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Claus Oxvig

Amino acid sequence of human pregnancy-associated plasma protein-A derived from cloned cDNA

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The amino acid sequence of human pregnancy-associated plasma protein-A (PAPP-A), a component of the circulating complex with the proform of eosinophil major basic protein (proMBP), has been determined from partial protein sequencing and from sequencing of cloned cDNA. The PAPP-A monomer contains 1547 amino acid residues, but is derived from a larger precursor of placental origin. PAPP-A contains 82 Cys residues, which are all bridged, 14 putative sites for N-glycosylation, and 7 putative sites for attachment of glycosaminoglycan groups. The C-terminal part of PAPP-A contains 5 approximately 60-residue motifs related to the short consensus repeats of complement proteins and selectins. The SCRs presently known can be grouped into three classes: complement-type, class I; selectin-type, class II; PAPP-A-type, class III. PAPP-A further contains three approximately 26-residue motifs, related to the lin-notch motifs of proteins regulating early tissue differentiation, and, in addition, a putative Zn2+ binding site similar to that found in many metalloproteinases has been identified. Apart from these features, the PAPP-A sequence is not related to other known protein sequences.
Original languageEnglish
JournalBiochemistry
Volume33
Issue6
Pages (from-to)1592-8
Number of pages7
ISSN0006-2960
DOIs
Publication statusPublished - 15 Feb 1994

    Research areas

  • Amino Acid Sequence, Base Sequence, Binding Sites, Blotting, Northern, Cloning, Molecular, Codon, Consensus Sequence, DNA, Complementary, Female, Glycosylation, Humans, Molecular Sequence Data, Pregnancy, Pregnancy-Associated Plasma Protein-A, RNA, Messenger, Repetitive Sequences, Nucleic Acid, Tissue Distribution, Zinc

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