Multiple CArG Boxes in the Human Cardiac Actin Gene Promoter Required for Expression in Embryonic Cardiac Muscle Cells Developing In Vitro from Embryonal Carcinoma Cells

Pari, Giovanna; Jardine, Karen; McBurney, Michael W.

doi:10.1128/mcb.11.9.4796-4803.1991

Cited by 6 publications

(7 citation statements)

References 68 publications

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“…The /3-actin control probe detected an mRNA of approximately 2 kb in each lane. As previously reported, a smaller form of /3-actin mRNA was also present in heart and skeletal muscle (Lamballe et al, 1991;Pari et al, 1991). The murine and human HCII transcripts were both approximately 2.2-2.3 kb in length (Figure 7).…”

Section: Quantification Of Dermatan Sulfate Cofactor In Murinesupporting

confidence: 77%

Murine Heparin Cofactor II: Purification, cDNA Sequence, Expression, and Gene Structure

et al. 1994

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Heparin cofactor II (HCII) is a glycoprotein in human plasma that inhibits thrombin rapidly in the presence of dermatan sulfate or heparin. Unexpectedly, we found that HCII activity in murine plasma is present in two proteins of 68 and 72 kDa. The two proteins have the same N-terminal amino acid sequence, and both react with an antibody raised against the C-terminal nine amino acid residues of murine HCII predicted from the cDNA sequence. Treatment of the two proteins with peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase yields a single 54-kDa band. Thus, murine plasma contains two forms of HCII that appear to have identical amino acid sequences but differ in the composition of their N-linked oligosaccharides. HCII cDNA clones isolated from a murine liver library include a 1434 bp open reading frame following the first Met codon, a TAA stop codon, and 580 bp of 3'-untranslated sequence terminating in a poly(A) tail. The amino acid sequence deduced from the cDNA contains the N-terminal sequence of purified murine plasma HCII preceded by a 23-residue hydrophobic sequence presumed to be the signal peptide. The amino acid sequence of murine HCII is 87% identical to that of human HCII, the greatest variability occurring in the N-terminal portion of the protein. Northern blot analysis reveals a 2.3-kb HCII mRNA in murine and human liver, but no HCII mRNA is detectable in heart, brain, spleen, lung, skeletal muscle, kidney, testis, placenta, pancreas, or intestine. Southern blot analysis of restriction fragment length polymorphisms in progeny on interspecific and intersubspecific crosses indicates that mice have a single HCII gene (designated Hcf2), which maps to chromosome 16 between Prm-1 and Igl. The murine HCII gene is approximately 7.1 kb in size and consists of at least four exons and three introns. The intron/exon organization is identical to that of the human HCII gene except at the 5' end, where the murine gene may lack a large intron in the 5'-untranslated region. Our results indicate that HCII is more highly conserved than the human and murine homologues of other serpins such as alpha 1-antitrypsin and alpha 1-antichymotrypsin.

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Section: Quantification Of Dermatan Sulfate Cofactor In Murinesupporting

confidence: 77%

Murine Heparin Cofactor II: Purification, cDNA Sequence, Expression, and Gene Structure

et al. 1994

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“…An alternative mechanism by which a gene could be expressed both in skeletal and in cardiac muscle is that a cardiac-specific factor could recognize and bind to the MyoD regulatory element. Analysis of the human cardiac a-actin promotor reveals that the sequences essential for expression in cardiac myocytes are similar to those implicated in MyoD-induced enhancement, suggesting that cardiac muscle might contain a MyoD-like activity (Pari et al, 1991). That two different factors could bind to the same consensus sequence has been observed for the basic helix-loop-helix (bHLH) family of transcriptional proteins (Weintraub et al, 1991).…”

Section: Discussionmentioning

confidence: 92%

Structure and organization of the heart isoform gene for bovine cytochrome c oxidase subunit VIIa

Seelan¹,

Li²

1992

Biochemistry

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Mammalian cytochrome c oxidase (COX) is a 13-subunit polypeptide complex that contains 10 subunits coded by the nucleus and 3 by the mitochondria. The nuclear-encoded subunits, though of unknown function, are presumed to play a regulatory role. Three of these (subunits VIa, VIIa, and VIII) generally exist in one of two isoforms--a constitutive (L) isoform or a skeletal muscle/heart-specific (H) isoform. To study the regulation, and possibly function, of these isoforms, we have begun characterizing the genes. In this paper we describe the isolation and characterization of the gene for the bovine COX VIIa-H isoform. The gene consists of four exons spanning 1.58 kb and is associated with a CpG island. There are no canonical TATA or CCAAT boxes immediately upstream of the transcription start site. Putative DNA sequence elements associated with respiratory function, muscle gene activation, and housekeeping function are present both in the upstream regions and within introns.

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“…The cells were selected in puromycin. The CA promoter is normally active only in muscle cells but is activated by MyoD in nonmuscle cells (37,49). Thus, only P19[MyoD] cells should contain active CA promoters and become puromycin resistant.…”

Section: Resultsmentioning

confidence: 99%

“…Previous work has shown that expression of transcripts encoding MyoD did not induce myogenesis in P19 cells (37). In this study, we have examined how the ectopic expression of MyoD affects the developmental potential of P19 cells.…”

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confidence: 93%

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Cellular Aggregation Enhances MyoD-Directed Skeletal Myogenesis in Embryonal Carcinoma Cells

Skerjanc

Slack

McBurney

1994

Molecular and Cellular Biology

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When introduced into P19 embryonal carcinoma cells, recombinant genes encoding MyoD converted only a small percentage (< 3%) of the transfected cells into skeletal muscle. We isolated stably transfected cells that expressed the MyoD transcript. These P19[MyoD] cells continued to express markers characteristic of undifferentiated stem cells but also expressed myf-5 and the myotonic dystrophy kinase, transcripts normally present in myoblasts but absent from P19 cells. Aggregation of P19[MyoD] cells induced the expression of myogenin, desmin, and the retinoblastoma protein and resulted in the rapid and abundant development of skeletal muscle. Both the embryonic and the slow isoforms of myosin heavy chain were present in this muscle, indicating that it resembled skeletal muscle formed from primary myoblasts. Since aggregation of P19 cells normally results in inefficient differentiation and the development of only low levels of cardiac muscle but no skeletal muscle, we conclude that MyoD imposes the skeletal muscle program on P19 cells and that the differentiation of these cells requires inductive events provided by cell aggregation.

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Multiple CArG Boxes in the Human Cardiac Actin Gene Promoter Required for Expression in Embryonic Cardiac Muscle Cells Developing In Vitro from Embryonal Carcinoma Cells

Cited by 6 publications

References 68 publications

Murine Heparin Cofactor II: Purification, cDNA Sequence, Expression, and Gene Structure

Murine Heparin Cofactor II: Purification, cDNA Sequence, Expression, and Gene Structure

Structure and organization of the heart isoform gene for bovine cytochrome c oxidase subunit VIIa

Cellular Aggregation Enhances MyoD-Directed Skeletal Myogenesis in Embryonal Carcinoma Cells

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