Human aldolase isozyme gene: the structure of multispecies aldolase B mRNAs

Sakakibara, Masahiro; Mukai, Tsunehiro; Yatsuki, Hitomi; Hori, Katsuji

doi:10.1093/nar/13.14.5055

Cited by 38 publications

(24 citation statements)

References 30 publications

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“…2), is identical as far as the amino acid sequence is concerned, with the sequence deduced from human liver cDNA [14] and the partial sequence of human muscle protein [30].…”

Section: T G C C a G C G A G T C C C T C T T C G T C T C T A A C C mentioning

confidence: 93%

“…1 shows the restriction map of clone McDA2 and the strategy used to obtain the complete sequence of the cloned insert. The identification of the characterized clone with aldolase A cDNA is based on amino acid homology with the known rabbit aldolase A translated inRNA (97%, see [12]), the partial protein sequence of human muscle aldolase A (loo%, see [30]) and the more recently published rat (97%, see [13]) and human liver (100%) aldolase A mRNA [14]. Lower amino acid homology was evident with known aldolase B mRNA sequences (69Y0, see [4,7,91) and with partial aldolase C mRNA sequences (84%, see [5]).…”

Section: Isolation and Characterization Of C D N A Clonesmentioning

confidence: 99%

“…The data obtained in rat support a multiplicity of mRNA for aldolase A and its tissue-specific patterns. Until now only one human mRNA sequence has been reported [14] and that was obtained from a liver cDNA library.In this paper we report the nucleotide sequence of a new human aldolase A mRNA, obtained from a fibroblast cDNA library. The sequence analysis of the 5'-non-coding region and its comparison with other known sequences demonstrate the multiplicity of aldolase A mRNA in man.…”

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confidence: 99%

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confidence: 99%

“…The muscle-type aldolase A has been studied at the mRNA level in rabbit [12], and more recently in rat [13] and in man [14,151. The data obtained in rat support a multiplicity of mRNA for aldolase A and its tissue-specific patterns.…”

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confidence: 99%

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A new human species of aldolase A mRNA from fibroblasts

et al. 1987

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A full-length cDNA aldolase A clone was isolated from a human fibroblast cDNA library and completely sequenced. Excluding the poly(A) tail, the clone covers 1095 base pairs (bp) bf the coding region, plus 199 bp downstream for the termination codon and 146 bp upstream for the initiation codon, within a total of 1440 bp.Primer extension experiments performed with human cultured fibroblast mRNA indicate an elongated product of a further 40 bp. These results evaluated together with those obtained in a concurrent study concerning aldolase A mRNA isolated from human liver are direct evidence of aldolase A mRNA multiplicity in man. The data also suggest the existence in mammals of three different classes of aldolase A mRNA, which would account for tissue specificity and resurgence of foetal expression in tumors.Three tissue-specific aldolase isoenzymes (A, B and C) are found in higher organisms [l]. At least three distinct genes code for these isoenzymes. The aldolase isoenzyme system (see [l, 21 for reviews) lends itself to the study of the tissuespecific and developmental regulatory mechanisms of gene expression and can provide information on some aspects of molecular evolution. Furthermore, diseases related to alterations at the gene level, such as hereditary fructose intolerance [3], may be studied via the analysis of such alterations.Within the framework of a study of the aldolase system, we have completely sequenced a full-length cDNA for human liver aldolase B [4] and a partial cDNA for mouse brain aldolase C [5]. Other groups have elucidated the mRNA structure and expression of aldolase B in rat [6] and in humans [7 -91, and have described the aldolase B gene organization and structure in chicken [lo] and in rat [ll].The muscle-type aldolase A has been studied at the mRNA level in rabbit [12], and more recently in rat [13] and in man [14, 151. The data obtained in rat support a multiplicity of mRNA for aldolase A and its tissue-specific patterns. Until now only one human mRNA sequence has been reported [14] and that was obtained from a liver cDNA library.In this paper we report the nucleotide sequence of a new human aldolase A mRNA, obtained from a fibroblast cDNA library. The sequence analysis of the 5'-non-coding region and its comparison with other known sequences demonstrate the multiplicity of aldolase A mRNA in man.Correspondence to F. Salvatore, Istituto di Scienze Biochimiche, I1 Facolta di Medicina e Chirurgia, Universita degli Studi di Napoli, Via Sergio Pansini, $1-80131 Napoli, ItalyAbbreviations. bp, base pairs in DNA; SSC, standard saline citrate, i.e. 0.15 M NaC1, 0.015 M sodium citrate, pH 7.0; ssDNA, single-stranded DNA; dsDNA, double-stranded DNA.Enzyme. Fructose-1,6-bisphosphate aldolase (EC 4.1.2.13). MATERIALS AND METHODS Mu teriulsChemicals were from Sigma, Merck or Serva. All the radionuclides, M13 primers and restriction enzymes were supplied by Amersham International plc (UK), AMV reverse transcriptase was from Boehringer Mannheim, deoxynucleotides were from P-L Biochemia Inc. (Milwau...

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“…2), is identical as far as the amino acid sequence is concerned, with the sequence deduced from human liver cDNA [14] and the partial sequence of human muscle protein [30].…”

Section: T G C C a G C G A G T C C C T C T T C G T C T C T A A C C mentioning

confidence: 93%

Section: Isolation and Characterization Of C D N A Clonesmentioning

confidence: 99%

mentioning

confidence: 99%

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confidence: 99%

mentioning

confidence: 99%

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A new human species of aldolase A mRNA from fibroblasts

et al. 1987

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Recent progress in the molecular genetic analysis of erythroenzymopathy

Fujii¹,

Shiro²

1990

American J Hematol

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During the relatively recent period in which normal genes for most red cell enzymes have been isolated, the techniques of molecular biology have been applied to the studies of erythroenzymopathy. Single nucleotide substitutions have been identified in aldolase, triosephosphate isomerase, glucose 6-phosphate dehydrogenase, and adenylate kinase variants by the cloning and nucleotide sequence of the patients' genes. Up to now, all of the enzyme-deficient variants which have been investigated have been caused by point mutations. An exception is a hemolytic anemia secondary to increased adenosine deaminase (ADA) activity. Red cell ADA activity increases on the order of a hundred-fold in affected individuals. The basic abnormality appears to result from overproduction of structurally normal enzyme due to abnormal transcriptional or translational efficiency.

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