Literature DB >> 7809065

Hereditary eosinophil peroxidase deficiency: immunochemical and spectroscopic studies and evidence for a compound heterozygosity of the defect.

M Romano1, P Patriarca, C Melo, F E Baralle, P Dri.   

Abstract

Hereditary eosinophil peroxidase (EPO; EC 1.11.1.7) deficiency is a rare abnormality of eosinophil granulocytes characterized by decreased or absent peroxidase activity and decreased volume of the granule matrix. The molecular basis of the defect is not known. We report here its molecular characterization in an EPO-deficient subject and his family members. The EPO-deficient eosinophils contained EPO-related material as determined immunochemically using either monoclonal or polyclonal anti-EPO antibodies but had no spectroscopic evidence of EPO. Eosinophil precursors from the EPO-deficient subject contained normally sized EPO mRNA, which was reverse transcribed into the corresponding cDNA clones encompassing the whole gene. Sequencing of these clones disclosed two mutations, a G-->A transition causing a nonconservative replacement of an arginine residue with a histidine and an insertion causing a shift in the reading frame with the appearance of a premature stop codon. The two mutations were located on different chromosomes indicating a compound heterozygosity for the defect. Both the son and the daughter of the proband inherited the G-->A transition, and their eosinophils contained a peroxidase activity intermediate between that of control subjects and the proband, suggesting that the transition is a deficiency-causing mutation. Eosinophil precursors from the EPO-deficient subject were found to actively synthesize an EPO that was apparently normal in terms of cytochemical reaction for peroxidase and immunoreactivity with monoclonal and polyclonal anti-EPO antibodies, but spectroscopically abnormal. The cytochemical reaction for peroxidase tended to decrease or disappear in the eosinophil precursors of the EPO-deficient subject but not of a normal subject as differentiation went on, suggesting that the Arg-->His substitution causes the production of an unstable EPO that undergoes progressive degradation as the cells mature.

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Year:  1994        PMID: 7809065      PMCID: PMC45465          DOI: 10.1073/pnas.91.26.12496

Source DB:  PubMed          Journal:  Proc Natl Acad Sci U S A        ISSN: 0027-8424            Impact factor:   11.205


  23 in total

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Journal:  Acta Haematol       Date:  1984       Impact factor: 2.195

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Journal:  Acta Haematol       Date:  1970       Impact factor: 2.195

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Authors:  Y Ohno; J I Gallin
Journal:  J Biol Chem       Date:  1985-07-15       Impact factor: 5.157

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Journal:  Proteins       Date:  1988

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Journal:  Blood       Date:  1982-08       Impact factor: 22.113

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Authors:  A W Segal; R Garcia; H Goldstone; A R Cross; O T Jones
Journal:  Biochem J       Date:  1981-04-15       Impact factor: 3.857

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Journal:  Biochem J       Date:  1983-03-01       Impact factor: 3.857

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Journal:  Blood       Date:  1985-02       Impact factor: 22.113

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  1 in total

1.  Impact of eosinophil-peroxidase (EPX) deficiency on eosinophil structure and function in mouse airways.

Authors:  Caroline M Percopo; Julia O Krumholz; Elizabeth R Fischer; Laura S Kraemer; Michelle Ma; Karen Laky; Helene F Rosenberg
Journal:  J Leukoc Biol       Date:  2018-10-04       Impact factor: 4.962

  1 in total

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