Covalent interaction between proform of eosinophil major basic protein (proMBP) and pregnancy-associated plasma protein-A (PAPP-A) is a cell-mediated event and required for proMBP inhibition of the catalytic activity of PAPP-A

Arun S. Sivanandam, Subburaman Mohan, Sanjay Kapur, Hirohito Kita, K. H.William Lau, Gyorgy Bagi, David J. Baylink, Xuezhong Qin

Research output: Contribution to journalArticle

10 Scopus citations

Abstract

This study was undertaken to determine the mechanism by which proform of eosinophil major basic protein (proMBP) inhibits the IGFBP-4 proteolytic activity of pregnancy-associated plasma protein (PAPP)-A. Co-overexpression of PAPP-A with proMBP in 293T cells, or co-incubation of 293T cells, respectively, overexpressing proMBP and PAPP-A resulted in the formation of a covalent proMBP-PAPP-A complex and inhibition of IGFBP-4 proteolysis. Similar results were obtained when recombinant proMBP and PAPP-A were incubated in the presence of U2 osteosarcoma cells or when recombinant proMBP was added to the U2 cells overexpressing PAPP-A. In contrast, no formation of covalent proMBP-PAPP-A complex or inhibition of IGFBP-4 proteolysis was observed when recombinant proMBP and PAPP-A were incubated under cell-free conditions, although proMBP was able to interact with PAPP-A in a non-covalent manner. These new findings suggest that formation of covalent proMBP-PAPP-A complex is a cell-mediated event and is required for proMBP to inhibit the catalytic activity of PAPP-A.

Original languageEnglish (US)
Pages (from-to)343-350
Number of pages8
JournalArchives of Biochemistry and Biophysics
Volume423
Issue number2
DOIs
StatePublished - Mar 15 2004

Keywords

  • Covalent interaction
  • IGFBP-4
  • PAPP-A
  • Protease
  • proMBP

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

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