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a Department of Molecular and Structural Biology, University of Aarhus, 8000 Aarhus C, Denmark
b Department of Clinical Biochemistry, Statens Serum Institut, 2300 Copenhagen S, Denmark
c Endocrine Research Unit, Mayo Clinic, Rochester, Minnesota 55905
d Department of Immunology and Medicine, Mayo Clinic, Rochester, Minnesota 55905
PAPP-A/proMBP, the complex of pregnancy-associated plasma protein-A (PAPP-A) and the proform of eosinophil major basic protein (proMBP), circulates at increasing levels during pregnancy. The major site of synthesis is the placenta, in which PAPP-A mRNA has been localized to the syncytiotrophoblast and the placental X cells, whereas proMBP mRNA has been localized to the placental X cells only. The function of PAPP-A/proMBP and its components has remained speculative for years. Recently, however, it has been shown that PAPP-A specifically cleaves insulin-like growth factor (IGF) binding protein-4 in an IGF-dependent manner. Female reproductive and nonreproductive tissues have previously been reported to contain PAPP-A immunoreactivity, based on studies using preparations of anti(PAPP-A/proMBP), now known to recognize both PAPP-A and proMBP, and other irrelevant antigens. To analyze for the presence of PAPP-A and proMBP mRNA, a sensitive semiquantitative reverse transcription (RT) polymerase chain reaction (PCR) method was developed. Reverse-transcribed poly(A)+ RNA was used as a template in a competitive PCR. PAPP-A and proMBP mRNA levels were normalized against the level of ß-actin mRNA. Both mRNA species were significantly more abundant in term placenta than in other tissues analyzed. All analyzed tissues, including endometrium, myometrium, colon, and kidney, contained both PAPP-A and proMBP mRNA.
2 Correspondence: Lars Sottrup-Jensen, Department of Molecular and Structural Biology, University of Aarhus, Gustav Wieds Vej 10C, 8000 Aarhus C, Denmark. FAX: 45 8612 3178; lsj{at}mbio.aau.dk
3 Current address: M&E Biotech A/S, Kogle Allé 6, 2970 Hørsholm, Denmark.
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