Hepatic Stellate Cells ◽  
Core Protein ◽  
Smooth Muscle Actin ◽  
Stellate Cells ◽  
Muscle Actin ◽  
Alpha Smooth Muscle Actin ◽  
Virus Core ◽  
Actin Expression
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