Complete deficiency of AMP deaminase in human erythrocytes

Ogasawara, Nagahisa; Goto, Haruko; Yamada, Yasukazu; Nishigaki, Itsuro; Itoh, T.; Hasegawa, I

doi:10.1016/0006-291x(84)91239-7

Cited by 43 publications

(26 citation statements)

References 8 publications

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“…The enzyme activity determined in healthy subjects using the method described is identical to that reported previously using assays monitoring ammonia production at 30 "C (500-750 nmol/h/mg Hb), allowing for the differences in incubation temperature (Ogasawara et al, 1984(Ogasawara et al, , 1987Zydowo et al, 1989). Our value is also comparable with the activity of 740 nmol/h/mg Hb found by Dale (1989) at 37°C using a radioisotopic assay.…”

Section: Discussionsupporting

confidence: 87%

“…Analysis of inherited purine disorders in humans has demonstrated the existence of an isolated deficiency of the skeletal muscle isoform with normal activity in other tissues (Fishbein, 1985). Recently, several subjects with a very low activity of erythrocyte AMP-deaminase have been described and assumed to represent a separate erythrocyte isoenzyme deficiency (Ogasawara et al, 1984(Ogasawara et al, , 1987Zydowo et al, 1989).…”

Section: Introductionmentioning

confidence: 99%

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A high performance liquid chromatographic assay for AMP‐deaminase activity in the erythrocytes of healthy subjects and patients with inherited purine disorders

Smolenski

Montero

Rodgers

et al. 1991

Biomedical Chromatography

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A novel method for measuring AMP-deaminase activity in human erythrocytes is presented, based on the determination of the reaction product, IMP, using high performance liquid chromatography. IMP formation was found to be proportional both to the incubation time and the amount of haemolysate over a wide range. The minimal detectable AMP-deaminase activity was more than 1000 times lower than the mean activity found in healthy controls (1083 nmol/h/mg Hb). No marked difference of activity was found in the patients with the following inherited purine disorders: familial juvenile gouty nephropathy and deficiencies of adenosine deaminase, hypoxanthine-guanine phosphoribosyltransferase or adenine phosphoribosyltransferase. The activity in the erythrocytes of patients with chronic renal failure was also similar to controls. The existence of subjects with low erythrocyte AMP-deaminase activity in the population has been confirmed.

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Section: Discussionsupporting

confidence: 87%

Section: Introductionmentioning

confidence: 99%

A high performance liquid chromatographic assay for AMP‐deaminase activity in the erythrocytes of healthy subjects and patients with inherited purine disorders

Smolenski

Montero

Rodgers

et al. 1991

Biomedical Chromatography

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“…Transcription of the AMPD2 gene can generate several N-terminal variants of the isoenzyme (Van den Bergh and Sabina, 1995). Gene AMPD3 (Mahnke-Zizelman and encodes for the isoenzymes E1 and E2 that were reported to be missing in an inherited erythrocyte deficiency (Ogasawara et al, 1984). The abundance of the multiple transcripts from the AMPD3 gene is developmentally regulated in skeletal muscle and liver (Mahnke-Zizelmann et al, 1997).…”

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confidence: 99%

AMP deaminase in rat brain: Localization in neurons and ependymal cells

Knecht

Wiesmüller

Gnau

et al. 2001

J of Neuroscience Research

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The purine nucleotide cycle enzyme AMP deaminase (AMPD) catalyzes the irreversible hydrolytic deamination of AMP. The physiological function of the purine nucleotide cycle in the brain is unknown. In situ hybridization and immunocytochemical studies were performed to identify the regional and cellular expression of AMPD in rat brain with the goal of elucidating the neural function of the purine nucleotide cycle. AMPD messenger RNA was detected in ventricular ependymal cells and cells of the choroid plexus and in neurons of distinct brain areas. Although only low antibody titers were obtained by immunization with the purified sheep brain AMPD, immunization of mice with synthetic lipopeptide vaccines containing oligopeptides derived from a known partial complementary DNA sequence of the enzyme yielded an antiserum suitable for immunocytochemistry. Immunostaining of cells in culture showed that neurons but not astroglial cells express appreciable amounts of the enzyme. Results of immunocytochemical staining performed on rat brain slices were in accord with the localization of AMPD messenger RNA, thus confirming the expression of AMPD in neurons of the brain stem, hippocampus, cerebellar nuclei and mesencephalic nuclei, as well as in ventricular ependymal cells and their cilia.

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“…Two clinical phenotypes of inherited AMPD deficiency have been described in humans. Homozygous deficiency of AMPD activity restricted to erythrocytes has been estimated to have a frequency of -0.03% in Japanese, Chinese, and Koreans (21). Deficiency of AMPD restricted to skeletal muscle is a common cause of inherited metabolic myopathy in the United States and Europe (30), and the latter phenotype is presumably a consequence of mutations in the AMPDJ gene.…”

mentioning

confidence: 99%

A novel pathway for alternative splicing: identification of an RNA intermediate that generates an alternative 5' splice donor site not present in the primary transcript of AMPD1.

Mineo¹,

Clarke²,

Sabina³

et al. 1990

Mol. Cell. Biol.

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AMP deaminase (AMPD) is a central enzyme in eucaryotic energy metabolism, and tissue-specific as well as stage-specific isoforms are found in many vertebrates. This study demonstrates the AMPDI gene product in rat is alternatively spliced. The second exon, a 12-base miniexon, was found to be excluded or included in a tissue-specific and stage-specific pattern. This AMP deaminase (AMP aminohydrolase; EC 3.5.4.6) (AMPD) activity has been found in all eucaryotic cells examined thus far, but it is not present in procaryotes, which suggests that this enzyme catalyzes a reaction that is important for energy metabolism in the specialized environment of the eucaryotic cell. Tissue-specific and stage-specific isoforms of AMPD have been reported in many vertebrates (14,22,23). In human and rats, two functional AMPD genes have been identified (16a). AMPDJ is expressed at high levels in skeletal muscle; AMPD2 is expressed in many nonmuscle tissues of the adult animal as well as in embryonic muscle, cardiac muscle, and smooth muscle. Two clinical phenotypes of inherited AMPD deficiency have been described in humans. Homozygous deficiency of AMPD activity restricted to erythrocytes has been estimated to have a frequency of -0.03% in Japanese, Chinese, and Koreans (21). Deficiency of AMPD restricted to skeletal muscle is a common cause of inherited metabolic myopathy in the United States and Europe (30), and the latter phenotype is presumably a consequence of mutations in the AMPDJ gene.Alternative splicing is used in many tissues, including skeletal muscle, to generate protein diversity (2). Prior studies suggest that more than one transcript may be produced from the AMPDJ gene in rat skeletal muscle. RNase mapping experiments performed with an AMPDI probe demonstrated the presence of two transcripts that have identical or closely related 5' and 3' termini, but the internal sequences of these transcripts diverge at one or more points (29). The study described here demonstrates that two mRNAs are produced from the rat AMPDJ gene and that the only difference between these two transcripts is the inclusion or exclusion of exon 2, a 12-base miniexon. The relative abundance of these two AMPD1 transcripts is regulated by tissue-specific and stage-specific signals. This pattern of alternative splicing exhibited by rat AMPDJ has been referred to as cassette splicing. It has been assumed in this type of splicing, the variably retained exon is removed as a part of a larger intron that contains the exon as well as both of the flanking introns (2). The study presented here demonstrates that this is not the only mechanism for cassette splicing. In the case of AMPDI, a novel pathway for alternative splicing has been identified. This pathway requires the formation of an RNA intermediate that generates a functional, alternative 5' splice donor site at the point where exon 1 is ligated to exon 2. The analogous RNA intermediate of the human AMPDI transcript generates a potential 5' splice donor site at the boundary of exon 1 and exon 2 that i...

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Complete deficiency of AMP deaminase in human erythrocytes

Cited by 43 publications

References 8 publications

A high performance liquid chromatographic assay for AMP‐deaminase activity in the erythrocytes of healthy subjects and patients with inherited purine disorders

A high performance liquid chromatographic assay for AMP‐deaminase activity in the erythrocytes of healthy subjects and patients with inherited purine disorders

AMP deaminase in rat brain: Localization in neurons and ependymal cells

A novel pathway for alternative splicing: identification of an RNA intermediate that generates an alternative 5' splice donor site not present in the primary transcript of AMPD1.

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