Nucleotide sequence of a cDNA encoding the human muscle-specific enolase (MSE)

Calı̀, Larissa; Feo, Salvatore; Oliva, Daniele; Giallongo, Agata

doi:10.1093/nar/18.7.1893

Cited by 19 publications

(22 citation statements)

References 3 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…enolase which is expressed in muscle tissue. This was confirmed by cloning the corresponding cDNA from a human skeletal muscle library [16]. A partial restriction map of the 3, clone B.21, with a 21-kb insert of genomic DNA, is shown in Fig.…”

Section: Isolation and Nucleotide Sequence Analysis Of The J? Enolasementioning

confidence: 72%

“…The 3, clone, B.21, containing the longest insert of genomic DNA, was further characterized for restriction-cleavage sites and by Southern-blot analysis, according to standard procedures [15]. Different regions of the p enolase cDNA [16] were used as probes to locate 5' and 3' ends of the gene. DNA fragments spanning the entire p enolase gene were isolated from the B.21 3, phage and subcloned into the KS' or KSBluescript vectors (Stratagene).…”

Section: Materials and Methods Isolation And Nucleotide Sequencing Ofmentioning

confidence: 99%

“…1 pg poly(A)-rich RNA from human skeletal muscle was annealed with 20 pmol 20-nucleotide oligomer, 5'-GTGGCATCC'M'CCC-ATACTT-3', complementary to bases 622-641 of the previously reported cDNA sequence [16] and reverse transcribed with 10 U AMV reverse transcriptase (Boehringer). After removing the excess oligomer by passage through a 2-ml Bio-Gel A-5m column (Bio-Rad), the single-strand cDNA was tailed with terminal deoxynucleotidyl transferase (BRL) in the presence of dATP.…”

Section: Northern-blot Analysis and Rna Sequencingmentioning

confidence: 99%

“…After removing the excess oligomer by passage through a 2-ml Bio-Gel A-5m column (Bio-Rad), the single-strand cDNA was tailed with terminal deoxynucleotidyl transferase (BRL) in the presence of dATP. Polymerase-chain-reaction amplification was performed with 25 pmol adaptor, 5'-GACTCGA-GTCGACATCG-3', containing the XhoI, SuZI, and CZuI recognition sites, 10 pmol (dT),, adaptor, having the same sequence as that of the previous adaptor plus 17 T residues at the 3' end, and 25 pmol specific oligomer, 5'-CTTGAAGG-AGCTGGCTCCCA-3', complementary to bases 545 -564 of the human / 3 enolase cDNA [16], following the described procedure [21]. RACE products were digested with the restriction enzymes SuZI and BclI, whose recognition sites are present in the adaptor and in the p enolase sequence, respectively.…”

Section: Northern-blot Analysis and Rna Sequencingmentioning

confidence: 99%

“…DNA fragments were separated by agarose gel electrophoresis and specific products were isolated by glass elution [22], then cloned in a Bluescript vector (Stratagene). Plasmids containing / 3 enolase cDNA inserts were identified by colony-lift hybridization using, as probe, one of the previously isolated cDNA [16] corresponding to the 5' coding region of the mRNA. Further screening of these isolated clones was performed with the 5' end-labeled oligomer a (see Fig.…”

Section: Northern-blot Analysis and Rna Sequencingmentioning

confidence: 99%

See 4 more Smart Citations

Structural features of the human gene for muscle‐specific enolase

Giallongo

Venturella

Oliva

et al. 1993

European Journal of Biochemistry

Self Cite

View full text Add to dashboard Cite

We report here the isolation and characterization of the human gene for the p or muscle-specific isoform of the glycolytic enzyme enolase. The nucleotide sequence analysis revealed structural features, such as organization as 11 coding exons, the first exon consisting of an untranslated sequence and hence resembling sequences of the other two members of the gene family, the a and y enolase genes. The p enolase locus spans about 6 kbp genomic DNA. Sequences matching the consensus sequence for muscle-specific regulatory factors are present in the 5'-flanking region and within the first intron. A combination of primer extension, S1 nuclease protection and RNA-sequencing experiments indicates that the gene has a unique transcriptional start site, 26 bp downstream of a TATA-like box; the differential usage of two donor sites within the untranslated exon I generates two alternatively spliced transcripts. The existence of the two mRNA, differing from one another in the presence or absence of a 42-nucleotide fragment in the leader sequence, was confirmed by cloning the corresponding cDNA using the rapid amplification of cDNA ends strategy. Secondarystructure predictions indicated that the leader sequences of the spliced forms could form hairpin structures with different free energies of formation, suggesting translational control.

show abstract

Section: Isolation and Nucleotide Sequence Analysis Of The J? Enolasementioning

confidence: 72%

Section: Materials and Methods Isolation And Nucleotide Sequencing Ofmentioning

confidence: 99%

Section: Northern-blot Analysis and Rna Sequencingmentioning

confidence: 99%

Section: Northern-blot Analysis and Rna Sequencingmentioning

confidence: 99%

Section: Northern-blot Analysis and Rna Sequencingmentioning

confidence: 99%

See 3 more Smart Citations

Structural features of the human gene for muscle‐specific enolase

Giallongo

Venturella

Oliva

et al. 1993

European Journal of Biochemistry

Self Cite

View full text Add to dashboard Cite

show abstract

Purification and characterization of immunoglobulin production stimulating factor-II? derived from Namalwa cells

et al. 1992

View full text Add to dashboard Cite

Two immunoglobulin production stimulating factors (IPSF) have been found in human Burkitt's lymphoma Namalwa cells. One IPSF named IPSF-II alpha was purified and identified as glyceraldehyde-3-phosphate dehydrogenase as previously reported. We report here purification, identification and characterization of IPSF-II beta. IPSF-II beta was purified by the serial use of ammonium sulfate fractionation, hydrophobic interaction column chromatography, anion-exchange column chromatography and gel filtration. The IPSF-II beta was estimated as a 46 KD monomeric polypeptide by gel filtration and SDS-PAGE. Partial amino acid sequence of the 46 KD protein was analyzed for 26 amino acid residues. The sequence very closely coincided with enolase (EC 4.2.1.11) derived from various origins and, it was completely homologous with that of human enolase alpha-chain. Rabbit muscle enolase stimulated IgM production of hybridoma lines, and IPSF-II beta had the enzymic activity. These results suggested that IPSF-II beta was alpha-enolase or its isozyme. IPSF activities of IPSF-II beta was stable in alkaline conditions whereas the enzymic activity was rapidly lost in alkaline conditions. Though IPSF-II beta stimulated IgM production of both human-human and mouse-mouse hybridoma lines in serum-free condition, it partially suppressed IgE production of mouse-mouse hybridoma lines.

show abstract

Characterization of squid enolase mRNA: Sequence analysis, tissue distribution, and axonal localization

et al. 1995

View full text Add to dashboard Cite

Enolase is a glycolytic enzyme whose amino acid sequence is highly conserved across a wide range of animal species. In mammals, enolase is known to be a dimeric protein composed of distinct but closely related subunits: alpha (non-neuronal), beta (muscle-specific), and gamma (neuron-specific). However, little information is available on the primary sequence of enolase in invertebrates. Here we report the isolation of two overlapping cDNA clones and the putative primary structure of the enzyme from the squid (Loligo pealii) nervous system. The composite sequence of those cDNA clones is 1575 bp and contains the entire coding region (1302 bp), as well as 66 and 207 bp of 5' and 3' untranslated sequence, respectively. Cross-species comparison of enolase primary structure reveals that squid enolase shares over 70% sequence identity to vertebrate forms of the enzyme. The greatest degree of sequence similarity was manifest to the alpha isoform of the human homologue. Results of Northern analysis revealed a single 1.6 kb mRNA species, the relative abundance of which differs approximately 10-fold between various tissues. Interestingly, evidence derived from in situ hybridization and polymerase chain reaction experiments indicate that the mRNA encoding enolase is present in the squid giant axon.

show abstract

Nucleotide sequence of a cDNA encoding the human muscle-specific enolase (MSE)

Cited by 19 publications

References 3 publications

Structural features of the human gene for muscle‐specific enolase

Structural features of the human gene for muscle‐specific enolase

Purification and characterization of immunoglobulin production stimulating factor-II? derived from Namalwa cells

Characterization of squid enolase mRNA: Sequence analysis, tissue distribution, and axonal localization

Contact Info

Product

Resources

About