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Claus Oxvig

Localization of pregnancy-associated plasma protein-A and colocalization of pregnancy-associated plasma protein-A messenger ribonucleic acid and eosinophil granule major basic protein messenger ribonucleic acid in placenta

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  • M Bonno, Department of Immunology, Mayo Clinic, Rochester, Minnesota.
  • ,
  • Claus Oxvig
  • G M Kephart
  • ,
  • J M Wagner
  • ,
  • Torsten Kristensen
  • ,
  • L Sottrup-Jensen
  • G J Gleich
The human eosinophil granule major basic protein (MBP), a 13.8 kilodalton cationic polypeptide constituting the core of the eosinophil granule, is cytotoxic to parasites and numerous mammalian cells. Concentrations of a molecule immunochemically similar to eosinophil granule MBP are present in maternal plasma, and MBP mRNA has been localized to placental X cells by in situ hybridization. Eosinophil granule MBP is initially translated as a nontoxic precursor (proMBP), containing a 9.9 kilodalton acidic pro-portion that is believed to neutralize MBP toxicity. Recent analyses of sera from pregnant women have revealed that pregnancy-associated plasma protein-A (PAPP-A), previously thought to be a homotetramer of PAPP-A subunits, is actually composed of PAPP-A subunits bound by disulfide bonds to equimolar amounts of proMBP molecules to form a complex, PAPP-A/proMBP. In addition, the PAPP-A subunit nucleotide and deduced amino acid sequence have been determined from cloned cDNA. The PAPP-A monomer found in plasma contains 1547 amino acid residues.
Original languageEnglish
JournalLaboratory Investigation
Pages (from-to)560-566
Number of pages7
Publication statusPublished - Oct 1994

    Research areas

  • Blood Proteins, Eosinophil Granule Proteins, Female, Fluorescent Antibody Technique, Humans, Immunohistochemistry, In Situ Hybridization, Placenta, Pregnancy, Pregnancy-Associated Plasma Protein-A, RNA, Messenger, Ribonucleases

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