Disease relevance of ACTA1

• A modified CXL retrovirus was used to clone an antisense smooth muscle alpha-actin ribozyme sequence adjacent to the reporter lacZ sequence [1].
• These plasmids, as well as a recombinant plasmid derived from chick alpha-actin mRNA, were used as probes for the estimation of mRNA levels in polyribosomes and in small ribonucleoprotein (RNP) particles of the ascites cells [2].
• A transgenic mouse line harboring a smooth muscle alpha-actin promoter polyomavirus middle T antigen transgene develops an epithelial hyperplasia in the rectum and distal stomach [3].
• Serum response element 1 has previously been reported to be necessary and sufficient for activation of the skeletal alpha-actin promoter during hypertrophy of the anterior latissimus dorsi (ALD) muscle of roosters [J. A. Carson, R. J. Schwartz, and F. W. Booth. Am. J. Physiol. 270 (Cell Physiol. 39): C1624-C1633, 1996] [4].
• Similar changes have been reported for birds with nutritionally induced muscular dystrophy (Bartlett, M. W., Egelstaff, P. A., Holden, T. M., Stinson, R. H. and Sweeny, P. R. (1973) Biochim. Biophys. Acta 328, 213-220) [5].

High impact information on ACTA1

• One subpopulation recognizes gamma actins from smooth muscle and nonmuscle cells, but does not recognize alpha actin from skeletal muscle [6].
• The specific expression of the vascular smooth muscle alpha-actin gene marks the onset of differentiation of cardiac cells and represents the first demonstration of coexpression of both smooth muscle and striated alpha-actin genes within myogenic cells [7].
• This modulation in smooth muscle alpha-actin gene expression correlated with the beginning of coexpression of sarcomeric alpha-actin transcripts in the epimyocardium and the onset of circulation in the embryo [7].
• In myoblasts, the skeletal tropomyosin-enriched microfilaments had a higher content of alpha-actin and phosphorylated isoforms of tropomyosin as compared with the tropomyosin-enriched microfilaments [8].
• It has been demonstrated that embryonic chicken gizzard smooth muscle contains a unique embryonic myosin light chain of 23,000 mol wt, called L23 (Katoh, N., and S. Kubo, 1978, Biochem. Biophys. Acta, 535:401-411; Takano-Ohmuro, H., T. Obinata, T. Mikawa, and T. Masaki, 1983, J. Biochem. (Tokyo), 93:903-908) [9].

Biological context of ACTA1

• The complete nucleotide sequence of the chick a-actin gene and its evolutionary relationship to the actin gene family [10].
• The nucleotide sequence of the chick a-actin gene reveals that the gene is comprised of 7 exons separated by six very short intervening sequences (IVS) [10].
• The comparison of beta and alpha-actin revealed differences in the timing and relative rates of ATP hydrolysis and P(i)-release [11].
• A simple method to transfer, integrate and study expression of foreign genes, such as chicken ovalbumin and alpha-actin in plant tumors [12].
• The differential regulation of skeletal alpha-actin transcription was equivalent with either purified or recombinant FGFs and was observed with 5' flanking sequences from either nucleotide -202 or -2000 to nucleotide -11 [13].

Anatomical context of ACTA1

• Actins isolated from muscle tissue with a sarcomeric structure like skeletal muscle and heart muscle invariably display, as previously shown, one single band with a pI of approximately 5.4 (alpha-actin) in isoelectric focusing gels [14].
• At Hamburger-Hamilton stage 12, the smooth muscle alpha-actin gene was selectively down-regulated in the heart such that only the conus, which subsequently participates in the formation of the vascular trunks, continued to express this gene [7].
• Sequential activation of alpha-actin genes during avian cardiogenesis: vascular smooth muscle alpha-actin gene transcripts mark the onset of cardiomyocyte differentiation [7].
• The latter is absolutely dependent on the rise of intracellular Ca++, as reflected by the fact that Ca++-induced rounding of chicken erythrocytes always precedes fusion (Volsky, D. and A. Loyter. 1977.Biochim. Biophys. Acta 471:253--259) [15].
• We present evidence that an alpha-actin in CEF cultures, identified by its electrofocusing behavior, retention in the cytoskeleton, and DNase 1 binding properties, is selectively and dramatically reduced in amount upon transformation by RSV [16].

Associations of ACTA1 with chemical compounds

• Phosphoribosylpyrophosphate (PP-Rib-P) synthetase (EC 2.7.6.1) subunit I gene (PRPS1) is constitutively expressed in various tissues (Taira, M., Iizasa, T., Yamada, K., Shimada, H., and Tatibana, M. (1989) Biochim. Biophys. Acta 1007, 203-208) [17].
• Similar to other skeletal alpha-actin genes, the nucleotide sequence codes for two amino acids, Met-Cys, preceding the known N-terminal Asp of the mature protein [18].
• In this report we have constructed unidirectional 5'-deletion and region-specific deletion-insertion mutations of the chicken skeletal alpha-actin upstream region and inserted these into the chloramphenicol acetyltransferase expression vector pSV0CAT [19].
• Chicken liver purine nucleoside phosphorylase, a trimer of molecular weight 90,000, is assumed to contain subunits of two different molecular weights (Murakami, K., and Tsushima, K. (1976) Biochim. Biophys. Acta 453, 205-210) [20].
• Trinitrophenylation of the reactive lysine (Lys84) in skeletal myosin subfragment 1 (S1) introduces a chiral probe (TNP) into an interface of the catalytic and lever arm domains of S1 [Muhlrad (1977) Biochim. Biophys. Acta 493, 154-166] [21].

Other interactions of ACTA1

• Transforming growth factor-beta response elements of the skeletal alpha-actin gene. Combinatorial action of serum response factor, YY1, and the SV40 enhancer-binding protein, TEF-1 [22].
• Additionally, stretch-induced alterations in SRF binding to SRE1, from the skeletal alpha-actin promoter, occur regardless of the rate of stretch-induced growth [23].

Analytical, diagnostic and therapeutic context of ACTA1

• Double staining of beta-galactosidase and smooth muscle alpha-actin using immunohistochemistry revealed that single cells infected with the CXL/ribozyme showed little to no smooth muscle alpha-actin protein [1].
• This observation is also reflected by Northern blot analysis, which demonstrates a temporal coincidence in the increase of both alpha-actin and elastin mRNA levels [24].
• A high-resolution atomic force microscopy (AFM) study has shown that the molecular packing on the tetragonal lysozyme (110) face corresponds to only one of two possible packing arrangements, suggesting that growth layers on this face are of bimolecular height [Li et al. (1999). Acta Cryst. D55, 1023-1035] [25].
• Gel mobility shift assays demonstrated that SRF binding with serum response element 1 of the skeletal alpha-actin promoter had no altered binding patterns from 6-day-stretched Pat nuclear extracts [26].
• An isolation procedure for synaptic plasma membranes from whole chick brain is reported that uses the combined flotation-sedimentation density gradient centrifugation procedure described by Jones and Matus (Jones, D. H. and Matus, A. I. (1974) Biochim. Biophys. Acta 356, 276-287) for rat brain [27].

References