Regulation of muscle differentiation: cloning of sequences from .alpha.-actin messenger ribonucleic acid

Schwartz, Robert J.; Haron, Jay A.; Rothblum, Katrina; Dugaiczyk, Achilles

doi:10.1021/bi00566a034

Cited by 106 publications

(64 citation statements)

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“…Studies of globin (3), vitellogenin (50), and chorion (43) gene families have shown that a melting temperature difference of 5°C or more would help to discriminate between related nucleic acid sequences. Previously, we showed that a melting temperature difference of 10 to 13°C exists between chicken askeletal actin cDNA and that of ,B-, -y-, and smooth muscle actin mRNA (39,41). Whereas these differences in nucleic acid homology allowed us to develop stringent hybridization conditions to quantitate actin mRNA species during myogenesis in culture (41), it also provided a rationale in the present study for grouping homologous actin genes.…”

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confidence: 89%

“…Two additional actin isoforms termed I and -y are distributed as cytoskeletal proteins in most nonmuscle cells. Both cytoplasmic actins contain 25 amino acid substitutions when compared with a-skeletal actin (47), and at the nucleic acid level these actins display the greatest sequence divergence among the known actin isoforms (39,41).…”

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confidence: 99%

“…The purified nuclei were suspended in a buffer containing 10 mM Tris-hydrochloride (pH 7.5), 10 mM NaCl, and 3 mM Na2-EDTA plus 0.5% SDS and then digested with proteinase K (50 ,ug/ml). The were constructed and characterized as described by Schwartz et al (39). A recombinant DNA clone containing a large portion of the chicken ,B-actin-coding sequence, pAl, was a generous gift from D. Cleveland (6).…”

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confidence: 99%

“…Restriction fragments containing the 5' actin-coding regions were detected by Southern blot hybridization with a 5'-specific probe containing 100 nucleotides of the actin-coding region and 300 nucleotides of the 5'-noncoding promoter region of the a-skeletal actin gene XAC5. The 3' portions of the actin-coding regions were detected with the use of a short actin cDNA clone, pAC51 (39). The following restriction enzymes, as well as those in Fig.…”

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Isolation and characterization of six different chicken actin genes.

Chang¹,

Zimmer²,

Bergsma³

et al. 1984

Mol. Cell. Biol.

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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 ft-skeletal, at-cardiac, and ft-smooth muscle actin genes. The nonmuscle isoforms included the ,I-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.,. This nonmuscle actin type has not been previously detected in warm-blooded vertebrates. We showed that interspersed, repeated DNA sequences closely flanked the ft-skeletal, ft-cardiac, II-, and type 5-like actin genes. The repeated DNA sequences which surround the f-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 ft-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.

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Isolation and characterization of six different chicken actin genes.

Chang¹,

Zimmer²,

Bergsma³

et al. 1984

Mol. Cell. Biol.

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“…Gel retardation assays detected AP-1 bind- Northern blotting was performed as described previously [12]. DNA probes specific to c-jun (an EcoRI fragment of pJac7) [13], MyoD (an EcoRI fragment of pVZCIIcc) [14], myogenin (an EcoRI fragment of pUC65-20) [15], actin (linearized plasmid p AC 269) [16] and glyceraldehyde-3-phosphate dehydrogenase (linearized plasmid pRGAPDH13) [17] were used for hybridizations. Synthetic oligodeoxynucleotides were used for fast troponin C (5'~CTCAGCCTGTT-GGTCCGT-3') and fast troponin T (5'-TTCCTCGTCAGACAT-3') hybridizations.…”

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Expression of c‐jun/AP‐1 during myogenic differentiation in mouse C₂C₁₂ myoblasts

1993

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Mitogen withdrawal triggers myogenic differentiation in skeletal myoblasts in culture. We have examined the expression of the proto‐oncogene c‐jun during this process in mouse C2C12 myoblasts. c‐jun belongs to a family of immediate early genes whose expression is activated in cultured cells in response to the addition of serum growth factors. Interestingly, expression of c‐jun was maintained in mouse C2C12 and rat L6 myoblasts undergoing myogenic differentiation under low‐serum conditions. Previously it has been reported that expression of c‐jun is downregulated during differentiation of C2 cells. However, our results using C2C12 cells, a subclone of the C2 line, show that c‐jun mRNA, protein and the activator‐protein 1 (AP‐1) DNA‐binding activity were easily detected in proliferating myoblasts and differentiated myotubes. Although overexpression of c‐jun has been shown to block myogenic differentiation in C2 cells, results presented here suggest that expression of c‐jun at physiological levels may not interfere with skeletal myogenesis.

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Post‐translational incorporation of actin into myofibrils in vitro: Evidence for isoform specificity

Peng

Fischman

1991

Cell Motil. Cytoskeleton

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The incorporation of actin into myofibrils has been examined in a cell-free system [Bouché et al.: Journal of Cell Biology 107:587-596, 1988; Goldfine et al.: Cellular and Molecular Biology of Muscle Development, 1989]. Actin was translated in a reticulocyte lysate in the presence of 35S-methionine (35S-actin) or purified from muscle and labeled with fluorescein-5-isothiocyanate (FITC-actin). Myofibrils were incubated with either 35S-actin or FITC-actin and then analyzed by gel electrophoresis or fluorescence microscopy. When myofibrils were incubated with FITC-actin monomer in the reticulocyte lysate buffer, strong fluorescent labeling was observed in Z-band regions and less so in I-bands. No fluorescence was detected in non-overlap regions of A-bands. Confocal microscopic analysis of these myofibrils indicated that FITC-actin was distributed evenly across the diameter of the myofibrils. These observations suggest that actin incorporation in the reticulocyte lysate buffer occurred at sites in the sarcomere which contain actin. In contrast, FITC-actin showed a variety of non-physiological incorporation patterns when incubated with myofibrils in the presence of an isotonic buffer (I-buffer). However, when ATP was added to I-buffer, FITC-actin showed a pattern of incorporation into myofibrils similar to that seen in the reticulocyte lysate buffer. Immunoblots indicated that actin of native size was released from myofibrils during incubation in the reticulocyte lysate buffer. No actin release was detected when the myofibrils were incubated in I-buffer lacking ATP. We used this system to compare the incorporation of actin isoforms into myofibrils. Both alpha- and beta-actins exhibited incorporation into the myofibrils but there was a three-fold greater incorporation of the alpha isoform. We propose that the differential affinities of actin isoforms for myofibrils and other cytoskeletal structures could provide a mechanism for actin isoform targeting within the cytoplasm.

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Regulation of muscle differentiation: cloning of sequences from .alpha.-actin messenger ribonucleic acid

Cited by 106 publications

References 40 publications

Isolation and characterization of six different chicken actin genes.

Isolation and characterization of six different chicken actin genes.

Expression of c‐jun/AP‐1 during myogenic differentiation in mouse C₂C₁₂ myoblasts

Post‐translational incorporation of actin into myofibrils in vitro: Evidence for isoform specificity

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Regulation of muscle differentiation: cloning of sequences from .alpha.-actin messenger ribonucleic acid

Cited by 106 publications

References 40 publications

Isolation and characterization of six different chicken actin genes.

Isolation and characterization of six different chicken actin genes.

Expression of c‐jun/AP‐1 during myogenic differentiation in mouse C2C12 myoblasts

Post‐translational incorporation of actin into myofibrils in vitro: Evidence for isoform specificity

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Expression of c‐jun/AP‐1 during myogenic differentiation in mouse C₂C₁₂ myoblasts